ID   ID1_HUMAN               Reviewed;         155 AA.
AC   P41134; A8K537; E1P5L4; O00651; O00652; Q16371; Q16377; Q5TE66; Q5TE67;
AC   Q969Z7; Q9H0Z5; Q9H109;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 3.
DT   02-SEP-2026, entry version 234.
DE   RecName: Full=DNA-binding protein inhibitor ID-1;
DE   AltName: Full=Class B basic helix-loop-helix protein 24;
DE            Short=bHLHb24;
DE   AltName: Full=Inhibitor of DNA binding 1;
DE   AltName: Full=Inhibitor of differentiation 1;
GN   Name=ID1; Synonyms=BHLHB24, ID;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ID-A).
RC   TISSUE=Placenta;
RX   PubMed=8086456; DOI=10.1016/0167-4781(94)90261-5;
RA   Deed R.W., Jasiok M., Norton J.D.;
RT   "Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1
RT   protein: identification of functionally conserved residues common to Id
RT   proteins.";
RL   Biochim. Biophys. Acta 1219:160-162(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ID-A AND ID-B).
RC   TISSUE=Lung;
RX   PubMed=8294468; DOI=10.1016/s0021-9258(17)42146-6;
RA   Hara E., Yamaguchi T., Nojima H., Ide T., Campisi J., Okayama H., Oda K.;
RT   "Id-related genes encoding helix-loop-helix proteins are required for G1
RT   progression and are repressed in senescent human fibroblasts.";
RL   J. Biol. Chem. 269:2139-2145(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ID-A AND ID-B).
RX   PubMed=7637581; DOI=10.1016/0169-328x(95)00017-m;
RA   Zhu W., Dahmen J., Bulfone A., Rigolet M., Hernandez M.-C., Kuo W.L.,
RA   Puelles L., Rubenstein J.L.R., Israel M.A.;
RT   "Id gene expression during development and molecular cloning of the human
RT   Id-1 gene.";
RL   Brain Res. Mol. Brain Res. 30:312-326(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=9070860; DOI=10.1006/bbrc.1997.6152;
RA   Nehlin J.O., Hara E., Kuo W.L., Collins C., Campisi J.;
RT   "Genomic organization, sequence, and chromosomal localization of the human
RT   helix-loop-helix Id1 gene.";
RL   Biochem. Biophys. Res. Commun. 231:628-634(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ID-A).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ID-A).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ID-A).
RC   TISSUE=Ovary, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   INTERACTION WITH CLOCK AND BMAL1.
RX   PubMed=20861012; DOI=10.1074/jbc.m110.175182;
RA   Ward S.M., Fernando S.J., Hou T.Y., Duffield G.E.;
RT   "The transcriptional repressor ID2 can interact with the canonical clock
RT   components CLOCK and BMAL1 and mediate inhibitory effects on mPer1
RT   expression.";
RL   J. Biol. Chem. 285:38987-39000(2010).
CC   -!- FUNCTION: Transcriptional regulator (lacking a basic DNA binding
CC       domain) which negatively regulates the basic helix-loop-helix (bHLH)
CC       transcription factors by forming heterodimers and inhibiting their DNA
CC       binding and transcriptional activity. Implicated in regulating a
CC       variety of cellular processes, including cellular growth, senescence,
CC       differentiation, apoptosis, angiogenesis, and neoplastic
CC       transformation. Inhibits skeletal muscle and cardiac myocyte
CC       differentiation. Regulates the circadian clock by repressing the
CC       transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with other HLH proteins. Interacts with COPS5,
CC       IFI204, GATA4 and NKX2-5 (By similarity). Interacts with CLOCK and
CC       BMAL1. {ECO:0000250, ECO:0000269|PubMed:20861012}.
CC   -!- INTERACTION:
CC       P41134; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-1215527, EBI-12108222;
CC       P41134; O14936: CASK; NbExp=3; IntAct=EBI-1215527, EBI-1215506;
CC       P41134; Q03135: CAV1; NbExp=6; IntAct=EBI-1215527, EBI-603614;
CC       P41134; P28329-3: CHAT; NbExp=3; IntAct=EBI-1215527, EBI-25837549;
CC       P41134; P22607: FGFR3; NbExp=3; IntAct=EBI-1215527, EBI-348399;
CC       P41134; P06396: GSN; NbExp=3; IntAct=EBI-1215527, EBI-351506;
CC       P41134; A6NI15: MSGN1; NbExp=5; IntAct=EBI-1215527, EBI-11991020;
CC       P41134; P13349: MYF5; NbExp=5; IntAct=EBI-1215527, EBI-17491620;
CC       P41134; P15173: MYOG; NbExp=4; IntAct=EBI-1215527, EBI-3906629;
CC       P41134; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1215527, EBI-5235340;
CC       P41134; Q99081: TCF12; NbExp=3; IntAct=EBI-1215527, EBI-722877;
CC       P41134; Q99081-3: TCF12; NbExp=3; IntAct=EBI-1215527, EBI-11952764;
CC       P41134; P15923-3: TCF3; NbExp=3; IntAct=EBI-1215527, EBI-12000326;
CC       P41134; P15884: TCF4; NbExp=4; IntAct=EBI-1215527, EBI-533224;
CC       P41134; P15884-3: TCF4; NbExp=3; IntAct=EBI-1215527, EBI-13636688;
CC       P41134; Q9Y649; NbExp=3; IntAct=EBI-1215527, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=ID-A;
CC         IsoId=P41134-1; Sequence=Displayed;
CC       Name=ID-B;
CC         IsoId=P41134-2; Sequence=VSP_002108;
CC   -!- DEVELOPMENTAL STAGE: Expression correlates with proliferation in some
CC       types of cells.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/40914/ID1";
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DR   EMBL; X77956; CAA54920.1; -; mRNA.
DR   EMBL; D13889; BAA02988.1; -; mRNA.
DR   EMBL; D13890; BAA02989.1; -; mRNA.
DR   EMBL; S78986; AAB35037.1; -; mRNA.
DR   EMBL; S78825; AAB35038.1; -; mRNA.
DR   EMBL; U57645; AAC13882.1; -; Genomic_DNA.
DR   EMBL; U57645; AAC13883.1; -; Genomic_DNA.
DR   EMBL; BT007443; AAP36111.1; -; mRNA.
DR   EMBL; AK291152; BAF83841.1; -; mRNA.
DR   EMBL; AL110115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL117381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76432.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76434.1; -; Genomic_DNA.
DR   EMBL; BC000613; AAH00613.1; -; mRNA.
DR   EMBL; BC012420; AAH12420.1; -; mRNA.
DR   CCDS; CCDS13185.1; -. [P41134-1]
DR   CCDS; CCDS13186.1; -. [P41134-2]
DR   PIR; A49727; A49727.
DR   PIR; B49727; B49727.
DR   PIR; JC5395; JC5395.
DR   PIR; JC5396; JC5396.
DR   PIR; S47524; S47524.
DR   RefSeq; NP_002156.2; NM_002165.4. [P41134-1]
DR   RefSeq; NP_851998.1; NM_181353.3. [P41134-2]
DR   AlphaFoldDB; P41134; -.
DR   SMR; P41134; -.
DR   BioGRID; 109623; 67.
DR   DIP; DIP-38112N; -.
DR   FunCoup; P41134; 1895.
DR   IntAct; P41134; 45.
DR   MINT; P41134; -.
DR   NDEx; IQUERY-CP-ID1; 11 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000365280; -.
DR   ChEMBL; CHEMBL1075116; -.
DR   iPTMnet; P41134; -.
DR   PhosphoSitePlus; P41134; -.
DR   BioMuta; ID1; -.
DR   DMDM; 21264450; -.
DR   jPOST; P41134; -.
DR   MassIVE; P41134; -.
DR   PaxDb; 9606-ENSP00000365280; -.
DR   PeptideAtlas; P41134; -.
DR   ProteomicsDB; 55400; -. [P41134-1]
DR   ProteomicsDB; 55401; -. [P41134-2]
DR   Pumba; P41134; -.
DR   Antibodypedia; 25205; 421 antibodies from 39 providers.
DR   DNASU; 3397; -.
DR   Ensembl; ENST00000376105.4; ENSP00000365273.3; ENSG00000125968.11. [P41134-2]
DR   Ensembl; ENST00000376112.4; ENSP00000365280.3; ENSG00000125968.11. [P41134-1]
DR   Ensembl; ENST00000718307.1; ENSP00000520744.1; ENSG00000125968.11. [P41134-1]
DR   Ensembl; ENST00000718308.1; ENSP00000520745.1; ENSG00000125968.11. [P41134-1]
DR   Ensembl; ENST00000903277.1; ENSP00000573336.1; ENSG00000125968.11. [P41134-1]
DR   Ensembl; ENST00000903278.1; ENSP00000573337.1; ENSG00000125968.11. [P41134-1]
DR   Ensembl; ENST00000903279.1; ENSP00000573338.1; ENSG00000125968.11. [P41134-1]
DR   Ensembl; ENST00000972141.1; ENSP00000642200.1; ENSG00000125968.11. [P41134-1]
DR   GeneID; 3397; -.
DR   KEGG; hsa:3397; -.
DR   MANE-Select; ENST00000376112.4; ENSP00000365280.3; NM_002165.4; NP_002156.2.
DR   UCSC; uc002wwg.3; human. [P41134-1]
DR   AGR; HGNC:5360; -.
DR   ClinPGx; PA29608; -.
DR   CTD; 3397; -.
DR   DisGeNET; 3397; -.
DR   GeneCards; ID1; -.
DR   HGNC; HGNC:5360; ID1.
DR   HPA; ENSG00000125968; Low tissue specificity.
DR   MIM; 600349; gene.
DR   OpenTargets; ENSG00000125968; -.
DR   VEuPathDB; HostDB:ENSG00000125968; -.
DR   eggNOG; ENOG502RZP5; Eukaryota.
DR   GeneTree; ENSGT00940000161109; -.
DR   HOGENOM; CLU_116790_0_0_1; -.
DR   InParanoid; P41134; -.
DR   OMA; LDMKGCY; -.
DR   OrthoDB; 10047910at2759; -.
DR   PAN-GO; P41134; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P41134; -.
DR   PathwayCommons; P41134; -.
DR   Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR   Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR   Reactome; R-HSA-9856649; Transcriptional and post-translational regulation of MITF-M expression and activity.
DR   SignaLink; P41134; -.
DR   SIGNOR; P41134; -.
DR   Agora; ENSG00000125968; -.
DR   BioGRID-ORCS; 3397; 31 hits in 1174 CRISPR screens.
DR   CD-CODE; 8C2F96ED; Centrosome.
DR   ChiTaRS; ID1; human.
DR   GeneWiki; ID1; -.
DR   GenomeRNAi; 3397; -.
DR   Pharos; P41134; Tbio.
DR   PRO; PR:P41134; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P41134; protein.
DR   Bgee; ENSG00000125968; Expressed in seminal vesicle and 196 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ARUK-UCL.
DR   GO; GO:0001525; P:angiogenesis; TAS:BHF-UCL.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; TAS:BHF-UCL.
DR   GO; GO:0048514; P:blood vessel morphogenesis; TAS:BHF-UCL.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:GDB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:BHF-UCL.
DR   CDD; cd19691; bHLH_dnHLH_ID1; 1.
DR   FunFam; 4.10.280.10:FF:000039; DNA-binding protein inhibitor ID-3; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; DNA-BINDING PROTEIN INHIBITOR; 1.
DR   PANTHER; PTHR11723:SF4; DNA-BINDING PROTEIN INHIBITOR ID-1; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Biological rhythms; Cytoplasm; Developmental protein;
KW   Nucleus; Proteomics identification; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..155
FT                   /note="DNA-binding protein inhibitor ID-1"
FT                   /id="PRO_0000127236"
FT   DOMAIN          53..105
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   MOTIF           98..111
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         143..155
FT                   /note="AACVPADDRILCR -> VRSRSDH (in isoform ID-B)"
FT                   /evidence="ECO:0000303|PubMed:7637581,
FT                   ECO:0000303|PubMed:8294468"
FT                   /id="VSP_002108"
FT   VARIANT         63
FT                   /note="N -> D (in dbSNP:rs1802548)"
FT                   /id="VAR_049544"
FT   CONFLICT        16
FT                   /note="S -> T (in Ref. 2; BAA02988/BAA02989)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="A -> R (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="Missing (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  16133 MW;  480287384B667161 CRC64;
     MKVASGSTAT AAAGPSCALK AGKTASGAGE VVRCLSEQSV AISRCAGGAG ARLPALLDEQ
     QVNVLLYDMN GCYSRLKELV PTLPQNRKVS KVEILQHVID YIRDLQLELN SESEVGTPGG
     RGLPVRAPLS TLNGEISALT AEAACVPADD RILCR
//
ID   EHD2_ORYSJ              Reviewed;         475 AA.
AC   B1B534; A3C4T1; Q7XEJ8;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Protein EARLY HEADING DATE 2 {ECO:0000303|PubMed:18790997};
DE            Short=Ehd2 {ECO:0000303|PubMed:18790997};
DE   AltName: Full=Protein RICE INDETERMINATE 1 {ECO:0000303|PubMed:18725639};
DE            Short=OsID {ECO:0000303|PubMed:16784536};
DE            Short=OsID1 {ECO:0000303|PubMed:18774969};
GN   Name=EHD2 {ECO:0000303|PubMed:18790997};
GN   Synonyms=GHD10 {ECO:0000303|PubMed:24280027}, ID
GN   {ECO:0000303|PubMed:16784536}, ID1 {ECO:0000303|PubMed:18774969}, RID1
GN   {ECO:0000303|PubMed:18725639};
GN   OrderedLocusNames=Os10g0419200 {ECO:0000312|EMBL:BAT10873.1},
GN   LOC_Os10g28330 {ECO:0000305};
GN   ORFNames=OSNPB_100419200 {ECO:0000312|EMBL:BAT10873.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Tohoku IL9;
RX   PubMed=18790997; DOI=10.1104/pp.108.125542;
RA   Matsubara K., Yamanouchi U., Wang Z.-X., Minobe Y., Izawa T., Yano M.;
RT   "Ehd2, a rice ortholog of the maize INDETERMINATE1 gene, promotes flowering
RT   by up-regulating Ehd1.";
RL   Plant Physiol. 148:1425-1435(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Zhonghua 11;
RX   PubMed=18725639; DOI=10.1073/pnas.0806019105;
RA   Wu C., You C., Li C., Long T., Chen G., Byrne M.E., Zhang Q.;
RT   "RID1, encoding a Cys2/His2-type zinc finger transcription factor, acts as
RT   a master switch from vegetative to floral development in rice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:12915-12920(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16784536; DOI=10.1186/1471-2164-7-158;
RA   Colasanti J., Tremblay R., Wong A.Y., Coneva V., Kozaki A., Mable B.K.;
RT   "The maize INDETERMINATE1 flowering time regulator defines a highly
RT   conserved zinc finger protein family in higher plants.";
RL   BMC Genomics 7:158-158(2006).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=18774969; DOI=10.1111/j.1365-313x.2008.03667.x;
RA   Park S.J., Kim S.L., Lee S., Je B.I., Piao H.L., Park S.H., Kim C.M.,
RA   Ryu C.-H., Park S.H., Xuan Y.H., Colasanti J., An G., Han C.D.;
RT   "Rice Indeterminate 1 (OsId1) is necessary for the expression of Ehd1
RT   (Early heading date 1) regardless of photoperiod.";
RL   Plant J. 56:1018-1029(2008).
RN   [10]
RP   REVIEW ON FLOWERING.
RX   PubMed=19304997; DOI=10.1093/aob/mcp063;
RA   Greenup A., Peacock W.J., Dennis E.S., Trevaskis B.;
RT   "The molecular biology of seasonal flowering-responses in Arabidopsis and
RT   the cereals.";
RL   Ann. Bot. 103:1165-1172(2009).
RN   [11]
RP   FUNCTION, MUTAGENESIS OF PRO-158, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Wuyunjing 7;
RX   PubMed=24280027; DOI=10.1186/1939-8433-6-24;
RA   Hu S., Dong G., Xu J., Su Y., Shi Z., Ye W., Li Y., Li G., Zhang B., Hu J.,
RA   Qian Q., Zeng D., Guo L.;
RT   "A point mutation in the zinc finger motif of RID1/EHD2/OsID1 protein leads
RT   to outstanding yield-related traits in japonica rice variety Wuyunjing 7.";
RL   Rice 6:24-24(2013).
RN   [12]
RP   REPRESSION BY DLF1.
RX   PubMed=25036785; DOI=10.1371/journal.pone.0102529;
RA   Cai Y., Chen X., Xie K., Xing Q., Wu Y., Li J., Du C., Sun Z., Guo Z.;
RT   "Dlf1, a WRKY transcription factor, is involved in the control of flowering
RT   time and plant height in rice.";
RL   PLoS ONE 9:E102529-E102529(2014).
RN   [13]
RP   INDUCTION BY FKF1.
RX   PubMed=25850808; DOI=10.1111/pce.12549;
RA   Han S.-H., Yoo S.-C., Lee B.-D., An G., Paek N.-C.;
RT   "Rice FLAVIN-BINDING, KELCH REPEAT, F-BOX 1 (OsFKF1) promotes flowering
RT   independent of photoperiod.";
RL   Plant Cell Environ. 38:2527-2540(2015).
RN   [14]
RP   REGULATION BY PHYTOCHROME.
RX   PubMed=25573482; DOI=10.1038/srep07709;
RA   Yoshitake Y., Yokoo T., Saito H., Tsukiyama T., Quan X., Zikihara K.,
RA   Katsura H., Tokutomi S., Aboshi T., Mori N., Inoue H., Nishida H.,
RA   Kohchi T., Teraishi M., Okumoto Y., Tanisaka T.;
RT   "The effects of phytochrome-mediated light signals on the developmental
RT   acquisition of photoperiod sensitivity in rice.";
RL   Sci. Rep. 5:7709-7709(2015).
RN   [15]
RP   REVIEW ON FLOWERING.
RX   PubMed=28491078; DOI=10.3389/fpls.2017.00665;
RA   Brambilla V., Gomez-Ariza J., Cerise M., Fornara F.;
RT   "The importance of being on time: Regulatory networks controlling
RT   photoperiodic flowering in cereals.";
RL   Front. Plant Sci. 8:665-665(2017).
CC   -!- FUNCTION: Transcription activator that acts as a flowering master
CC       switch in both long and short days, independently of the circadian
CC       clock (PubMed:18725639, PubMed:18774969, PubMed:18790997,
CC       PubMed:19304997, PubMed:24280027). Promotes flowering upstream of HD1
CC       by up-regulating FTL1, FTL4, FTL5, FTL6, EHD1, HD3A and RFT1
CC       (PubMed:18725639, PubMed:18774969, PubMed:18790997). Seems to repress
CC       FTL11 expression (PubMed:18725639). May recognize the consensus motif
CC       5'-TTTGTCGTAAT-3' in target gene promoters (PubMed:18725639).
CC       {ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969,
CC       ECO:0000269|PubMed:18790997, ECO:0000269|PubMed:24280027,
CC       ECO:0000303|PubMed:19304997}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC       ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969,
CC       ECO:0000269|PubMed:24280027}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in developing leaves (more in
CC       sheaths than in blades, especially in the outer epidermal cell of
CC       immature leaves and in the region immediately beneath the meristem
CC       where internodes are visible) and panicles, and, at very low levels,
CC       around the shoot apex and in roots. {ECO:0000269|PubMed:18725639,
CC       ECO:0000269|PubMed:18774969, ECO:0000269|PubMed:18790997,
CC       ECO:0000269|PubMed:24280027}.
CC   -!- DEVELOPMENTAL STAGE: Detected in young expanded leaves emerging from
CC       the culms (PubMed:18774969). In young panicles, accumulates in
CC       spikelets and panicle branches (PubMed:18774969). Under short days
CC       (SD), observed in leaves by 1 week after germination and reaches a peak
CC       by 2 weeks. Subsequently, the level gradually decreases, but maintains
CC       at low levels even after flowering (about 9 weeks) (PubMed:18790997).
CC       Under long days (LD), present in leaves at low levels during all
CC       developmental stages from at least 1 week after germination
CC       (PubMed:18790997). {ECO:0000269|PubMed:18774969,
CC       ECO:0000269|PubMed:18790997}.
CC   -!- INDUCTION: Induced by FKF1 (PubMed:25850808). Down-regulated by DLF1
CC       (PubMed:25036785). During the basic vegetative growth phase (BVP,
CC       photoperiod-insensitive phase), suppressed via phytochrome-mediated
CC       light signals involving the phytochromobilin synthase HY2
CC       (PubMed:25573482). {ECO:0000269|PubMed:25036785,
CC       ECO:0000269|PubMed:25573482, ECO:0000269|PubMed:25850808}.
CC   -!- DISRUPTION PHENOTYPE: Never-flowering phenotype in the rid1 mutant
CC       (PubMed:18725639). Extremely delayed flowering under both short- (SD)
CC       and long-day (LD) conditions, associated with reduced EHD1, HD3A and
CC       RFT1 levels, but increased leaves and nodes production
CC       (PubMed:18725639, PubMed:18774969, PubMed:18790997). Levels of FTL1 and
CC       FTL4 are slightly reduced under both LD and SD, expression of FTL5 is
CC       down-regulated under LD, whereas FTL6 is down-regulated only under SD
CC       (PubMed:18725639). In contrast, the accumulation of FTL11 is slightly
CC       higher under both SD and LD (PubMed:18725639). Reduced levels of MADS1,
CC       MADS14 and MADS15, downstream genes of EHD1 (PubMed:18774969).
CC       {ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969,
CC       ECO:0000269|PubMed:18790997}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP53791.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF26530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAZ16094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAZ16094.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB359195; BAG12102.1; -; Genomic_DNA.
DR   EMBL; AB359196; BAG12103.1; -; mRNA.
DR   EMBL; FJ009578; ACH87394.1; -; mRNA.
DR   EMBL; FJ009579; ACH87395.1; -; Genomic_DNA.
DR   EMBL; DP000086; AAP53791.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008216; BAF26530.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014966; BAT10873.1; -; Genomic_DNA.
DR   EMBL; CM000147; EAZ16094.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B1B534; -.
DR   FunCoup; B1B534; 743.
DR   STRING; 39947.B1B534; -.
DR   PaxDb; 39947-B1B534; -.
DR   EnsemblPlants; Os10t0419200-01; Os10t0419200-01; Os10g0419200.
DR   Gramene; Os10t0419200-01; Os10t0419200-01; Os10g0419200.
DR   KEGG; dosa:Os10g0419200; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_014578_4_2_1; -.
DR   InParanoid; B1B534; -.
DR   OMA; ATTVACC; -.
DR   OrthoDB; 6354171at2759; -.
DR   PlantReactome; R-OSA-9928995; Drought escape (DE) via ABA-dependent pathway.
DR   Proteomes; UP000059680; Chromosome 10.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR   GO; GO:0048575; P:short-day photoperiodism, flowering; IMP:UniProtKB.
DR   FunFam; 3.30.160.60:FF:000554; protein indeterminate-domain 12-like; 1.
DR   FunFam; 3.30.160.60:FF:000131; protein indeterminate-domain 5, chloroplastic-like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   InterPro; IPR055187; C2CH-3rd_BIRD-IDD.
DR   InterPro; IPR055185; C2CH-4th_BIRD-IDD.
DR   InterPro; IPR055186; C2H2-2nd_BIRD-IDD.
DR   InterPro; IPR031140; IDD1-16.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR10593:SF136; PROTEIN INDETERMINATE-DOMAIN 12; 1.
DR   PANTHER; PTHR10593; SERINE/THREONINE-PROTEIN KINASE RIO; 1.
DR   Pfam; PF22995; C2CH-3rd_BIRD-IDD; 1.
DR   Pfam; PF22992; C2CH-4th_BIRD-IDD; 1.
DR   Pfam; PF22996; C2H2-2nd_BIRD-IDD; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..475
FT                   /note="Protein EARLY HEADING DATE 2"
FT                   /id="PRO_0000447325"
FT   ZN_FING         105..127
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         155..185
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   ZN_FING         190..213
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         217..240
FT                   /note="CCHC-type 2; atypical"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..239
FT                   /note="SHR-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   MOTIF           123..130
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           177..184
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         221
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q700D2"
FT   MUTAGEN         158
FT                   /note="P->L: In ghd10; delayed flowering time, tall stalks
FT                   and increased panicle length and primary branch number,
FT                   thus leading to increased grains yield. Reduced expression
FT                   of EHD1, HD1, RFT1, HD3A and MADS15 under both short-days
FT                   (SD) and long-days (LD) conditions."
FT                   /evidence="ECO:0000269|PubMed:24280027"
SQ   SEQUENCE   475 AA;  50672 MW;  107CE5B7004BF4A1 CRC64;
     MLLSDLSSDQ EATGSNSHGG GGGDRMVVGS HGAAHVVLSN LFLPPAAAAA ATMLLPAAPV
     MVRPAAMAAA QEPRAKKKRS LPGNPDPEAE VIALSPRALV ATNRFVCEVC NKGFQRDQNL
     QLHRRGHNLP WKLRHRAAAV SAVTTAAPAP RKRVYVCPEP TCVHHDPARA LGDLTGIKKH
     FSRKHGEKRW RCERCGKRYA VHSDWKAHVK NCGTREYRCD CGILFSRKDS LLTHRAFCDA
     LAEESARLLA AANNSSSITT TTCNNSNISS NNNNNNINSI SNSNNLLITS SSSSPPLFLP
     FSTTPAENPN PNQLLFLQQH QAAHHQLLLP QFQQPPSSPP AYFDHLAFGG GGGVITGSSC
     NDDNSSIAGD VMVAAGGDSV SFGLTSEGSV TMHAGDVGRR RLTRDFLGVD HDAGEVDELE
     LDELPADLST TAAACQGCNF AAATTAACCA TDFTTGSRQY LGRLPPVNET WSHNF
//
ID   ID1_MOUSE               Reviewed;         168 AA.
AC   P20067; Q61101; Q9D897;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   02-SEP-2026, entry version 201.
DE   RecName: Full=DNA-binding protein inhibitor ID-1;
DE   AltName: Full=Inhibitor of DNA binding 1;
DE   AltName: Full=Inhibitor of differentiation 1;
GN   Name=Id1; Synonyms=Id, Id-1, Idb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX   PubMed=2156629; DOI=10.1016/0092-8674(90)90214-y;
RA   Benezra R., Davis R.L., Lockshon D., Turner D.L., Weintraub H.;
RT   "The protein Id: a negative regulator of helix-loop-helix DNA binding
RT   proteins.";
RL   Cell 61:49-59(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   STRAIN=Swiss albino; TISSUE=Brain;
RX   PubMed=8765747; DOI=10.1016/0167-4781(96)00092-9;
RA   Hernandez M.-C., Andres-Barquin P.J., Israel M.A.;
RT   "Molecular cloning of the cDNA encoding a helix-loop-helix protein, mouse
RT   ID1B: tissue-specific expression of ID1A and ID1B genes.";
RL   Biochim. Biophys. Acta 1308:28-30(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   INTERACTION WITH IFI204.
RX   PubMed=11940648; DOI=10.1128/mcb.22.9.2893-2905.2002;
RA   Liu C.-J., Ding B., Wang H., Lengyel P.;
RT   "The MyoD-inducible p204 protein overcomes the inhibition of myoblast
RT   differentiation by Id proteins.";
RL   Mol. Cell. Biol. 22:2893-2905(2002).
RN   [5]
RP   INTERACTION WITH COPS5.
RX   PubMed=15451666; DOI=10.1016/j.jmb.2004.08.043;
RA   Berse M., Bounpheng M., Huang X., Christy B., Pollmann C., Dubiel W.;
RT   "Ubiquitin-dependent degradation of Id1 and Id3 is mediated by the COP9
RT   signalosome.";
RL   J. Mol. Biol. 343:361-370(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX   PubMed=16516211; DOI=10.1016/j.febslet.2006.02.038;
RA   Makita J., Kurooka H., Mori K., Akagi Y., Yokota Y.;
RT   "Identification of the nuclear export signal in the helix-loop-helix
RT   inhibitor Id1.";
RL   FEBS Lett. 580:1812-1816(2006).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH GATA4 AND NKX2-5.
RX   PubMed=16556596; DOI=10.1074/jbc.m511748200;
RA   Ding B., Liu C.-J., Huang Y., Yu J., Kong W., Lengyel P.;
RT   "p204 protein overcomes the inhibition of the differentiation of P19 murine
RT   embryonal carcinoma cells to beating cardiac myocytes by Id proteins.";
RL   J. Biol. Chem. 281:14893-14906(2006).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=19217292; DOI=10.1016/j.cub.2008.12.052;
RA   Duffield G.E., Watson N.P., Mantani A., Peirson S.N., Robles-Murguia M.,
RA   Loros J.J., Israel M.A., Dunlap J.C.;
RT   "A role for Id2 in regulating photic entrainment of the mammalian circadian
RT   system.";
RL   Curr. Biol. 19:297-304(2009).
CC   -!- FUNCTION: Transcriptional regulator (lacking a basic DNA binding
CC       domain) which negatively regulates the basic helix-loop-helix (bHLH)
CC       transcription factors by forming heterodimers and inhibiting their DNA
CC       binding and transcriptional activity. Implicated in regulating a
CC       variety of cellular processes, including cellular growth, senescence,
CC       differentiation, apoptosis, angiogenesis, and neoplastic
CC       transformation. Inhibits skeletal muscle and cardiac myocyte
CC       differentiation. Regulates the circadian clock by repressing the
CC       transcriptional activator activity of the CLOCK-BMAL1 heterodimer.
CC       {ECO:0000269|PubMed:16556596, ECO:0000269|PubMed:19217292}.
CC   -!- SUBUNIT: Heterodimer with other HLH proteins. Interacts with CLOCK and
CC       BMAL1 (By similarity). Interacts with COPS5, IFI204, GATA4 and NKX2-5.
CC       {ECO:0000250, ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:15451666,
CC       ECO:0000269|PubMed:16556596}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16516211}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16516211}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=Long;
CC         IsoId=P20067-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P20067-2; Sequence=VSP_002109;
CC   -!- INDUCTION: Expressed in a circadian manner in the suprachiasmatic
CC       nucleus (SCN) of the brain and heart with peak levels seen between CT16
CC       and CT20 in the SCN and between CT8 and CT12 in the heart.
CC       {ECO:0000269|PubMed:19217292}.
CC   -!- PTM: Polyubiquitinated; which is favored by Ifi204 and leads to
CC       proteasomal degradation. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M31885; AAA37879.1; ALT_INIT; mRNA.
DR   EMBL; U43884; AAC52760.1; -; mRNA.
DR   EMBL; AK008264; BAB25564.1; -; mRNA.
DR   CCDS; CCDS16897.1; -. [P20067-2]
DR   CCDS; CCDS89567.1; -. [P20067-1]
DR   PIR; A34690; A34690.
DR   PIR; S72171; S72171.
DR   RefSeq; NP_034625.1; NM_010495.3. [P20067-2]
DR   PDB; 6MGM; X-ray; 1.79 A; A/B=52-104.
DR   PDB; 6MGN; X-ray; 1.90 A; B=58-104.
DR   PDB; 6U2U; X-ray; 1.50 A; A/B=59-104.
DR   AlphaFoldDB; P20067; -.
DR   SMR; P20067; -.
DR   FunCoup; P20067; 1258.
DR   IntAct; P20067; 3.
DR   MINT; P20067; -.
DR   STRING; 10090.ENSMUSP00000092019; -.
DR   iPTMnet; P20067; -.
DR   PhosphoSitePlus; P20067; -.
DR   PaxDb; 10090-ENSMUSP00000092019; -.
DR   ProteomicsDB; 267189; -. [P20067-1]
DR   ProteomicsDB; 267190; -. [P20067-2]
DR   Pumba; P20067; -.
DR   Antibodypedia; 25205; 421 antibodies from 39 providers.
DR   Ensembl; ENSMUST00000038368.9; ENSMUSP00000092019.5; ENSMUSG00000042745.10. [P20067-2]
DR   AGR; MGI:96396; -.
DR   MGI; MGI:96396; Id1.
DR   VEuPathDB; HostDB:ENSMUSG00000042745; -.
DR   eggNOG; ENOG502RZP5; Eukaryota.
DR   GeneTree; ENSGT00940000161109; -.
DR   HOGENOM; CLU_116790_0_0_1; -.
DR   InParanoid; P20067; -.
DR   OMA; LDMKGCY; -.
DR   PhylomeDB; P20067; -.
DR   Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR   PRO; PR:P20067; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P20067; protein.
DR   Bgee; ENSMUSG00000042745; Expressed in mucous cell of stomach and 364 other cell types or tissues.
DR   ExpressionAtlas; P20067; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; ISO:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR   GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0060426; P:lung vasculature development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:GO_Central.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0031648; P:protein destabilization; IDA:MGI.
DR   GO; GO:0045765; P:regulation of angiogenesis; IMP:MGI.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
DR   GO; GO:1901342; P:regulation of vasculature development; ISO:GO_Central.
DR   GO; GO:0046677; P:response to antibiotic; IMP:MGI.
DR   CDD; cd19691; bHLH_dnHLH_ID1; 1.
DR   FunFam; 4.10.280.10:FF:000039; DNA-binding protein inhibitor ID-3; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   IDEAL; IID50360; -.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; DNA-BINDING PROTEIN INHIBITOR; 1.
DR   PANTHER; PTHR11723:SF4; DNA-BINDING PROTEIN INHIBITOR ID-1; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   PDBsum; 6MGM; -.
DR   PDBsum; 6MGN; -.
DR   PDBsum; 6U2U; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Biological rhythms; Cytoplasm;
KW   Developmental protein; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..168
FT                   /note="DNA-binding protein inhibitor ID-1"
FT                   /id="PRO_0000127237"
FT   DOMAIN          46..98
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          53..106
FT                   /note="Interaction with IFI204"
FT                   /evidence="ECO:0000250"
FT   MOTIF           91..104
FT                   /note="Nuclear export signal"
FT   VAR_SEQ         136..168
FT                   /note="VRSESEYYIILQWETEATGGGCPPSLLFRRIAI -> AACVPADDRILCR
FT                   (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:2156629"
FT                   /id="VSP_002109"
FT   CONFLICT        140
FT                   /note="S -> A (in Ref. 3; BAB25564)"
FT                   /evidence="ECO:0000305"
FT   HELIX           62..72
FT                   /evidence="ECO:0007829|PDB:6U2U"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:6U2U"
FT   HELIX           84..102
FT                   /evidence="ECO:0007829|PDB:6U2U"
SQ   SEQUENCE   168 AA;  17914 MW;  7F7EF0177358F516 CRC64;
     MKVASGSAAA AAGPSCSLKA GRTAGEVVLG LSEQSVAISR CAGTRLPALL DEQQVNVLLY
     DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT TGGRGLPVRA
     PLSTLNGEIS ALAAEVRSES EYYIILQWET EATGGGCPPS LLFRRIAI
//
ID   A8U072_PETMA            Unreviewed;       105 AA.
AC   A8U072;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   02-SEP-2026, entry version 58.
DE   SubName: Full=Id {ECO:0000313|EMBL:ABW74716.1};
GN   Name=Id {ECO:0000313|EMBL:ABW74716.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|EMBL:ABW74716.1};
RN   [1] {ECO:0000313|EMBL:ABW74716.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14651928; DOI=10.1016/j.ydbio.2003.09.006;
RA   Meulemans D., McCauley D., Bronner-Fraser M.;
RT   "Id expression in amphioxus and lamprey highlights the role of gene
RT   cooption during neural crest evolution.";
RL   Dev. Biol. 264:430-442(2003).
RN   [2] {ECO:0000313|EMBL:ABW74716.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17765683; DOI=10.1016/j.devcel.2007.08.005;
RA   Sauka-Spengler T., Meulemans D., Jones M., Bronner-Fraser M.;
RT   "Ancient evolutionary origin of the neural crest gene regulatory network.";
RL   Dev. Cell 13:405-420(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00981}.
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DR   EMBL; EU089675; ABW74716.1; -; mRNA.
DR   AlphaFoldDB; A8U072; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IEA:TreeGrafter.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd19691; bHLH_dnHLH_ID1; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; DNA-BINDING PROTEIN INHIBITOR; 1.
DR   PANTHER; PTHR11723:SF17; PROTEIN EXTRA-MACROCHAETAE; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00981}; Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00981};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00981}.
FT   DOMAIN          17..70
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          31..70
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00981"
SQ   SEQUENCE   105 AA;  11400 MW;  7D927ACE52DDBB57 CRC64;
     MKAVSPVRSV HRQSAEAAAA VHRLAEERLL YDMKGCYSRL SQLVPTLANT GRKASRMEIL
     QHVIDYILDL QVALDEGPVE EGAPGDAQVC TDMASLTGNN ETLCC
//
ID   Q9EU69_STREE            Unreviewed;       453 AA.
AC   Q9EU69; G8JZU2; Q7D4E7;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   02-SEP-2026, entry version 134.
DE   SubName: Full=ABC transporter {ECO:0000313|EMBL:CAC18583.1, ECO:0000313|EMBL:VST69084.1};
DE   SubName: Full=BlpB protein {ECO:0000313|EMBL:CAC03518.1};
DE   SubName: Full=SpiD {ECO:0000313|EMBL:ABU67980.1};
GN   Name=iD {ECO:0000313|EMBL:CAC18583.1};
GN   Synonyms=blpB {ECO:0000313|EMBL:CAC03518.1}, lcnD
GN   {ECO:0000313|EMBL:VST69084.1};
GN   ORFNames=SAMEA3389245_01245 {ECO:0000313|EMBL:VST69084.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:CAC18583.1};
RN   [1] {ECO:0000313|EMBL:CAC03518.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KNR.7/87 {ECO:0000313|EMBL:CAC03518.1};
RA   de Saizieu A., Gardes C., Flint N., Wagner C., Kamber M., Mitchell T.J.,
RA   Keck W., Amrein K.E., Lange R.;
RT   "Microarray based identification of a novel Streptococcus pneumoniae
RT   regulon controlled by an autoinduced peptide.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAC18583.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KNR7/87 {ECO:0000313|EMBL:CAC18583.1};
RA   Reichmann P., Hakenbeck R.;
RT   "A Peptide Inducible Signal Transduction System in Streptococcus
RT   pneumoniae: Evidence for Bacteriocin Production.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABU67980.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=628 {ECO:0000313|EMBL:ABU68009.1}, and TIGR4
RC   {ECO:0000313|EMBL:ABU67980.1};
RX   PubMed=17704229; DOI=10.1128/JB.00474-07;
RA   Lux T., Nuhn M., Hakenbeck R., Reichmann P.;
RT   "Diversity of bacteriocins and activity spectrum in Streptococcus
RT   pneumoniae.";
RL   J. Bacteriol. 189:7741-7751(2007).
RN   [4] {ECO:0000313|EMBL:VST69084.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPSC535 {ECO:0000313|EMBL:VST69084.1};
RG   Pathogen Informatics;
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000256|ARBA:ARBA00009477}.
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DR   EMBL; EF488093; ABU67980.1; -; Genomic_DNA.
DR   EMBL; EF488095; ABU68009.1; -; Genomic_DNA.
DR   EMBL; AJ276410; CAC03518.1; -; Genomic_DNA.
DR   EMBL; AJ278419; CAC18583.1; -; Genomic_DNA.
DR   EMBL; CABCSJ010000004; VST69084.1; -; Genomic_DNA.
DR   PIR; F95061; F95061.
DR   RefSeq; WP_001069075.1; NZ_CFCG01000011.1.
DR   AlphaFoldDB; Q9EU69; -.
DR   SMR; Q9EU69; -.
DR   PATRIC; fig|1313.6511.peg.501; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR058786; BSH_LcnD/ComB.
DR   InterPro; IPR058794; HB_LcnD/ComB-like.
DR   InterPro; IPR058795; LcnD/ComB-like_C.
DR   InterPro; IPR060199; LcnD/ComB-like_N.
DR   InterPro; IPR005696; MesE/LcnD.
DR   InterPro; IPR050739; MFP.
DR   NCBIfam; TIGR01000; bacteriocin_acc; 1.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR   PANTHER; PTHR30386:SF26; TRANSPORT PROTEIN COMB; 1.
DR   Pfam; PF25935; BSH_LcnD; 1.
DR   Pfam; PF27342; ComB_N; 1.
DR   Pfam; PF25887; HB_LcnD; 1.
DR   Pfam; PF25940; LcnD_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..40
FT                   /note="LcnD/ComB-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF27342"
FT   DOMAIN          58..345
FT                   /note="LcnD/ComB-like barrel-sandwich hybrid"
FT                   /evidence="ECO:0000259|Pfam:PF25935"
FT   DOMAIN          98..306
FT                   /note="LcnD/ComB-like long helical bundle"
FT                   /evidence="ECO:0000259|Pfam:PF25887"
FT   DOMAIN          350..438
FT                   /note="LcnD/ComB-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF25940"
FT   COILED          288..315
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   453 AA;  50528 MW;  3019554307E1063C CRC64;
     MNPNLFRSVE FYQRRYHNYA TVLIIPLSLL FTFILIFSLV ATKEITVTSQ GEIAPTSVIA
     SIQSTSDNPI LANHLVANQV VEKGDLLIKY SETMEESQKT ALATQLQRLE KQKEGLGILK
     QSLEKATDLF SGEDEFGYHN TFMNFTKQSH DIELGITKTN TEVSNQANLS NSSSSAIEQE
     ITKVQQQIGE YQELRDAIIN NRARLPTGNP HQSILNRYLV ASQGQTQGTA EEPFLSQINQ
     SIAGLESSIA SLKIQQAGIG SVATYDNSLA TKIEVLRTQF LQTASQQQLT VENQLTELKV
     QLDQATQRLE NNTLTSPSKG IVHLNSEFEG KNRIPTGTEI AQIFPVITDT REVLITYYVS
     SDYLPLLDKG QTVRLKLEKI GNHGTTIIGQ LQTIDQTPTR TEQGNLFKLT ALAKLSNEDS
     KLIQYGLQGR VTSVTTKKTY FDYFKDKILT HSD
//
ID   S5TRM3_PLADU            Unreviewed;       118 AA.
AC   S5TRM3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   02-SEP-2026, entry version 30.
DE   SubName: Full=Transcription factor Id {ECO:0000313|EMBL:AGS55452.1};
GN   Name=Id {ECO:0000313|EMBL:AGS55452.1};
OS   Platynereis dumerilii (Dumeril's clam worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Platynereis.
OX   NCBI_TaxID=6359 {ECO:0000313|EMBL:AGS55452.1};
RN   [1] {ECO:0000313|EMBL:AGS55452.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23891818; DOI=10.1016/j.ydbio.2013.07.013;
RA   Gazave E., Behague J., Laplane L., Guillou A., Preau L., Demilly A.,
RA   Balavoine G., Vervoort M.;
RT   "Posterior elongation in the annelid Platynereis dumerilii involves stem
RT   cells molecularly related to primordial germ cells.";
RL   Dev. Biol. 382:246-267(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00981}.
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DR   EMBL; KC999056; AGS55452.1; -; mRNA.
DR   AlphaFoldDB; S5TRM3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IEA:TreeGrafter.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd19684; bHLH_dnHLH_ID; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; DNA-BINDING PROTEIN INHIBITOR; 1.
DR   PANTHER; PTHR11723:SF17; PROTEIN EXTRA-MACROCHAETAE; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00981}; Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00981};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00981}.
FT   DOMAIN          20..72
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          34..72
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00981"
SQ   SEQUENCE   118 AA;  13075 MW;  1AC4B5DC36C8A1AE CRC64;
     MKATVCTKTH ELGVALDRFR ISKPKAADVP ICEADMQACF HKLKELVPTI PQDRKISRVA
     LLQHVIDYIL DLELTLEHSP TSRNSPPSLL QTALAAMPAS IDRKPLGEAT NICYPENN
//