ID   ID3_HUMAN               Reviewed;         119 AA.
AC   Q02535; A8K1T8; O75641;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   29-SEP-2021, entry version 195.
DE   RecName: Full=DNA-binding protein inhibitor ID-3;
DE   AltName: Full=Class B basic helix-loop-helix protein 25;
DE            Short=bHLHb25;
DE   AltName: Full=Helix-loop-helix protein HEIR-1;
DE   AltName: Full=ID-like protein inhibitor HLH 1R21;
DE   AltName: Full=Inhibitor of DNA binding 3;
DE   AltName: Full=Inhibitor of differentiation 3;
GN   Name=ID3; Synonyms=1R21, BHLHB25, HEIR1;
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], AND VARIANT ALA-105.
RX   PubMed=1628620; DOI=10.1002/j.1460-2075.1992.tb05321.x;
RA   Ellmeier W., Aguzzi A., Kleiner E., Kurzbauer R., Weith A.;
RT   "Mutually exclusive expression of a helix-loop-helix gene and N-myc in
RT   human neuroblastomas and in normal development.";
RL   EMBO J. 11:2563-2571(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT ALA-105.
RX   PubMed=8437843;
RA   Deed R.W., Bianchi S.M., Atherton G.T., Johnston D., Santibanez-Koref M.,
RA   Murphy J.J., Norton J.D.;
RT   "An immediate early human gene encodes an Id-like helix-loop-helix protein
RT   and is regulated by protein kinase C activation in diverse cell types.";
RL   Oncogene 8:599-607(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-105.
RC   TISSUE=Blood;
RX   PubMed=7828896; DOI=10.1016/0378-1119(94)90676-9;
RA   Deed R.W., Hirose T., Mitchell E.L.D., Santibanez-Koref M.F., Norton J.D.;
RT   "Structural organisation and chromosomal mapping of the human Id-3 gene.";
RL   Gene 151:309-314(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-105.
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-105.
RC   TISSUE=Hippocampus;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-105.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-105.
RC   TISSUE=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   [9]
RP   INTERACTION WITH CLOCK AND ARNTL.
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).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. Involved in myogenesis by inhibiting skeletal muscle
CC       and cardiac myocyte differentiation and promoting muscle precursor
CC       cells proliferation. Inhibits the binding of E2A-containing protein
CC       complexes to muscle creatine kinase E-box enhancer. Regulates the
CC       circadian clock by repressing the transcriptional activator activity of
CC       the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:8437843}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with other HLH proteins. Interacts
CC       with COPS5 and COPS7A. Interacts with IFI204. Interacts with GATA4 and
CC       NKX2-5. Interacts with ANKRD2; both proteins cooperate in myoblast
CC       differentiation (By similarity). Interacts with CLOCK and ARNTL/BMAL1.
CC       {ECO:0000250, ECO:0000269|PubMed:20861012}.
CC   -!- INTERACTION:
CC       Q02535; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-1387094, EBI-11954519;
CC       Q02535; A0A087WZT3: BOLA2B; NbExp=3; IntAct=EBI-1387094, EBI-12006120;
CC       Q02535; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-1387094, EBI-7317823;
CC       Q02535; Q02930-3: CREB5; NbExp=5; IntAct=EBI-1387094, EBI-10192698;
CC       Q02535; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1387094, EBI-10976677;
CC       Q02535; Q5RGS3: FAM74A1; NbExp=3; IntAct=EBI-1387094, EBI-10244822;
CC       Q02535; Q14192: FHL2; NbExp=4; IntAct=EBI-1387094, EBI-701903;
CC       Q02535; O43559: FRS3; NbExp=3; IntAct=EBI-1387094, EBI-725515;
CC       Q02535; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-1387094, EBI-11978177;
CC       Q02535; P49639: HOXA1; NbExp=3; IntAct=EBI-1387094, EBI-740785;
CC       Q02535; Q92993: KAT5; NbExp=3; IntAct=EBI-1387094, EBI-399080;
CC       Q02535; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-1387094, EBI-3957672;
CC       Q02535; P61968: LMO4; NbExp=3; IntAct=EBI-1387094, EBI-2798728;
CC       Q02535; A6NI15: MSGN1; NbExp=3; IntAct=EBI-1387094, EBI-11991020;
CC       Q02535; P13349: MYF5; NbExp=3; IntAct=EBI-1387094, EBI-17491620;
CC       Q02535; P51149: RAB7A; NbExp=3; IntAct=EBI-1387094, EBI-1056089;
CC       Q02535; O00560: SDCBP; NbExp=3; IntAct=EBI-1387094, EBI-727004;
CC       Q02535; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1387094, EBI-5235340;
CC       Q02535; Q99081: TCF12; NbExp=5; IntAct=EBI-1387094, EBI-722877;
CC       Q02535; Q99081-3: TCF12; NbExp=4; IntAct=EBI-1387094, EBI-11952764;
CC       Q02535; P15923: TCF3; NbExp=3; IntAct=EBI-1387094, EBI-769630;
CC       Q02535; P15923-3: TCF3; NbExp=3; IntAct=EBI-1387094, EBI-12000326;
CC       Q02535; P15884: TCF4; NbExp=5; IntAct=EBI-1387094, EBI-533224;
CC       Q02535; P15884-3: TCF4; NbExp=3; IntAct=EBI-1387094, EBI-13636688;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in lung, kidney and adrenal
CC       gland, but not in adult brain.
CC   -!- INDUCTION: By phorbol 12-myristate 13-acetate (PMA).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA47360.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X66924; CAA47360.1; ALT_INIT; mRNA.
DR   EMBL; X69111; CAA48862.1; -; mRNA.
DR   EMBL; X73428; CAA51827.1; -; Genomic_DNA.
DR   EMBL; BT006791; AAP35437.1; -; mRNA.
DR   EMBL; AK290003; BAF82692.1; -; mRNA.
DR   EMBL; AL021154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471134; EAW95060.1; -; Genomic_DNA.
DR   EMBL; BC003107; AAH03107.1; -; mRNA.
DR   CCDS; CCDS237.1; -.
DR   PIR; I37092; S28529.
DR   RefSeq; NP_002158.3; NM_002167.4.
DR   PDB; 2LFH; NMR; -; A/B=29-83.
DR   PDBsum; 2LFH; -.
DR   BMRB; Q02535; -.
DR   SMR; Q02535; -.
DR   BioGRID; 109625; 47.
DR   DIP; DIP-713N; -.
DR   IntAct; Q02535; 40.
DR   STRING; 9606.ENSP00000363689; -.
DR   iPTMnet; Q02535; -.
DR   PhosphoSitePlus; Q02535; -.
DR   BioMuta; ID3; -.
DR   DMDM; 322510035; -.
DR   EPD; Q02535; -.
DR   jPOST; Q02535; -.
DR   MassIVE; Q02535; -.
DR   MaxQB; Q02535; -.
DR   PaxDb; Q02535; -.
DR   PeptideAtlas; Q02535; -.
DR   PRIDE; Q02535; -.
DR   ProteomicsDB; 58106; -.
DR   Antibodypedia; 4480; 608 antibodies.
DR   DNASU; 3399; -.
DR   Ensembl; ENST00000374561; ENSP00000363689; ENSG00000117318.
DR   Ensembl; ENST00000634790; ENSP00000489102; ENSG00000283060.
DR   GeneID; 3399; -.
DR   KEGG; hsa:3399; -.
DR   UCSC; uc001bhh.5; human.
DR   CTD; 3399; -.
DR   DisGeNET; 3399; -.
DR   GeneCards; ID3; -.
DR   HGNC; HGNC:5362; ID3.
DR   HPA; ENSG00000117318; Tissue enhanced (seminal).
DR   MIM; 600277; gene.
DR   neXtProt; NX_Q02535; -.
DR   OpenTargets; ENSG00000117318; -.
DR   PharmGKB; PA29610; -.
DR   VEuPathDB; HostDB:ENSG00000117318; -.
DR   eggNOG; ENOG502S53I; Eukaryota.
DR   GeneTree; ENSGT00940000160504; -.
DR   HOGENOM; CLU_116790_1_0_1; -.
DR   InParanoid; Q02535; -.
DR   OMA; CCVSEQS; -.
DR   OrthoDB; 1624054at2759; -.
DR   PhylomeDB; Q02535; -.
DR   TreeFam; TF326217; -.
DR   PathwayCommons; Q02535; -.
DR   Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR   SIGNOR; Q02535; -.
DR   BioGRID-ORCS; 3399; 13 hits in 1042 CRISPR screens.
DR   ChiTaRS; ID3; human.
DR   GeneWiki; ID3_(gene); -.
DR   GenomeRNAi; 3399; -.
DR   Pharos; Q02535; Tbio.
DR   PRO; PR:Q02535; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q02535; protein.
DR   Bgee; ENSG00000117318; Expressed in right lobe of thyroid gland and 224 other tissues.
DR   Genevisible; Q02535; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1901707; F:leptomycin B binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0140416; F:transcription regulator inhibitor activity; TAS:ARUK-UCL.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0072750; P:cellular response to leptomycin B; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:GDB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GDB.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR   GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; PTHR11723; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Biological rhythms; Myogenesis; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..119
FT                   /note="DNA-binding protein inhibitor ID-3"
FT                   /id="PRO_0000127247"
FT   DOMAIN          28..80
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   VARIANT         105
FT                   /note="T -> A (in dbSNP:rs11574)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1628620,
FT                   ECO:0000269|PubMed:7828896, ECO:0000269|PubMed:8437843,
FT                   ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT                   /id="VAR_016122"
FT   VARIANT         111
FT                   /note="S -> A (in dbSNP:rs11542317)"
FT                   /id="VAR_030739"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:2LFH"
FT   HELIX           43..54
FT                   /evidence="ECO:0007829|PDB:2LFH"
FT   HELIX           66..81
FT                   /evidence="ECO:0007829|PDB:2LFH"
SQ   SEQUENCE   119 AA;  12999 MW;  7FC38B56B4DCEFBC CRC64;
     MKALSPVRGC YEAVCCLSER SLAIARGRGK GPAAEEPLSL LDDMNHCYSR LRELVPGVPR
     GTQLSQVEIL QRVIDYILDL QVVLAEPAPG PPDGPHLPIQ TAELTPELVI SNDKRSFCH
//