ID   R3HCL_HUMAN             Reviewed;         792 AA.
AC   Q7Z5L2; O60598; Q5W0B4; Q5W0B5; Q86VT9; Q8N9H0;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 3.
DT   02-OCT-2024, entry version 145.
DE   RecName: Full=Coiled-coil domain-containing protein R3HCC1L;
DE   AltName: Full=Growth inhibition and differentiation-related protein 88;
DE   AltName: Full=Putative mitochondrial space protein 32.1;
DE   AltName: Full=R3H and coiled-coil domain-containing protein 1-like;
GN   Name=R3HCC1L; Synonyms=C10orf28, GIDRP88;
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 1), AND VARIANT ARG-656.
RA   Yan J., Zhang J., Peng X., Luo D., Deng Y., Bao L., Liu Z., Li B., Gao X.;
RT   "Molecular cloning and characterization of a novel gene GIDRP88, encoding a
RT   growth inhibition and differentiation related protein.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT ARG-656.
RC   TISSUE=Ovary;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-362 (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=10867487; DOI=10.1159/000021014;
RA   Page N.M., Butlin D.J., Manyonda I., Lowry P.J.;
RT   "The development of a genetic profile of placental gene expression during
RT   the first trimester of pregnancy: a potential tool for identifying novel
RT   secreted markers.";
RL   Fetal Diagn. Ther. 15:237-245(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-792 (ISOFORM 2), AND VARIANTS
RP   ARG-566 AND ARG-656.
RC   TISSUE=Cerebellum;
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   INTERACTION WITH THE EJC COMPLEX, AND MUTAGENESIS OF 14-ARG--TYR-20.
RX   PubMed=20930030; DOI=10.1101/gad.604610;
RA   Kashima I., Jonas S., Jayachandran U., Buchwald G., Conti E., Lupas A.N.,
RA   Izaurralde E.;
RT   "SMG6 interacts with the exon junction complex via two conserved EJC-
RT   binding motifs (EBMs) required for nonsense-mediated mRNA decay.";
RL   Genes Dev. 24:2440-2450(2010).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- SUBUNIT: May interact with the exon junction complex (EJC) composed at
CC       least of CASC3, EIF4A3, MAGOH and RBM8A.
CC   -!- INTERACTION:
CC       Q7Z5L2; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-10262006, EBI-10261970;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7Z5L2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z5L2-2; Sequence=VSP_014920;
CC       Name=3;
CC         IsoId=Q7Z5L2-3; Sequence=VSP_014919, VSP_014921;
CC   -!- TISSUE SPECIFICITY: Expressed in placenta.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC05748.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC04364.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF525304; AAP80788.1; -; mRNA.
DR   EMBL; AL139241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL355301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047908; AAH47908.1; -; mRNA.
DR   EMBL; AF050198; AAC05748.1; ALT_FRAME; mRNA.
DR   EMBL; AK094479; BAC04364.1; ALT_INIT; mRNA.
DR   CCDS; CCDS31267.1; -. [Q7Z5L2-2]
DR   CCDS; CCDS58093.1; -. [Q7Z5L2-3]
DR   CCDS; CCDS73178.1; -. [Q7Z5L2-1]
DR   RefSeq; NP_001243548.1; NM_001256619.1. [Q7Z5L2-1]
DR   RefSeq; NP_001243549.1; NM_001256620.1.
DR   RefSeq; NP_001243550.1; NM_001256621.1. [Q7Z5L2-3]
DR   RefSeq; XP_011537942.1; XM_011539640.1. [Q7Z5L2-1]
DR   RefSeq; XP_011537943.1; XM_011539641.1. [Q7Z5L2-1]
DR   RefSeq; XP_011537944.1; XM_011539642.1. [Q7Z5L2-1]
DR   RefSeq; XP_011537945.1; XM_011539643.1. [Q7Z5L2-1]
DR   RefSeq; XP_011537946.1; XM_011539644.1. [Q7Z5L2-1]
DR   RefSeq; XP_011537947.1; XM_011539645.2. [Q7Z5L2-1]
DR   RefSeq; XP_011537948.1; XM_011539646.1. [Q7Z5L2-1]
DR   RefSeq; XP_011537949.1; XM_011539647.1.
DR   RefSeq; XP_011537950.1; XM_011539648.1. [Q7Z5L2-1]
DR   RefSeq; XP_016871563.1; XM_017016074.1.
DR   AlphaFoldDB; Q7Z5L2; -.
DR   SMR; Q7Z5L2; -.
DR   BioGRID; 118115; 22.
DR   IntAct; Q7Z5L2; 10.
DR   STRING; 9606.ENSP00000483494; -.
DR   CarbonylDB; Q7Z5L2; -.
DR   GlyGen; Q7Z5L2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7Z5L2; -.
DR   PhosphoSitePlus; Q7Z5L2; -.
DR   BioMuta; R3HCC1L; -.
DR   DMDM; 71648680; -.
DR   jPOST; Q7Z5L2; -.
DR   MassIVE; Q7Z5L2; -.
DR   PaxDb; 9606-ENSP00000483494; -.
DR   PeptideAtlas; Q7Z5L2; -.
DR   ProteomicsDB; 69316; -. [Q7Z5L2-1]
DR   ProteomicsDB; 69317; -. [Q7Z5L2-2]
DR   ProteomicsDB; 69318; -. [Q7Z5L2-3]
DR   Pumba; Q7Z5L2; -.
DR   Antibodypedia; 52284; 117 antibodies from 24 providers.
DR   DNASU; 27291; -.
DR   Ensembl; ENST00000370586.6; ENSP00000359618.1; ENSG00000166024.14. [Q7Z5L2-3]
DR   Ensembl; ENST00000612478.4; ENSP00000483494.1; ENSG00000166024.14. [Q7Z5L2-1]
DR   Ensembl; ENST00000613938.4; ENSP00000479916.1; ENSG00000166024.14. [Q7Z5L2-3]
DR   GeneID; 27291; -.
DR   KEGG; hsa:27291; -.
DR   UCSC; uc009xvx.4; human. [Q7Z5L2-1]
DR   AGR; HGNC:23512; -.
DR   CTD; 27291; -.
DR   DisGeNET; 27291; -.
DR   GeneCards; R3HCC1L; -.
DR   HGNC; HGNC:23512; R3HCC1L.
DR   HPA; ENSG00000166024; Low tissue specificity.
DR   neXtProt; NX_Q7Z5L2; -.
DR   OpenTargets; ENSG00000166024; -.
DR   VEuPathDB; HostDB:ENSG00000166024; -.
DR   eggNOG; KOG4483; Eukaryota.
DR   GeneTree; ENSGT00530000063711; -.
DR   HOGENOM; CLU_025109_0_0_1; -.
DR   InParanoid; Q7Z5L2; -.
DR   OrthoDB; 1099789at2759; -.
DR   PhylomeDB; Q7Z5L2; -.
DR   TreeFam; TF324168; -.
DR   PathwayCommons; Q7Z5L2; -.
DR   SignaLink; Q7Z5L2; -.
DR   BioGRID-ORCS; 27291; 10 hits in 1161 CRISPR screens.
DR   ChiTaRS; R3HCC1L; human.
DR   GenomeRNAi; 27291; -.
DR   Pharos; Q7Z5L2; Tbio.
DR   PRO; PR:Q7Z5L2; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q7Z5L2; protein.
DR   Bgee; ENSG00000166024; Expressed in primordial germ cell in gonad and 116 other cell types or tissues.
DR   ExpressionAtlas; Q7Z5L2; baseline and differential.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR039884; R3HC1/R3HCL.
DR   PANTHER; PTHR21678:SF7; COILED-COIL DOMAIN-CONTAINING PROTEIN R3HCC1L; 1.
DR   PANTHER; PTHR21678; GROWTH INHIBITION AND DIFFERENTIATION RELATED PROTEIN 88; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..792
FT                   /note="Coiled-coil domain-containing protein R3HCC1L"
FT                   /id="PRO_0000087487"
FT   REGION          7..27
FT                   /note="EJC-binding motif; may mediate interaction with the
FT                   EJC"
FT   REGION          32..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          751..783
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        548..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         712
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJM3"
FT   VAR_SEQ         1..608
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014919"
FT   VAR_SEQ         595..608
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014920"
FT   VAR_SEQ         609
FT                   /note="K -> M (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014921"
FT   VARIANT         113
FT                   /note="S -> P (in dbSNP:rs12775148)"
FT                   /id="VAR_056898"
FT   VARIANT         238
FT                   /note="K -> N (in dbSNP:rs7922159)"
FT                   /id="VAR_056899"
FT   VARIANT         261
FT                   /note="S -> G (in dbSNP:rs35373035)"
FT                   /id="VAR_056900"
FT   VARIANT         535
FT                   /note="D -> A (in dbSNP:rs34494334)"
FT                   /id="VAR_056901"
FT   VARIANT         546
FT                   /note="P -> S (in dbSNP:rs35122894)"
FT                   /id="VAR_061652"
FT   VARIANT         566
FT                   /note="H -> R (in dbSNP:rs11189513)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_023092"
FT   VARIANT         656
FT                   /note="H -> R (in dbSNP:rs1952061)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT                   /id="VAR_023093"
FT   MUTAGEN         14..20
FT                   /note="RPDMALY->EPDMALE: Loss of interaction with the EJC."
FT                   /evidence="ECO:0000269|PubMed:20930030"
FT   CONFLICT        212
FT                   /note="K -> E (in Ref. 1; AAP80788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        438
FT                   /note="S -> G (in Ref. 1; AAP80788)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   792 AA;  87883 MW;  10009E3042856E52 CRC64;
     MQQESERCRV RARRPDMALY VPKARRGAVL LKTGDEEESC GSPNSVVKEK QKESSLSQKE
     VFKDKPEARR LNINPDRKEH NCREEKKSST KLRMDTCLQK TNRVCSKRGT TESKEVLSQG
     QQQGAPNAGV ITNAPLQRHF KPKKVECLEV ETTDVTGHER ILLSQACLEI SEAQVPSKPF
     QNVEFCDFSR HEPDGEAFED KDLEGRIETD TKVLEILYEF PRVFSSVMKP ENMIVPIKLS
     SDSEIVQQSM QTSDGILNPS SGGITTTSVP GSPDGVFDQT CVDFEVESVG GIANSTGFIL
     DQKDTDSIPA TMGHISLSES TNDTVSPVMI RECEKNDSTA DELHVKHEPP DTAVLAHETH
     RDSGFKNVGD ITNKACMMDT TGMSCSDHVT VDSPYVVAVR IADETSINTR SFSKFVGMSA
     DATPLHVARS GNDTEDFSNP SACSDIYGES ISSHFTESTG KLIESLSDCA SSLPIKKIAG
     SNYNTFLDSE LSMLNGTKVL SDSAVGIDLG STGDTTEALH ELRTAEEFKT EEQDDSGSIE
     FGVSFPDRES SSMETSIEPK ATETSHTEGI TAIEESWESM FNDDGDCLDP RLLQEGILMH
     IKPENHCSKL SGNTKSRESI QEPRSDYYNH EVPDIDLSDC EFPHVIEIYD FPQEFHTEDL
     LRVFCSYQKK GFDIKWVDDT HALGVFSSPI TARDALGIKH TMVKIRPLSQ ATRAAKAKAR
     AYAEFLQPAK ERPETSAALA RRLVISALGV RSKQSKTERE AELKKLQEAR ERKRLEAKQR
     EDIWEGRDQS TV
//