R3HCL_HUMAN
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 03-AUG-2022, entry version 134.
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};
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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. [Q7Z5L2-1]
DR AlphaFoldDB; Q7Z5L2; -.
DR SMR; Q7Z5L2; -.
DR BioGRID; 118115; 20.
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 EPD; Q7Z5L2; -.
DR jPOST; Q7Z5L2; -.
DR MassIVE; Q7Z5L2; -.
DR MaxQB; Q7Z5L2; -.
DR PaxDb; Q7Z5L2; -.
DR PeptideAtlas; Q7Z5L2; -.
DR PRIDE; Q7Z5L2; -.
DR ProteomicsDB; 69316; -. [Q7Z5L2-1]
DR ProteomicsDB; 69317; -. [Q7Z5L2-2]
DR ProteomicsDB; 69318; -. [Q7Z5L2-3]
DR Antibodypedia; 52284; 102 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 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; 844916at2759; -.
DR PhylomeDB; Q7Z5L2; -.
DR TreeFam; TF324168; -.
DR PathwayCommons; Q7Z5L2; -.
DR SignaLink; Q7Z5L2; -.
DR BioGRID-ORCS; 27291; 10 hits in 1083 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 right testis and 114 other tissues.
DR ExpressionAtlas; Q7Z5L2; baseline and differential.
DR Genevisible; Q7Z5L2; HS.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039884; R3HC1/R3HCL.
DR PANTHER; PTHR21678; PTHR21678; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; 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
