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RIMC1_HUMAN
ID   RIMC1_HUMAN             Reviewed;         294 AA.
AC   A6NDU8; A2RRM9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=RAB7A-interacting MON1-CCZ1 complex subunit 1 {ECO:0000305};
DE   AltName: Full=UPF0600 protein C5orf51;
GN   Name=RIMOC1 {ECO:0000312|HGNC:HGNC:27750}; Synonyms=C5orf51;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
RN   [6]
RP   FUNCTION, INTERACTION WITH MON1A-CCZ1B COMPLEX AND RAB7A, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=34432599; DOI=10.1080/15548627.2021.1960116;
RA   Yan B.R., Li T., Coyaud E., Laurent E.M.N., St-Germain J., Zhou Y.,
RA   Kim P.K., Raught B., Brumell J.H.;
RT   "C5orf51 is a component of the MON1-CCZ1 complex and controls RAB7A
RT   localization and stability during mitophagy.";
RL   Autophagy 18:829-840(2022).
CC   -!- FUNCTION: Plays an important role in the removal of damaged
CC       mitochondria via mitophagy by controlling the stability and
CC       localization of RAB7A. Required for the recruitment of RAB7A and ATG9A
CC       vesicles to damaged mitochondria and promotes the stability of RAB7A by
CC       inhibiting its proteasomal degradation during mitophagy.
CC       {ECO:0000269|PubMed:34432599}.
CC   -!- SUBUNIT: Interacts with the MON1A-CCZ1B complex (PubMed:34432599).
CC       Interacts with GDP-bound RAB7A and promotes its interaction with the
CC       MON1A-CCZ1B complex (PubMed:34432599). {ECO:0000269|PubMed:34432599}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:34432599}.
CC   -!- SIMILARITY: Belongs to the RIMOC1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI31722.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR   EMBL; AC034222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471119; EAW56017.1; -; Genomic_DNA.
DR   EMBL; BC131721; AAI31722.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS34151.1; -.
DR   RefSeq; NP_787117.3; NM_175921.5.
DR   AlphaFoldDB; A6NDU8; -.
DR   BioGRID; 130165; 18.
DR   IntAct; A6NDU8; 4.
DR   STRING; 9606.ENSP00000371061; -.
DR   GlyGen; A6NDU8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; A6NDU8; -.
DR   MetOSite; A6NDU8; -.
DR   PhosphoSitePlus; A6NDU8; -.
DR   BioMuta; C5orf51; -.
DR   EPD; A6NDU8; -.
DR   jPOST; A6NDU8; -.
DR   MassIVE; A6NDU8; -.
DR   MaxQB; A6NDU8; -.
DR   PaxDb; A6NDU8; -.
DR   PeptideAtlas; A6NDU8; -.
DR   PRIDE; A6NDU8; -.
DR   ProteomicsDB; 929; -.
DR   Antibodypedia; 23213; 70 antibodies from 13 providers.
DR   DNASU; 285636; -.
DR   Ensembl; ENST00000381647.7; ENSP00000371061.2; ENSG00000205765.10.
DR   GeneID; 285636; -.
DR   KEGG; hsa:285636; -.
DR   MANE-Select; ENST00000381647.7; ENSP00000371061.2; NM_175921.6; NP_787117.3.
DR   UCSC; uc003jmo.4; human.
DR   CTD; 285636; -.
DR   GeneCards; C5orf51; -.
DR   HGNC; HGNC:27750; RIMOC1.
DR   HPA; ENSG00000205765; Low tissue specificity.
DR   neXtProt; NX_A6NDU8; -.
DR   OpenTargets; ENSG00000205765; -.
DR   VEuPathDB; HostDB:ENSG00000205765; -.
DR   eggNOG; ENOG502QW9A; Eukaryota.
DR   GeneTree; ENSGT00390000011383; -.
DR   HOGENOM; CLU_082742_0_0_1; -.
DR   InParanoid; A6NDU8; -.
DR   OMA; GASCTTH; -.
DR   OrthoDB; 909559at2759; -.
DR   PhylomeDB; A6NDU8; -.
DR   TreeFam; TF331577; -.
DR   PathwayCommons; A6NDU8; -.
DR   SignaLink; A6NDU8; -.
DR   BioGRID-ORCS; 285636; 6 hits in 1052 CRISPR screens.
DR   ChiTaRS; C5orf51; human.
DR   GenomeRNAi; 285636; -.
DR   Pharos; A6NDU8; Tdark.
DR   PRO; PR:A6NDU8; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; A6NDU8; protein.
DR   Bgee; ENSG00000205765; Expressed in esophagus squamous epithelium and 195 other tissues.
DR   ExpressionAtlas; A6NDU8; baseline and differential.
DR   Genevisible; A6NDU8; HS.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000423; P:mitophagy; IMP:UniProtKB.
DR   InterPro; IPR037657; RIMC1.
DR   PANTHER; PTHR28494; PTHR28494; 1.
DR   Pfam; PF17716; DUF5561; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Cytoplasm; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..294
FT                   /note="RAB7A-interacting MON1-CCZ1 complex subunit 1"
FT                   /id="PRO_0000341214"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   VARIANT         20
FT                   /note="Q -> H (in dbSNP:rs12520325)"
FT                   /id="VAR_044032"
SQ   SEQUENCE   294 AA;  33620 MW;  31BE22D36F768CC4 CRC64;
     MAAAVSSVVR RVEELGDLAQ AHIQQLSEAA GEDDHFLIRA SAALEKLKLL CGEEKECSNP
     SNLLELYTQA ILDMTYFEEN KLVDEDFPED SSSQKVKELI SFLSEPEILV KENNMHPKHC
     NLLGDELLEC LSWRRGALLY MYCHSLTKRR EWLLRKSSLL KKYLLDGISY LLQMLNYRCP
     IQLNEGVSFQ DLDTAKLLSA GIFSDIHLLA MMYSGEMCYW GSKYCADQQP ENHEVDTSVS
     GAGCTTYKEP LDFREVGEKI LKKYVSVCEG PLKEQEWNTT NAKQILNFFH HRCN
 
 
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