RB40C_HUMAN
ID RB40C_HUMAN Reviewed; 281 AA.
AC Q96S21; A2IDE2; D3DU54; O60795; Q4TT41; Q5PXE8; Q6PIU5;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ras-related protein Rab-40C;
DE AltName: Full=Rar-like protein;
DE AltName: Full=Ras-like protein family member 8C;
DE AltName: Full=SOCS box-containing protein RAR3;
GN Name=RAB40C; Synonyms=RARL, RASL8C;
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 2).
RC TISSUE=Brain;
RA Sievert V., Buessow K.;
RT "Sequencing of E. coli expression clones for human proteins.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP FUNCTION IN AN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, INTERACTION WITH CUL5; RNF7; ELOB AND ELOC, AND MUTAGENESIS
RP OF 212-LEU--PRO-215 AND 221-HIS-LEU-222.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C.,
RA Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1
RT and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
CC -!- FUNCTION: Probable substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins. {ECO:0000269|PubMed:15601820}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the probable SCF-like ECS(RAB40C) E3 ubiquitin-
CC protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC
CC complex and RAB40C. Interacts with CUL5, RNF7, ELOB and ELOC.
CC {ECO:0000269|PubMed:15601820}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96S21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96S21-2; Sequence=VSP_055835;
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY823398; AAV83924.1; -; mRNA.
DR EMBL; AE006464; AAK61236.1; -; Genomic_DNA.
DR EMBL; Z84479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85791.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85792.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85793.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85794.1; -; Genomic_DNA.
DR EMBL; BC028696; AAH28696.1; -; mRNA.
DR CCDS; CCDS10413.1; -. [Q96S21-1]
DR RefSeq; NP_001166134.1; NM_001172663.1. [Q96S21-1]
DR RefSeq; NP_001166135.1; NM_001172664.1. [Q96S21-1]
DR RefSeq; NP_001166136.1; NM_001172665.1. [Q96S21-1]
DR RefSeq; NP_001166137.1; NM_001172666.1. [Q96S21-2]
DR RefSeq; NP_066991.3; NM_021168.4. [Q96S21-1]
DR AlphaFoldDB; Q96S21; -.
DR SMR; Q96S21; -.
DR BioGRID; 121771; 34.
DR IntAct; Q96S21; 9.
DR STRING; 9606.ENSP00000438492; -.
DR GlyGen; Q96S21; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96S21; -.
DR PhosphoSitePlus; Q96S21; -.
DR BioMuta; RAB40C; -.
DR DMDM; 27734457; -.
DR EPD; Q96S21; -.
DR jPOST; Q96S21; -.
DR MassIVE; Q96S21; -.
DR PaxDb; Q96S21; -.
DR PeptideAtlas; Q96S21; -.
DR PRIDE; Q96S21; -.
DR ProteomicsDB; 78059; -. [Q96S21-1]
DR TopDownProteomics; Q96S21-1; -. [Q96S21-1]
DR Antibodypedia; 35310; 136 antibodies from 24 providers.
DR DNASU; 57799; -.
DR Ensembl; ENST00000248139.8; ENSP00000248139.3; ENSG00000197562.10. [Q96S21-1]
DR Ensembl; ENST00000535977.5; ENSP00000438492.1; ENSG00000197562.10. [Q96S21-1]
DR Ensembl; ENST00000538492.5; ENSP00000438382.1; ENSG00000197562.10. [Q96S21-1]
DR Ensembl; ENST00000539661.5; ENSP00000445050.1; ENSG00000197562.10. [Q96S21-1]
DR GeneID; 57799; -.
DR KEGG; hsa:57799; -.
DR MANE-Select; ENST00000248139.8; ENSP00000248139.3; NM_021168.5; NP_066991.3.
DR UCSC; uc002chr.4; human. [Q96S21-1]
DR CTD; 57799; -.
DR DisGeNET; 57799; -.
DR GeneCards; RAB40C; -.
DR HGNC; HGNC:18285; RAB40C.
DR HPA; ENSG00000197562; Tissue enhanced (skin).
DR MIM; 619551; gene.
DR neXtProt; NX_Q96S21; -.
DR OpenTargets; ENSG00000197562; -.
DR PharmGKB; PA34139; -.
DR VEuPathDB; HostDB:ENSG00000197562; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000158979; -.
DR InParanoid; Q96S21; -.
DR OMA; RMAFFEV; -.
DR OrthoDB; 1065856at2759; -.
DR PhylomeDB; Q96S21; -.
DR TreeFam; TF323230; -.
DR PathwayCommons; Q96S21; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q96S21; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57799; 9 hits in 1081 CRISPR screens.
DR ChiTaRS; RAB40C; human.
DR GenomeRNAi; 57799; -.
DR Pharos; Q96S21; Tbio.
DR PRO; PR:Q96S21; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96S21; protein.
DR Bgee; ENSG00000197562; Expressed in skin of leg and 94 other tissues.
DR ExpressionAtlas; Q96S21; baseline and differential.
DR Genevisible; Q96S21; HS.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00174; RHO; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..281
FT /note="Ras-related protein Rab-40C"
FT /id="PRO_0000121261"
FT DOMAIN 175..228
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 245..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 273
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 278
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 115..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_055835"
FT MUTAGEN 212..215
FT /note="LPLP->AAAA: Abolishes interaction with RNF7 and
FT CUL5."
FT /evidence="ECO:0000269|PubMed:15601820"
FT MUTAGEN 221..222
FT /note="HL->AA: Abolishes interaction with RNF7."
FT /evidence="ECO:0000269|PubMed:15601820"
FT CONFLICT 64
FT /note="K -> R (in Ref. 5; AAH28696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 31304 MW; 478F974645AA91EC CRC64;
MGSQGSPVKS YDYLLKFLLV GDSDVGKGEI LESLQDGAAE SPYAYSNGID YKTTTILLDG
RRVKLELWDT SGQGRFCTIF RSYSRGAQGI LLVYDITNRW SFDGIDRWIK EIDEHAPGVP
RILVGNRLHL AFKRQVPTEQ ARAYAEKNCM TFFEVSPLCN FNVIESFTEL SRIVLMRHGM
EKIWRPNRVF SLQDLCCRAI VSCTPVHLID KLPLPVTIKS HLKSFSMANG MNAVMMHGRS
YSLASGAGGG GSKGNSLKRS KSIRPPQSPP QNCSRSNCKI S
