RB40A_HUMAN
ID RB40A_HUMAN Reviewed; 277 AA.
AC Q8WXH6; O00407; Q17RQ5; Q6DK06; Q8TF06;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ras-related protein Rab-40A;
DE AltName: Full=SOCS box-containing protein RAR2A;
DE Short=Protein Rar-2;
DE Flags: Precursor;
GN Name=RAB40A;
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].
RA Zhou Y., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Homo sapiens Rar protein.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kile B.T., Hilton D.J., Nicola N.A.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16923123; DOI=10.1111/j.1365-2443.2006.00997.x;
RA Itoh T., Satoh M., Kanno E., Fukuda M.;
RT "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing
RT proteins based on their Rab-binding activity.";
RL Genes Cells 11:1023-1037(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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).
CC -!- FUNCTION: May be a 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:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
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; AF132748; AAL75949.1; -; mRNA.
DR EMBL; AF422143; AAL60514.1; -; mRNA.
DR EMBL; AB232637; BAF02899.1; -; mRNA.
DR EMBL; Z69733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074854; AAH74854.1; -; mRNA.
DR EMBL; BC074855; AAH74855.1; -; mRNA.
DR EMBL; BC113501; AAI13502.1; -; mRNA.
DR EMBL; BC117232; AAI17233.1; -; mRNA.
DR CCDS; CCDS35357.1; -.
DR RefSeq; NP_543155.2; NM_080879.2.
DR RefSeq; XP_005262140.1; XM_005262083.4.
DR RefSeq; XP_011529174.1; XM_011530872.2.
DR AlphaFoldDB; Q8WXH6; -.
DR SMR; Q8WXH6; -.
DR BioGRID; 126773; 22.
DR IntAct; Q8WXH6; 7.
DR MINT; Q8WXH6; -.
DR STRING; 9606.ENSP00000361716; -.
DR iPTMnet; Q8WXH6; -.
DR PhosphoSitePlus; Q8WXH6; -.
DR BioMuta; RAB40A; -.
DR DMDM; 83287759; -.
DR MassIVE; Q8WXH6; -.
DR PaxDb; Q8WXH6; -.
DR PeptideAtlas; Q8WXH6; -.
DR PRIDE; Q8WXH6; -.
DR Antibodypedia; 29065; 129 antibodies from 23 providers.
DR DNASU; 142684; -.
DR Ensembl; ENST00000304236.2; ENSP00000305648.1; ENSG00000172476.4.
DR Ensembl; ENST00000372633.1; ENSP00000361716.1; ENSG00000172476.4.
DR GeneID; 142684; -.
DR KEGG; hsa:142684; -.
DR MANE-Select; ENST00000304236.2; ENSP00000305648.1; NM_080879.3; NP_543155.2.
DR UCSC; uc004ekk.4; human.
DR CTD; 142684; -.
DR DisGeNET; 142684; -.
DR GeneCards; RAB40A; -.
DR HGNC; HGNC:18283; RAB40A.
DR HPA; ENSG00000172476; Tissue enhanced (epididymis).
DR MIM; 301065; gene.
DR neXtProt; NX_Q8WXH6; -.
DR OpenTargets; ENSG00000172476; -.
DR PharmGKB; PA34137; -.
DR VEuPathDB; HostDB:ENSG00000172476; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000167159; -.
DR HOGENOM; CLU_041217_11_0_1; -.
DR InParanoid; Q8WXH6; -.
DR OMA; HRMNCFG; -.
DR OrthoDB; 1065856at2759; -.
DR PhylomeDB; Q8WXH6; -.
DR TreeFam; TF323230; -.
DR PathwayCommons; Q8WXH6; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q8WXH6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 142684; 16 hits in 627 CRISPR screens.
DR GeneWiki; RAB40A; -.
DR GenomeRNAi; 142684; -.
DR Pharos; Q8WXH6; Tbio.
DR PRO; PR:Q8WXH6; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8WXH6; protein.
DR Bgee; ENSG00000172476; Expressed in corpus epididymis and 97 other tissues.
DR Genevisible; Q8WXH6; 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 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..274
FT /note="Ras-related protein Rab-40A"
FT /id="PRO_0000121257"
FT PROPEP 275..277
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370830"
FT DOMAIN 175..228
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
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 MOD_RES 274
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 269
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 274
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 45
FT /note="H -> L (in dbSNP:rs1180895)"
FT /id="VAR_034435"
FT CONFLICT 250
FT /note="K -> KR (in Ref. 2; AAL60514)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="E -> K (in Ref. 2; AAL60514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31076 MW; EB00BFF4E56A8577 CRC64;
MSAPGSPDQA YDFLLKFLLV GDRDVGKSEI LESLQDGAAE SPYSHLGGID YKTTTILLDG
QRVKLKLWDT SGQGRFCTIF RSYSRGAQGV ILVYDIANRW SFEGMDRWIK KIEEHAPGVP
KILVGNRLHL AFKRQVPREQ AQAYAERLGV TFFEVSPLCN FNIIESFTEL ARIVLLRHRM
NWLGRPSKVL SLQDLCCRTI VSCTPVHLVD KLPLPSTLRS HLKSFSMAKG LNARMMRGLS
YSLTTSSTHK SSLCKVEIVC PPQSPPKNCT RNSCKIS
