RAB3C_RAT
ID RAB3C_RAT Reviewed; 227 AA.
AC P62824; Q62858; Q62974; Q63482; Q9CXQ1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein Rab-3C;
GN Name=Rab3c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Oho C., Nemoto Y., Omori A., Takahashi M.;
RT "Rab3C is associated with N-type Ca channel in rat brain.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pheochromocytoma;
RX PubMed=8885988; DOI=10.1006/bbrc.1996.1563;
RA Viggeswarapu M., Wildey G.M.;
RT "Cloning and tissue expression of the rat RAB 3C GTP-binding protein.";
RL Biochem. Biophys. Res. Commun. 227:645-650(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-218.
RC TISSUE=Brain;
RX PubMed=8841986;
RX DOI=10.1002/(sici)1097-4547(19960801)45:3<258::aid-jnr7>3.0.co;2-c;
RA Madison D.L., Krueger W.H., Kim T., Pfeiffer S.E.;
RT "Differential expression of rab3 isoforms in oligodendrocytes and
RT astrocytes.";
RL J. Neurosci. Res. 45:258-268(1996).
RN [4]
RP INTERACTION WITH RIMS1.
RX PubMed=9252191; DOI=10.1038/41580;
RA Wang Y., Okamoto M., Schmitz F., Hofmann K., Suedhof T.C.;
RT "Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion.";
RL Nature 388:593-598(1997).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RIMS2, RPH3A and RPH3AL (By similarity).
CC Interacts with RIMS1 (PubMed:9252191). Interacts with GDI2 and CHM;
CC phosphorylation at Thr-86 disrupts these interactions (By similarity).
CC Interacts with MADD (via uDENN domain); the GTP-bound form is preferred
CC for interaction (By similarity). {ECO:0000250|UniProtKB:P62823,
CC ECO:0000250|UniProtKB:Q96E17, ECO:0000269|PubMed:9252191}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM and
CC RAB GDP dissociation inhibitor GDI2. {ECO:0000250|UniProtKB:Q96E17}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; D78197; BAA11302.1; -; mRNA.
DR EMBL; U54807; AAC52879.1; -; mRNA.
DR EMBL; U37099; AAC52704.1; -; mRNA.
DR PIR; JC5066; JC5066.
DR RefSeq; NP_598220.1; NM_133536.2.
DR AlphaFoldDB; P62824; -.
DR SMR; P62824; -.
DR BioGRID; 251075; 4.
DR IntAct; P62824; 2.
DR MINT; P62824; -.
DR STRING; 10116.ENSRNOP00000015871; -.
DR iPTMnet; P62824; -.
DR PhosphoSitePlus; P62824; -.
DR jPOST; P62824; -.
DR PaxDb; P62824; -.
DR PRIDE; P62824; -.
DR Ensembl; ENSRNOT00000116600; ENSRNOP00000096986; ENSRNOG00000011623.
DR GeneID; 171058; -.
DR KEGG; rno:171058; -.
DR CTD; 115827; -.
DR RGD; 620923; Rab3c.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000157368; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P62824; -.
DR OMA; WQKDASD; -.
DR OrthoDB; 1218073at2759; -.
DR PhylomeDB; P62824; -.
DR TreeFam; TF313199; -.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:P62824; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011623; Expressed in frontal cortex and 10 other tissues.
DR Genevisible; P62824; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR CDD; cd01865; Rab3; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037872; Rab3.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..227
FT /note="Ras-related protein Rab-3C"
FT /id="PRO_0000121087"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..67
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 37..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 56..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63012"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 173..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96E17"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63941"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20337"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62823"
FT MOD_RES 227
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 225
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 227
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 141
FT /note="A -> V (in Ref. 2; AAC52879)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..160
FT /note="QR -> RH (in Ref. 2; AAC52879)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="A -> G (in Ref. 2; AAC52879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25872 MW; 179DF4D9B451B7B0 CRC64;
MRHEAPMQMA SAQDARFGQK DSSDQNFDYM FKLLIIGNSS VGKTSFLFRY ADDSFTSAFV
STVGIDFKVK TVFKNEKRIK LQIWDTAGQE RYRTITTAYY RGAMGFILMY DITNEESFNA
VQDWSTQIKT YSWDNAQVIL AGNKCDMEDE RVVSTERGQR LGEQLGFEFF ETSAKDNINV
KQTFERLVDI ICDKMSESLE TDPAITAAKQ STRLKETPPP PQPNCGC
