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   24-JAN-2024, entry version 153.
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; 10116-ENSRNOP00000015871; -.
DR   Ensembl; ENSRNOT00000116600.1; ENSRNOP00000096986.1; ENSRNOG00000011623.7.
DR   Ensembl; ENSRNOT00055019886; ENSRNOP00055016035; ENSRNOG00055011684.
DR   Ensembl; ENSRNOT00055019889; ENSRNOP00055016037; ENSRNOG00055011684.
DR   Ensembl; ENSRNOT00060006420; ENSRNOP00060004808; ENSRNOG00060003825.
DR   Ensembl; ENSRNOT00060006425; ENSRNOP00060004812; ENSRNOG00060003825.
DR   Ensembl; ENSRNOT00065033273; ENSRNOP00065026632; ENSRNOG00065019722.
DR   Ensembl; ENSRNOT00065033279; ENSRNOP00065026636; ENSRNOG00065019722.
DR   GeneID; 171058; -.
DR   KEGG; rno:171058; -.
DR   AGR; RGD:620923; -.
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; PSSQCNC; -.
DR   OrthoDB; 8685at2759; -.
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 cell types or tissues.
DR   GO; GO:0005768; C:endosome; 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:0030672; C:synaptic vesicle membrane; IDA:SynGO.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037872; Rab3.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 1.
DR   PANTHER; PTHR47980:SF15; RAS-RELATED PROTEIN RAB-3C; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; P62824; RN.
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
//