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   02-SEP-2026, entry version 162.
DE   RecName: Full=Ras-related protein Rab-3C;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P10949};
GN   Name=Rab3c {ECO:0000312|RGD:620923};
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: The small GTPases Rab are key regulators of intracellular
CC       membrane trafficking, from the formation of transport vesicles to their
CC       fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC       and an active GTP-bound form that is able to recruit to membranes
CC       different sets of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion.
CC       {ECO:0000250|UniProtKB:P10949}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P10949};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P10949};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P10949};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP. Regulated
CC       by GTPase activating proteins (GAPs) which increase the GTP hydrolysis
CC       activity. Inhibited by GDP dissociation inhibitors (GDIs) which prevent
CC       Rab-GDP dissociation. {ECO:0000250|UniProtKB:P20336}.
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   -!- DOMAIN: Switch 1, switch 2 and the interswitch regions are
CC       characteristic of Rab GTPases and mediate the interactions with Rab
CC       downstream effectors. The switch regions undergo conformational changes
CC       upon nucleotide binding which drives interaction with specific sets of
CC       effector proteins, with most effectors only binding to GTP-bound Rab.
CC       {ECO:0000250|UniProtKB:P10949}.
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_598220.2; NM_133536.3.
DR   RefSeq; XP_038957541.1; XM_039101613.2.
DR   AlphaFoldDB; P62824; -.
DR   SMR; P62824; -.
DR   BioGRID; 251075; 5.
DR   FunCoup; P62824; 1420.
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; ENSRNOT00000116600.2; ENSRNOP00000096986.1; ENSRNOG00000011623.8.
DR   Ensembl; ENSRNOT00000170596.1; ENSRNOP00000104946.1; ENSRNOG00000011623.8.
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; FDMEDER; -.
DR   OrthoDB; 9989112at2759; -.
DR   PhylomeDB; P62824; -.
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   ExpressionAtlas; P62824; baseline and differential.
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:0003925; F:G protein activity; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR   GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
DR   CDD; cd01865; Rab3; 1.
DR   FunFam; 3.40.50.300:FF:000206; Ras-related protein Rab-3C; 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.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR050305; Small_GTPase_Rab.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 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.
PE   1: Evidence at protein level;
KW   Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; 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           53..66
FT                   /note="Switch 1"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   MOTIF           86..104
FT                   /note="Switch 2"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   COMPBIAS        217..227
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         42
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         43
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         44
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         175
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
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
//