RAB3C_BOVIN
ID RAB3C_BOVIN Reviewed; 227 AA.
AC P10949; Q2KI25;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras-related protein Rab-3C;
DE AltName: Full=SMG P25C;
GN Name=RAB3C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3136152; DOI=10.1016/s0021-9258(18)37922-5;
RA Matsui Y., Kikuchi A., Kondo J., Hishida T., Teranishi Y., Takai Y.;
RT "Nucleotide and deduced amino acid sequences of a GTP-binding protein
RT family with molecular weights of 25,000 from bovine brain.";
RL J. Biol. Chem. 263:11071-11074(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL (By similarity).
CC Interacts with GDI2, CHM and CHML; phosphorylation at Thr-86 disrupts
CC these interactions (By similarity). Interacts with MADD (via uDENN
CC domain); the GTP-bound form is preferred for interaction (By
CC similarity). {ECO:0000250|UniProtKB:P62823,
CC ECO:0000250|UniProtKB:Q96E17}.
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,
CC CHML and RAB GDP dissociation inhibitor GDI2.
CC {ECO:0000250|UniProtKB:Q96E17}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30418.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M19887; AAA30418.1; ALT_INIT; mRNA.
DR EMBL; BC112795; AAI12796.1; -; mRNA.
DR PIR; C29224; C29224.
DR RefSeq; NP_001040071.1; NM_001046606.2.
DR AlphaFoldDB; P10949; -.
DR SMR; P10949; -.
DR STRING; 9913.ENSBTAP00000009611; -.
DR PaxDb; P10949; -.
DR PRIDE; P10949; -.
DR Ensembl; ENSBTAT00000009611; ENSBTAP00000009611; ENSBTAG00000007306.
DR GeneID; 338100; -.
DR KEGG; bta:338100; -.
DR CTD; 115827; -.
DR VEuPathDB; HostDB:ENSBTAG00000007306; -.
DR VGNC; VGNC:33651; RAB3C.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000157368; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P10949; -.
DR OMA; WQKDASD; -.
DR OrthoDB; 1218073at2759; -.
DR TreeFam; TF313199; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000007306; Expressed in oocyte and 48 other tissues.
DR ExpressionAtlas; P10949; baseline and differential.
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; IEA:Ensembl.
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:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IBA:GO_Central.
DR GO; GO:0019882; P:antigen processing and presentation; IEA:Ensembl.
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; IBA:GO_Central.
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 2: Evidence at transcript 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_0000121084"
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 126..129
FT /note="TQIK -> LNQ (in Ref. 1; AAA30418)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..157
FT /note="TER -> SEE (in Ref. 1; AAA30418)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> H (in Ref. 1; AAA30418)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="A -> P (in Ref. 1; AAA30418)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="Q -> H (in Ref. 1; AAA30418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25938 MW; 73574205DEFAC72D CRC64;
MRHEAPMQMA SAQDARYGQK DSSDQNFDYM FKLLIIGNSS VGKTSFLFRY ADDSFTSAFV
STVGIDFKVK TVFKNEKRIK LQIWDTAGQE RYRTITTAYY RGAMGFILMY DITNEESFNA
VQDWSTQIKT YSWDNAQVIL VGNKCDMEDE RVISTERGQH LGEQLGFEFF ETSAKDNINV
KQTFERLVDI ICDKMSESLE TDPAITAAKQ NTRLKETPPP PQPNCGC
