RAB3B_BOVIN
ID RAB3B_BOVIN Reviewed; 219 AA.
AC P10948; Q0IIB4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ras-related protein Rab-3B;
DE AltName: Full=SMG P25B;
GN Name=RAB3B;
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 (AUG-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. The GTP-bound
CC form interacts with GAS8/DRC4 (via coiled-coil domains) (By
CC similarity). Interacts with GDI2, CHM and CHML; phosphorylation at Thr-
CC 86 disrupts these interactions (By similarity). Interacts with MADD
CC (via uDENN domain); the GTP-bound form is preferred for interaction (By
CC similarity). {ECO:0000250|UniProtKB:P20337,
CC ECO:0000250|UniProtKB:Q9CZT8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9CZT8}. Note=Colocalizes with GAS8/DRC4 in the
CC Golgi apparatus. {ECO:0000250|UniProtKB:Q9CZT8}.
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:P20337}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M19886; AAA30417.1; -; mRNA.
DR EMBL; BC122723; AAI22724.1; -; mRNA.
DR PIR; B29224; B29224.
DR RefSeq; NP_776872.1; NM_174447.4.
DR AlphaFoldDB; P10948; -.
DR SMR; P10948; -.
DR STRING; 9913.ENSBTAP00000007019; -.
DR PaxDb; P10948; -.
DR PRIDE; P10948; -.
DR Ensembl; ENSBTAT00000007019; ENSBTAP00000007019; ENSBTAG00000005337.
DR GeneID; 282030; -.
DR KEGG; bta:282030; -.
DR CTD; 5865; -.
DR VEuPathDB; HostDB:ENSBTAG00000005337; -.
DR VGNC; VGNC:33650; RAB3B.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000159943; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P10948; -.
DR OMA; AICEKMS; -.
DR OrthoDB; 1426655at2759; -.
DR TreeFam; TF313199; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000005337; Expressed in omental fat pad and 70 other tissues.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0098691; C:dopaminergic synapse; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0051586; P:positive regulation of dopamine uptake involved in synaptic transmission; 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:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
DR GO; GO:0097494; P:regulation of vesicle size; IEA:Ensembl.
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 Acetylation; Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT CHAIN 2..219
FT /note="Ras-related protein Rab-3B"
FT /id="PRO_0000121080"
FT MOTIF 51..59
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 29..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 48..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63012"
FT BINDING 77..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 165..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20337"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63941"
FT MOD_RES 219
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 217
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 219 AA; 24766 MW; C5D45F40BBE4ACAD CRC64;
MASVTDGKAG VKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA FVSTVGIDFK
VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWATQI
KTYSWDNAQV ILVGNKCDME EERVVPTEKG RLLAEQLGFD FFEASAKENI SVRQAFERLV
DAICDKMSDT LDTDPSLLGT SKNTRLSDTP PLLQQNCSC
