RAB3B_RAT
ID RAB3B_RAT Reviewed; 219 AA.
AC Q63941;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ras-related protein Rab-3B;
GN Name=Rab3b;
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=Epididymis;
RX PubMed=9245721; DOI=10.1006/bbrc.1997.7039;
RA Klengel R., Piiper A., Pittelkow S., Zeuzem S.;
RT "Differential expression of Rab3 isoforms during differentiation of
RT pancreatic acinar cell line AR42J.";
RL Biochem. Biophys. Res. Commun. 236:719-722(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-82.
RC TISSUE=Mast cell;
RX PubMed=7508866; DOI=10.1016/0014-5793(94)80409-5;
RA Oberhauser A.F., Balan V., Fernandez-Badilla C.L., Fernandez J.M.;
RT "RT-PCR cloning of Rab3 isoforms expressed in peritoneal mast cells.";
RL FEBS Lett. 339:171-174(1994).
RN [3]
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).
RN [4]
RP INTERACTION WITH RIMS2.
RX PubMed=10748113; DOI=10.1074/jbc.m909008199;
RA Wang Y., Sugita S., Suedhof T.C.;
RT "The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3
RT and a new class of Src homology 3 domain proteins.";
RL J. Biol. Chem. 275:20033-20044(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RPH3A and RPH3AL (By similarity). Interacts
CC with RIMS1 (PubMed:9252191). Interacts with RIMS2 (PubMed:10748113).
CC The GTP-bound form interacts with GAS8/DRC4 (via coiled-coil domains)
CC (By similarity). Interacts with GDI2, and CHM; 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, ECO:0000269|PubMed:10748113,
CC ECO:0000269|PubMed:9252191}.
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 and
CC RAB GDP dissociation inhibitor GDI2. {ECO:0000250|UniProtKB:P20337}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Y14019; CAA74341.1; -; mRNA.
DR EMBL; S68807; AAB29894.1; -; mRNA.
DR PIR; I53485; I53485.
DR RefSeq; NP_112353.1; NM_031091.2.
DR AlphaFoldDB; Q63941; -.
DR SMR; Q63941; -.
DR BioGRID; 249627; 1.
DR IntAct; Q63941; 1.
DR MINT; Q63941; -.
DR STRING; 10116.ENSRNOP00000010645; -.
DR iPTMnet; Q63941; -.
DR PhosphoSitePlus; Q63941; -.
DR jPOST; Q63941; -.
DR PaxDb; Q63941; -.
DR PRIDE; Q63941; -.
DR GeneID; 81755; -.
DR KEGG; rno:81755; -.
DR CTD; 5865; -.
DR RGD; 620922; Rab3b.
DR VEuPathDB; HostDB:ENSRNOG00000008001; -.
DR eggNOG; KOG0093; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q63941; -.
DR OMA; AICEKMS; -.
DR PhylomeDB; Q63941; -.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:Q63941; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008001; Expressed in heart and 17 other tissues.
DR Genevisible; Q63941; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
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; 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:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; NAS:RGD.
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:0018125; P:peptidyl-cysteine methylation; ISO:RGD.
DR GO; GO:0051586; P:positive regulation of dopamine uptake involved in synaptic transmission; 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:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:0097494; P:regulation of vesicle size; 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 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_0000121083"
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:0007744|PubMed:22673903"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 24785 MW; E68ACC0C2D552F67 CRC64;
MASVTDGNTG IRDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA FVSTVGIDFK
VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWATQI
KTYSWDNAQV ILVGNKCDME EERVIPTEKG RLLAEQLGFD FFEASAKENI SVRQAFERLV
DAICDKMSDS MDTDPSVLGA SKTTRLSDTP PLLQQNCSC
