RAB3A_MACFA
ID RAB3A_MACFA Reviewed; 220 AA.
AC Q4R4R9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ras-related protein Rab-3A;
GN Name=RAB3A; ORFNames=QflA-12931;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small GTP-binding protein that plays a central role in
CC regulated exocytosis and secretion. Controls the recruitment, tethering
CC and docking of secretory vesicles to the plasma membrane (By
CC similarity). Upon stimulation, switches to its active GTP-bound form,
CC cycles to vesicles and recruits effectors such as RIMS1, RIMS2,
CC Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules
CC onto the plasma membrane (By similarity). Upon GTP hydrolysis by
CC GTPase-activating protein, dissociates from the vesicle membrane
CC allowing the exocytosis to proceed (By similarity). Stimulates insulin
CC secretion through interaction with RIMS2 or RPH3AL effectors in
CC pancreatic beta cells (By similarity). Regulates calcium-dependent
CC lysosome exocytosis and plasma membrane repair (PMR) via the
CC interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (By similarity).
CC Acts as a positive regulator of acrosome content secretion in sperm
CC cells by interacting with RIMS1 (By similarity). Also plays a role in
CC the regulation of dopamine release by interacting with synaptotagmin
CC I/SYT (By similarity). {ECO:0000250|UniProtKB:P20336,
CC ECO:0000250|UniProtKB:P63011, ECO:0000250|UniProtKB:P63012}.
CC -!- SUBUNIT: Interacts with RIMS1 and RIMS2 (By similarity). Interacts with
CC Rabphilin-3A/RPH3A and Rab effector Noc2/RPH3AL (By similarity).
CC Interacts with SYTL4 (By similarity). Interacts with RAB3IP (By
CC similarity). Interacts with SGSM1 and SGSM3 (By similarity). Interacts
CC with SYT1 (By similarity). Interacts with MYH9; this interaction is
CC essential for lysosome exocytosis and plasma membrane repair (By
CC similarity). Interacts with STXBP1; this interaction promotes RAB3A
CC dissociation from the vesicle membrane (By similarity). Interacts with
CC GDI1, GDI2, CHM and CHML; phosphorylation at Thr-86 disrupts these
CC interactions (By similarity). Interacts with MADD (via uDENN domain);
CC the GTP-bound form is preferred for interaction (By similarity).
CC {ECO:0000250|UniProtKB:P20336, ECO:0000250|UniProtKB:P63011,
CC ECO:0000250|UniProtKB:P63012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P63012}. Lysosome
CC {ECO:0000250|UniProtKB:P20336}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:P63012}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P63011}. Cell membrane {ECO:0000305}; Lipid-
CC anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Presynapse
CC {ECO:0000250|UniProtKB:P63011}. Postsynapse
CC {ECO:0000250|UniProtKB:P63011}. Note=Cycles between a vesicle-
CC associated GTP-bound form and a cytosolic GDP-bound form.
CC {ECO:0000250|UniProtKB:P63012}.
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 inhibitors GDI1 and GDI2.
CC {ECO:0000250|UniProtKB:P20336}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB169825; BAE01906.1; -; mRNA.
DR RefSeq; NP_001270908.1; NM_001283979.1.
DR AlphaFoldDB; Q4R4R9; -.
DR SMR; Q4R4R9; -.
DR STRING; 9541.XP_005588484.1; -.
DR Ensembl; ENSMFAT00000065781; ENSMFAP00000015259; ENSMFAG00000030826.
DR GeneID; 101865846; -.
DR CTD; 5864; -.
DR VEuPathDB; HostDB:ENSMFAG00000030826; -.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000158959; -.
DR OMA; KECTDNI; -.
DR OrthoDB; 1426655at2759; -.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000030826; Expressed in frontal cortex and 6 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Cell projection; Cytoplasm; Cytoplasmic vesicle; Exocytosis;
KW GTP-binding; Lipoprotein; Lysosome; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..220
FT /note="Ras-related protein Rab-3A"
FT /id="PRO_0000121077"
FT REGION 194..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20336"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63011"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63011"
FT MOD_RES 220
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 220
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 24984 MW; 08B59F8C9BD2EB40 CRC64;
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI
KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV
DVICEKMSES LDTADPAVTG AKQGPQLSDQ QVPPHQDCAC
