RAB3A_BOVIN
ID RAB3A_BOVIN Reviewed; 220 AA.
AC P11023; Q17QM2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ras-related protein Rab-3A;
DE AltName: Full=SMG P25A;
GN Name=RAB3A;
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], AND PARTIAL PROTEIN SEQUENCE.
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=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP ISOPRENYLATION AT CYS-218 AND CYS-220.
RX PubMed=1906176; DOI=10.1073/pnas.88.14.6196;
RA Farnsworth C.C., Kawata M., Yoshida Y., Takai Y., Gelb M.H., Glomset J.A.;
RT "C-terminus of the small GTP-binding protein smg p25A contains two
RT geranylgeranylated cysteine residues and a methyl ester.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6196-6200(1991).
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 SNCA (By similarity). Interacts with GDI1, GDI2, CHM and CHML;
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:P20336,
CC ECO:0000250|UniProtKB:P63011, 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 -!- TISSUE SPECIFICITY: Specifically expressed in brain.
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; M19885; AAA30416.1; -; mRNA.
DR EMBL; BC118278; AAI18279.1; -; mRNA.
DR PIR; A29224; A29224.
DR RefSeq; NP_776871.2; NM_174446.3.
DR AlphaFoldDB; P11023; -.
DR SMR; P11023; -.
DR CORUM; P11023; -.
DR STRING; 9913.ENSBTAP00000002783; -.
DR PaxDb; P11023; -.
DR PRIDE; P11023; -.
DR Ensembl; ENSBTAT00000014062; ENSBTAP00000014062; ENSBTAG00000010635.
DR GeneID; 282029; -.
DR KEGG; bta:282029; -.
DR CTD; 5864; -.
DR VEuPathDB; HostDB:ENSBTAG00000010635; -.
DR VGNC; VGNC:33649; RAB3A.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000158959; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P11023; -.
DR OrthoDB; 1426655at2759; -.
DR TreeFam; TF313199; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000010635; Expressed in Ammon's horn and 102 other tissues.
DR ExpressionAtlas; P11023; baseline.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0008021; C:synaptic vesicle; ISS:AgBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:AgBase.
DR GO; GO:0031489; F:myosin V binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISS:AgBase.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; ISS:AgBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; ISS:AgBase.
DR GO; GO:0007005; P:mitochondrion organization; ISS:AgBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISS:AgBase.
DR GO; GO:0009791; P:post-embryonic development; ISS:AgBase.
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; ISS:AgBase.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; ISS:AgBase.
DR GO; GO:0003016; P:respiratory system process; ISS:AgBase.
DR GO; GO:0051602; P:response to electrical stimulus; ISS:AgBase.
DR GO; GO:0050975; P:sensory perception of touch; ISS:AgBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:AgBase.
DR GO; GO:0016188; P:synaptic vesicle maturation; ISS:AgBase.
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 Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Exocytosis; GTP-binding; Lipoprotein; Lysosome;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..220
FT /note="Ras-related protein Rab-3A"
FT /id="PRO_0000121075"
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|UniProtKB:P20336"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1906176"
FT LIPID 220
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1906176"
FT CONFLICT 125
FT /note="W -> S (in Ref. 1; AAA30416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 24954 MW; B77FB461DC25E79E CRC64;
MASATDARYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI
KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV
DVICEKMSES LDTADPAVTG AKQGPQLTDQ QAPPHQDCAC
