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Ras-related protein Rab-3A

 RAB3A_HUMAN             Reviewed;         220 AA.
P20336; A8K0J4; Q9NYE1;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
12-SEP-2018, entry version 199.
RecName: Full=Ras-related protein Rab-3A;
Name=RAB3A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2501306;
Zahraoui A., Touchot N., Chardin P., Tavitian A.;
"The human Rab genes encode a family of GTP-binding proteins related
to yeast YPT1 and SEC4 products involved in secretion.";
J. Biol. Chem. 264:12394-12401(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10574328; DOI=10.1016/S0898-6568(99)00037-6;
Sullivan M., Olsen A.S., Houslay M.D.;
"Genomic organisation of the human cyclic AMP-specific
phosphodiesterase PDE4C gene and its chromosomal localisation to
19p13.1, between RAB3A and JUND.";
Cell. Signal. 11:735-742(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
Liu Y., Li J., He J.J.;
"Functional cloning and characterization of human fetal brain cDNAs.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
ISOPRENYLATION AT CYS-218 AND CYS-220, AND METHYLATION AT CYS-220.
PubMed=1648736; DOI=10.1073/pnas.88.14.6264;
Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R.,
Sinensky M., Balch W.E., Buss J.E., Der C.J.;
"Isoprenoid modification of rab proteins terminating in CC or CXC
motifs.";
Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
[10]
ISOPRENYLATION AT CYS-218 AND CYS-220, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=7991565; DOI=10.1073/pnas.91.25.11963;
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.;
"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of
adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.";
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994).
-!- FUNCTION: Involved in exocytosis by regulating a late step in
synaptic vesicle fusion. Could play a role in neurotransmitter
release by regulating membrane flow in the nerve terminal.
-!- SUBUNIT: Heterodimer with RIMS2. Part of a ternary complex
involving PCLO and EPAC2. Interacts with RPH3A and RPH3AL.
Interacts with the exocyst complex through SEC15. Binds SYTL4 and
RIMS1. Interacts with RAB3IP. Interacts with SGSM1 and SGSM3 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q96QF0:RAB3IP; NbExp=3; IntAct=EBI-1045943, EBI-747844;
P47224:RABIF; NbExp=7; IntAct=EBI-1045943, EBI-713992;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- TISSUE SPECIFICITY: Specifically expressed in brain.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; M28210; AAA60242.1; -; mRNA.
EMBL; AF157809; AAD46811.1; -; Genomic_DNA.
EMBL; AF157806; AAD46811.1; JOINED; Genomic_DNA.
EMBL; AF157807; AAD46811.1; JOINED; Genomic_DNA.
EMBL; AF157808; AAD46811.1; JOINED; Genomic_DNA.
EMBL; AF254795; AAF67748.1; -; mRNA.
EMBL; AF498931; AAM21079.1; -; mRNA.
EMBL; AK289559; BAF82248.1; -; mRNA.
EMBL; AC068499; AAF67385.1; -; Genomic_DNA.
EMBL; CH471106; EAW84672.1; -; Genomic_DNA.
EMBL; BC011782; AAH11782.1; -; mRNA.
CCDS; CCDS12372.1; -.
PIR; C34323; C34323.
RefSeq; NP_002857.1; NM_002866.4.
RefSeq; XP_011526466.1; XM_011528164.1.
UniGene; Hs.27744; -.
ProteinModelPortal; P20336; -.
SMR; P20336; -.
BioGrid; 111802; 39.
IntAct; P20336; 12.
MINT; P20336; -.
STRING; 9606.ENSP00000222256; -.
iPTMnet; P20336; -.
PhosphoSitePlus; P20336; -.
SwissPalm; P20336; -.
BioMuta; RAB3A; -.
DMDM; 131801; -.
EPD; P20336; -.
MaxQB; P20336; -.
PaxDb; P20336; -.
PeptideAtlas; P20336; -.
PRIDE; P20336; -.
ProteomicsDB; 53748; -.
DNASU; 5864; -.
Ensembl; ENST00000222256; ENSP00000222256; ENSG00000105649.
GeneID; 5864; -.
KEGG; hsa:5864; -.
UCSC; uc002nie.3; human.
CTD; 5864; -.
DisGeNET; 5864; -.
EuPathDB; HostDB:ENSG00000105649.9; -.
GeneCards; RAB3A; -.
HGNC; HGNC:9777; RAB3A.
HPA; CAB009949; -.
HPA; CAB078998; -.
HPA; HPA003160; -.
MIM; 179490; gene.
neXtProt; NX_P20336; -.
OpenTargets; ENSG00000105649; -.
PharmGKB; PA34132; -.
eggNOG; KOG0093; Eukaryota.
eggNOG; ENOG410ZZXQ; LUCA.
GeneTree; ENSGT00890000139330; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P20336; -.
KO; K07882; -.
OMA; QLTEQPA; -.
OrthoDB; EOG091G0J64; -.
PhylomeDB; P20336; -.
TreeFam; TF313199; -.
Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
SIGNOR; P20336; -.
GeneWiki; RAB3A; -.
GenomeRNAi; 5864; -.
PRO; PR:P20336; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105649; Expressed in 205 organ(s), highest expression level in anterior cingulate cortex.
CleanEx; HS_RAB3A; -.
ExpressionAtlas; P20336; baseline and differential.
Genevisible; P20336; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
GO; GO:0060201; C:clathrin-sculpted acetylcholine transport vesicle membrane; TAS:Reactome.
GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
GO; GO:0070083; C:clathrin-sculpted monoamine transport vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0051021; F:GDP-dissociation inhibitor binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0045054; P:constitutive secretory pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0061670; P:evoked neurotransmitter secretion; IEA:Ensembl.
GO; GO:0014047; P:glutamate secretion; TAS:Reactome.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0048790; P:maintenance of presynaptic active zone structure; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045921; P:positive regulation of exocytosis; TAS:ParkinsonsUK-UCL.
GO; GO:1903307; P:positive regulation of regulated secretory pathway; IMP:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0050975; P:sensory perception of touch; IEA:Ensembl.
GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:ParkinsonsUK-UCL.
GO; GO:0016188; P:synaptic vesicle maturation; IEA:Ensembl.
GO; GO:0036465; P:synaptic vesicle recycling; ISS:ParkinsonsUK-UCL.
CDD; cd01865; Rab3; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR037872; Rab3.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Exocytosis; GTP-binding;
Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Phosphoprotein; Prenylation; Protein transport; Reference proteome;
Transport.
CHAIN 1 220 Ras-related protein Rab-3A.
/FTId=PRO_0000121076.
NP_BIND 29 37 GTP. {ECO:0000250|UniProtKB:O95716}.
NP_BIND 48 54 GTP. {ECO:0000250|UniProtKB:P63012}.
NP_BIND 77 81 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 135 138 GTP. {ECO:0000250|UniProtKB:O95716}.
NP_BIND 165 167 GTP. {ECO:0000250|UniProtKB:O95716}.
MOTIF 51 59 Effector region. {ECO:0000250}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:P63011}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:P63011}.
MOD_RES 220 220 Cysteine methyl ester.
{ECO:0000269|PubMed:1648736}.
LIPID 218 218 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:1648736,
ECO:0000269|PubMed:7991565}.
LIPID 220 220 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:1648736,
ECO:0000269|PubMed:7991565}.
CONFLICT 70 70 R -> K (in Ref. 2; AAF67748).
{ECO:0000305}.
CONFLICT 180 180 V -> E (in Ref. 2; AAF67748).
{ECO:0000305}.
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


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