ID   RAB3A_MOUSE             Reviewed;         220 AA.
AC   P63011; P05713; Q3TSL4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   11-JUN-2014, entry version 107.
DE   RecName: Full=Ras-related protein Rab-3A;
GN   Name=Rab3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7687127;
RA   Baumert M., Fischer von Mollard G., Jahn R., Suedhof T.C.;
RT   "Structure of the murine rab3A gene: correlation of genomic
RT   organization with antibody epitopes.";
RL   Biochem. J. 293:157-163(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 13-35; 42-60; 73-83; 122-136; 152-167 AND 179-202,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH RIMS2.
RX   PubMed=11056535; DOI=10.1038/35041046;
RA   Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H.,
RA   Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S.;
RT   "cAMP-GEFII is a direct target of cAMP in regulated exocytosis.";
RL   Nat. Cell Biol. 2:805-811(2000).
RN   [6]
RP   INTERACTION WITH RIMS1.
RX   PubMed=11431472; DOI=10.1074/jbc.M103337200;
RA   Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT   "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants
RT   partially related through N-terminal alpha-helix motifs.";
RL   J. Biol. Chem. 276:32480-32488(2001).
RN   [7]
RP   INTERACTION WITH RIMS2.
RX   PubMed=12401793; DOI=10.1074/jbc.M210146200;
RA   Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M.,
RA   Sasaki T., Tajima N., Iwanaga T., Seino S.;
RT   "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-
RT   GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis.";
RL   J. Biol. Chem. 277:50497-50502(2002).
RN   [8]
RP   INTERACTION WITH RIMS1; RIMS2; RPH3A AND RPH3AL.
RX   PubMed=12578829; DOI=10.1074/jbc.M212341200;
RA   Fukuda M.;
RT   "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT   Identification of a critical determinant of Rab3A/Rab27A recognition
RT   by Rim2.";
RL   J. Biol. Chem. 278:15373-15380(2003).
RN   [9]
RP   INTERACTION WITH SYTL4.
RX   PubMed=12590134; DOI=10.1074/jbc.M213090200;
RA   Fukuda M.;
RT   "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT   interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL   J. Biol. Chem. 278:15390-15396(2003).
RN   [10]
RP   INTERACTION WITH SGSM1 AND SGSM3.
RX   PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA   Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT   small G protein (RAP and RAB)-mediated signaling pathway.";
RL   Genomics 90:249-260(2007).
CC   -!- FUNCTION: Involved in exocytosis by regulating a late step in
CC       synaptic vesicle fusion. Could play a role in neurotransmitter
CC       release by regulating membrane flow in the nerve terminal (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer with RIMS2. Part of a ternary complex
CC       involving PCLO and EPAC2. Interacts with RPH3A and RPH3AL.
CC       Interacts with the exocyst complex through SEC15. Binds SYTL4,
CC       RIMS1 and RIMS2. Interacts with RAB3IP. Interacts with SGSM1 and
CC       SGSM3.
CC   -!- INTERACTION:
CC       P47708:Rph3a; NbExp=2; IntAct=EBI-398393, EBI-398376;
CC       Q8TDW5:SYTL5 (xeno); NbExp=2; IntAct=EBI-398393, EBI-2939487;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; X72966; CAA51470.1; -; Genomic_DNA.
DR   EMBL; AK005362; BAB23976.1; -; mRNA.
DR   EMBL; AK158727; BAE34630.1; -; mRNA.
DR   EMBL; AK161975; BAE36661.1; -; mRNA.
DR   EMBL; BC053519; AAH53519.1; -; mRNA.
DR   PIR; S34070; S34070.
DR   RefSeq; NP_001159871.1; NM_001166399.2.
DR   RefSeq; NP_033027.1; NM_009001.6.
DR   RefSeq; XP_006509665.1; XM_006509602.1.
DR   RefSeq; XP_006509666.1; XM_006509603.1.
DR   UniGene; Mm.5083; -.
DR   ProteinModelPortal; P63011; -.
DR   SMR; P63011; 18-186.
DR   BioGrid; 202544; 7.
DR   DIP; DIP-31051N; -.
DR   IntAct; P63011; 12.
DR   MINT; MINT-85820; -.
DR   PhosphoSite; P63011; -.
DR   MaxQB; P63011; -.
DR   PaxDb; P63011; -.
DR   PRIDE; P63011; -.
DR   Ensembl; ENSMUST00000034301; ENSMUSP00000034301; ENSMUSG00000031840.
DR   Ensembl; ENSMUST00000110090; ENSMUSP00000105717; ENSMUSG00000031840.
DR   Ensembl; ENSMUST00000110092; ENSMUSP00000105719; ENSMUSG00000031840.
DR   Ensembl; ENSMUST00000110093; ENSMUSP00000105720; ENSMUSG00000031840.
DR   GeneID; 19339; -.
DR   KEGG; mmu:19339; -.
DR   UCSC; uc009mbi.2; mouse.
DR   CTD; 5864; -.
DR   MGI; MGI:97843; Rab3a.
DR   eggNOG; COG1100; -.
DR   HOGENOM; HOG000233968; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P63011; -.
DR   KO; K07882; -.
DR   OMA; QLTEQPA; -.
DR   OrthoDB; EOG7JQBPC; -.
DR   PhylomeDB; P63011; -.
DR   TreeFam; TF313199; -.
DR   ChiTaRS; RAB3A; mouse.
DR   NextBio; 296339; -.
DR   PRO; PR:P63011; -.
DR   ArrayExpress; P63011; -.
DR   Bgee; P63011; -.
DR   CleanEx; MM_RAB3A; -.
DR   Genevestigator; P63011; -.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic membrane; IMP:MGI.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0051602; P:response to electrical stimulus; IMP:MGI.
DR   GO; GO:0050975; P:sensory perception of touch; IMP:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003579; Small_GTPase_Rab_type.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 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; Complete proteome; Direct protein sequencing;
KW   Exocytosis; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN         1    220       Ras-related protein Rab-3A.
FT                                /FTId=PRO_0000121078.
FT   NP_BIND      29     36       GTP (By similarity).
FT   NP_BIND      48     54       GTP (By similarity).
FT   NP_BIND      77     81       GTP (By similarity).
FT   NP_BIND     135    138       GTP (By similarity).
FT   MOTIF        51     59       Effector region (By similarity).
FT   MOD_RES     220    220       Cysteine methyl ester (By similarity).
FT   LIPID       218    218       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       220    220       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   220 AA;  24970 MW;  1A3E9F8C9D09EB40 CRC64;
     MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
     VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI
     KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV
     DVICEKMSES LDTADPAVTG AKQGPQLTDQ QAPPHQDCAC
//