RB3GP_RAT
ID RB3GP_RAT Reviewed; 775 AA.
AC P69735;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Rab3 GTPase-activating protein catalytic subunit;
DE AltName: Full=RAB3 GTPase-activating protein 130 kDa subunit;
DE AltName: Full=Rab3-GAP p130;
DE Short=Rab3-GAP;
DE Flags: Fragments;
GN Name=Rab3gap1; Synonyms=Rab3gap;
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 PROTEIN SEQUENCE OF 2-11; 161-171; 404-419 AND 539-557.
RC TISSUE=Brain;
RX PubMed=9030515; DOI=10.1074/jbc.272.8.4655;
RA Fukui K., Sasaki T., Imazumi K., Matsuura Y., Nakanishi H., Takai Y.;
RT "Isolation and characterization of a GTPase activating protein specific for
RT the Rab3 subfamily of small G proteins.";
RL J. Biol. Chem. 272:4655-4658(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 12-775.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9733780; DOI=10.1074/jbc.273.38.24781;
RA Nagano F., Sasaki T., Fukui K., Asakura T., Imazumi K., Takai Y.;
RT "Molecular cloning and characterization of the noncatalytic subunit of the
RT Rab3 subfamily-specific GTPase-activating protein.";
RL J. Biol. Chem. 273:24781-24785(1998).
RN [4]
RP INTERACTION WITH DMXL2.
RX PubMed=11809763; DOI=10.1074/jbc.c100730200;
RA Nagano F., Kawabe H., Nakanishi H., Shinohara M., Deguchi-Tawarada M.,
RA Takeuchi M., Sasaki T., Takai Y.;
RT "Rabconnectin-3, a novel protein that binds both GDP/GTP exchange protein
RT and GTPase-activating protein for Rab3 small G protein family.";
RL J. Biol. Chem. 277:9629-9632(2002).
CC -!- FUNCTION: Probable catalytic subunit of a GTPase activating protein
CC that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and
CC RAB3D). Rab3 proteins are involved in regulated exocytosis of
CC neurotransmitters and hormones. Specifically converts active Rab3-GTP
CC to the inactive form Rab3-GDP. Required for normal eye and brain
CC development. May participate in neurodevelopmental processes such as
CC proliferation, migration and differentiation before synapse formation,
CC and non-synaptic vesicular release of neurotransmitters.
CC -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed
CC of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex
CC interacts with DMXL2 (PubMed:11809763, PubMed:9733780). Interacts with
CC LMAN1 (By similarity). {ECO:0000250|UniProtKB:Q15042,
CC ECO:0000269|PubMed:11809763, ECO:0000269|PubMed:9733780}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9733780}. Note=In
CC neurons, it is enriched in the synaptic soluble fraction.
CC -!- SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.
CC {ECO:0000305}.
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DR EMBL; AABR03085327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P69735; -.
DR IntAct; P69735; 1.
DR STRING; 10116.ENSRNOP00000005289; -.
DR iPTMnet; P69735; -.
DR PhosphoSitePlus; P69735; -.
DR jPOST; P69735; -.
DR PaxDb; P69735; -.
DR PRIDE; P69735; -.
DR RGD; 1306487; Rab3gap1.
DR eggNOG; KOG2390; Eukaryota.
DR InParanoid; P69735; -.
DR PhylomeDB; P69735; -.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0021854; P:hypothalamus development; ISO:RGD.
DR GO; GO:0034389; P:lipid droplet organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:GO_Central.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0061646; P:positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:1903061; P:positive regulation of protein lipidation; ISS:GO_Central.
DR GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
DR InterPro; IPR045700; Rab3GAP1.
DR InterPro; IPR045698; Rab3GAP1_C.
DR InterPro; IPR026147; Rab3GAP1_conserved.
DR PANTHER; PTHR21422; PTHR21422; 1.
DR Pfam; PF19533; Rab3-GAP_cat_C; 1.
DR Pfam; PF13890; Rab3-GTPase_cat; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9030515"
FT CHAIN 2..775
FT /note="Rab3 GTPase-activating protein catalytic subunit"
FT /id="PRO_0000191657"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UJ7"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UJ7"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT NON_CONS 11..12
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 86587 MW; DF836260D18EC380 CRC64;
MAADSEPESE VGCPLTPLPP VSIAIRFTYV LQDWQQYFWP QQPPDIDALV GGEVGGLEFG
KLPFGACEDP ISELHLATTW PHLTEGIIVD NDVYSDLDPV QAPHWSVRVR KADNPQCLLG
DFVTEFLKIC RRKESTDEIL GRSTFEEEGR VADITHALSK LTEPAPVPIH KLSVSNMVHT
AKKKIRKHRG EESPLNNDVL NTILLFLFPD AASEKPLDGT TSVDNSNPAA EAGDYTLYNQ
FKSAPSDSLT YKLALCLCMI NFYHGGLKGV AHLWQEFVLE MRFRWENNFL IPGLASGPPD
LRCCLLHQKL QMLNCCIERK KARDEGKKTS PSDSMTKAYP ADAGKAGGQL GLDHLRDTEK
EKGEAGKSWD SWSDSEEEFF ECLSDAEDLR GNGQESTKKG GPKDMAPLKP EGRLHQHGKL
TLLRNGEPLY IPVTQEPAPM TEDLLEEQSE VLAKLGTSAE GAHLRARMQS ACLLSDMESF
KAANPGCCLE DFVRWYSPRD YIEEEVTDEK GNVVLKGELS ARMKIPSNMW VEAWETAKPV
PARRQRRLFD DTREAEKVLH YLAMQKPADL ARHLLPCVIH AAVLKVKEEE SLENIPSVKK
IIKQIIAHSS KVLRFPSPED KKLEEIILQI TTVEAIIARA RSLKAKFGTE KCEHEEEKED
LERFVSCLLE QPEVAVTGAG RGHAGRIIHK LFVNAQRAAA VALPEEELKR SGCPEERRQT
LVSDFPPPAG RELILRATVP RPAPYSKALP QRMYSVLTKE DFRLAGAFSS DTSFF
