RBGPR_RAT
ID RBGPR_RAT Reviewed; 1386 AA.
AC Q5U1Z0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Rab3 GTPase-activating protein non-catalytic subunit;
DE AltName: Full=Rab3 GTPase-activating protein 150 kDa subunit;
DE AltName: Full=Rab3-GAP p150;
DE Short=Rab3-GAP150;
DE AltName: Full=Rab3-GAP regulatory subunit;
GN Name=Rab3gap2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [2]
RP PROTEIN SEQUENCE OF 41-54; 532-544 AND 1218-1229, FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1053-1386.
RC TISSUE=Ovary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-976, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulatory subunit of a GTPase activating protein that has
CC specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3
CC proteins are involved in regulated exocytosis of neurotransmitters and
CC hormones. Rab3 GTPase-activating complex specifically converts active
CC Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and
CC brain development. May participate in neurodevelopmental processes such
CC as proliferation, migration and differentiation before synapse
CC formation, and non-synaptic vesicular release of neurotransmitters.
CC {ECO:0000269|PubMed:9733780}.
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:Q9H2M9,
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 regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86380.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03085350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03089585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03089113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03089836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03089287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03087362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086380; AAH86380.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001035244.2; NM_001040154.2.
DR AlphaFoldDB; Q5U1Z0; -.
DR BioGRID; 252892; 2.
DR IntAct; Q5U1Z0; 1.
DR STRING; 10116.ENSRNOP00000003216; -.
DR iPTMnet; Q5U1Z0; -.
DR PhosphoSitePlus; Q5U1Z0; -.
DR jPOST; Q5U1Z0; -.
DR PaxDb; Q5U1Z0; -.
DR PeptideAtlas; Q5U1Z0; -.
DR PRIDE; Q5U1Z0; -.
DR GeneID; 289350; -.
DR KEGG; rno:289350; -.
DR CTD; 25782; -.
DR RGD; 1311518; Rab3gap2.
DR eggNOG; KOG2727; Eukaryota.
DR InParanoid; Q5U1Z0; -.
DR OrthoDB; 790713at2759; -.
DR PhylomeDB; Q5U1Z0; -.
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 PRO; PR:Q5U1Z0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1903061; P:positive regulation of protein lipidation; ISS:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR InterPro; IPR026059; Rab3GAP2.
DR InterPro; IPR029257; RAB3GAP2_C.
DR InterPro; IPR032839; RAB3GAP_N.
DR PANTHER; PTHR12472; PTHR12472; 1.
DR Pfam; PF14656; RAB3GAP2_C; 1.
DR Pfam; PF14655; RAB3GAP2_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1386
FT /note="Rab3 GTPase-activating protein non-catalytic
FT subunit"
FT /id="PRO_0000191664"
FT REGION 31..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMG7"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 899
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2M9"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2M9"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 1231
FT /note="K -> R (in Ref. 3; AAH86380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1386 AA; 154431 MW; B2C96FC7FEE56785 CRC64;
MACSIVQFCS FQDLQSARDF LFPQLREETP GALRRDPSKT SNWEDDSWGA WEETEPQEPE
EEGNTSKTQK HSWLQECVLS LSPTSDLMVI AREQKAAFLV RKWKHSDKGK EEMQFAVGWS
GSVSAEEGEY VTSALCIPLA SQKRSSTGRP DWTCIVVGFT SGYVRFYTEG VLLLAQLLNE
DRVLQLKCRT YEIPRHPGVT EQNEELSILY PAAIVTIDGF SLFQSLRACR NQVAKAAASG
NENIQPPPLA YKKWGLQDID TIIDHASIGI MTLSPFDQMK TASNIGGFNA AIKNSPPAMS
QYITVGSSPF TGFFYALEGS TQPLLSHVAL AVASKLTSAL FSAASGWLGW KSKHEEETVQ
KQKPKMEPAT PLAVRFGLPD SRRHGESICL SPCNTLAAVT DDFGRVILLD VARGIAIRMW
KGYRDAQIGW IQIVEDLHER VPEKGDFSPF GNTQGPSRVA QFLVIYAPRR GILEVWSTQQ
GPRVGAFNVG KHCRLLYPGY KIMGLNNVTS QSWQPQTYQI CLVDPVSASV KAVNVPFHLA
LSDKKSERAK DLHLVKKLAA LLRAKSPRPD SFEAEIKELI LDIKYPATKK QALESILASD
RVSFSCLRNV TQTSMDTLKN QELESVDEGL LQFCASKLKL LHLYESVSQL NTLDFHSDTP
FSDNDLAVLL RLDDKELLKL RALLEKYKQE NTKATVRFSE DADGVLPVKT FLEYLDYEKD
ALSIRKTSEE ECVALGSFFF WKCLHGESST EDMCHTLESA GLSPQQLLSL LLSVWLSKEK
DILDKPQSVC CLHTMLSLLS KMKVAIDETW DSQSVSPWWQ QMRMACIQSE NNGAALLSAH
VGHSVAAQMS SSATDKKFSQ MVLDADAEAL TDSWEALSLD TEYWKLLLRQ LEDCLILQTL
LHSRASPPAA KASSPQTEPL PRLSVKKLLE GGKGGIADSV AKWIFKQDLS PELLKCANRE
KDVENPDEPR EGIARSPPEV SEVETDLGAV PDLLRLAYEQ FPCSLELDVL HAHCCWEYVV
QWNKDPEEAR FLVRSIEHLR HILNPHVQNG ISLMMWNTFL VKRFSAATYL MDKVGKSPKD
RLCRRDVGMS DTALTSFLGS CLDLLQTSLE ADISRDEVQV PVLDTEDAWL SVEGPTSIVE
LALEQKPIHY PLVEHHSILC SILYAAMSFS LKSVKPLALF DSKGKNAFFK DLTSIQLLPS
GEMDPNFISV RQQFLLKVVS AAVQAQHSKD KDPSARAADT HGQDLNWTAL AVDLAHHLQV
SEDVIRRHYV GELYSYGADL LGEEAILQVQ DKEVLASQLL VLTGQRLAHA LFHTQTKEGM
ELLARLPPTL CTWLKAMNPQ DLQNTGVPVA ATAKLVHKVM ELLPEKHGQY SLALHLIEAV
EAMATL
