RBGPR_MOUSE
ID RBGPR_MOUSE Reviewed; 1366 AA.
AC Q8BMG7; Q6PEU0; Q80TQ6; Q8BX72;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
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; Synonyms=Kiaa0839;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 319-1366 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Forelimb;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-1366 (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 432-1364 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). Interacts with LMAN1 (By
CC similarity). {ECO:0000250|UniProtKB:Q5U1Z0,
CC ECO:0000250|UniProtKB:Q9H2M9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In neurons, it is
CC enriched in the synaptic soluble fraction. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BMG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BMG7-2; Sequence=VSP_013313;
CC -!- SIMILARITY: Belongs to the Rab3-GAP regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57872.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27296.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65667.2; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AK031191; BAC27296.1; ALT_INIT; mRNA.
DR EMBL; AK048759; BAC33447.1; -; mRNA.
DR EMBL; AC129195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057872; AAH57872.1; ALT_INIT; mRNA.
DR EMBL; AK122385; BAC65667.2; ALT_SEQ; Transcribed_RNA.
DR RefSeq; NP_001157226.1; NM_001163754.1.
DR AlphaFoldDB; Q8BMG7; -.
DR BioGRID; 221114; 4.
DR IntAct; Q8BMG7; 1.
DR STRING; 10090.ENSMUSP00000066325; -.
DR GlyConnect; 2664; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BMG7; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BMG7; -.
DR PhosphoSitePlus; Q8BMG7; -.
DR EPD; Q8BMG7; -.
DR jPOST; Q8BMG7; -.
DR MaxQB; Q8BMG7; -.
DR PaxDb; Q8BMG7; -.
DR PeptideAtlas; Q8BMG7; -.
DR PRIDE; Q8BMG7; -.
DR ProteomicsDB; 255118; -. [Q8BMG7-1]
DR ProteomicsDB; 255119; -. [Q8BMG7-2]
DR GeneID; 98732; -.
DR KEGG; mmu:98732; -.
DR CTD; 25782; -.
DR MGI; MGI:1916043; Rab3gap2.
DR eggNOG; KOG2727; Eukaryota.
DR InParanoid; Q8BMG7; -.
DR OrthoDB; 790713at2759; -.
DR PhylomeDB; Q8BMG7; -.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 98732; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rab3gap2; mouse.
DR PRO; PR:Q8BMG7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BMG7; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030234; F:enzyme regulator activity; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISO:MGI.
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:MGI.
DR GO; GO:1903061; P:positive regulation of protein lipidation; ISS:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS: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 Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1366
FT /note="Rab3 GTPase-activating protein non-catalytic
FT subunit"
FT /id="PRO_0000191663"
FT REGION 30..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 VAR_SEQ 1..1068
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013313"
FT CONFLICT 727
FT /note="I -> V (in Ref. 1; BAC27296)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="K -> E (in Ref. 1; BAC27296 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="E -> V (in Ref. 1; BAC27296 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="S -> T (in Ref. 3; AAH57872)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="Q -> H (in Ref. 3; AAH57872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1366 AA; 152535 MW; A84C2C1416F673BA CRC64;
MACSIVQFCS FQDLQSARDF LFPHLREETP GALKRDPSKT SSWEDDSWGA WEETEPREPE
EEGNTSKTQK NSWLQECVLS LSPTSDLMVI AREQKAAFLV RKWKHGDKGK EEMQFAVGWS
GSVSAEEGEY VTSALCIPLA SQKRSSTGRP DWTCIVVGFT SGYVRFYTEG VLLLAQLLNE
DKVLQLKCRT YEIPRHPGVT EQNEELSILY PAAIVTIDGF SLFQSLRACR NQVAKAAASG
NENIQPPPLA YKKWGLQDID TIIDHASVGI MTLSPFDQMK TASNIGGFNA AIKNSPPAMS
QYITVGSSPF TGFFYALEGS TQPLLSHVAL AVASKLTSAL FSAASGWLGW KSKHEEDTVQ
KQKPKMEPAT PLAVRFGLPD SRRHGESICL SPCNTLAAVT DDFGRVILLD VARGIAIRMW
KGYRDAQVGW IQIVEDLHER VPEKGGFSPF GNTQGPSRVA QFLVIYAPRR GILEVWNTQQ
GPRVGAFNVG KHCRLLYPGY KIMGLNNVTS QSWQPQTYQI CLVDPVSASV KAVNVPFHLA
LSDKKSERAK DLHLVKKLSA LLRAKSPRPD SFETEIKELI LDIKYPATKK QALESILASD
RLSFSCLRNV TQTLMDTLKN QELESVDEGL LQFCASKLKL LHLYESVSQL NTLDFHSDTP
FSDNDLAVLL RLDDKELLKL RALLEKYKQE NTKATVRFSE DADRVLPVKT FLEYLEYEKD
ALSIRKIGEE ECVALGSFFF WKCLHGKSST EEMCHSLESA GLSPQQLLSL LLSVWLSKEK
DILDKPQSVC CLHTMLSLLS KMKVAIDETW DSQSVSPWWQ QMRMACIQSE NSGAALLSAH
VGHSVAAQMS SGATDKKFSQ MELDADAEAL TDSWEALSLD TEYWKLLLRQ LEDCLILQTL
LHSKLSPPAA KAPSLQSEPL PRLSVKKLLE GGKGGIADSV AKWIFKQDLS PELLKCANKE
RDVENPDEPR EDLLHLAYEQ FPCSLELDVL HAHCCWEYVV QWNKDPEEAR FLVRSIEHLK
QILNPHVQNG IALMMWNTFL VKRFSAATYL MDKVGKSPKD RLCRRDVGMS DTALTSFLGS
CLELLQTSLE ADISRDEVQV PVLDTEDAWL SVEGPISIVE LALEQKPIHY PLVEHHSVLC
SILYASMRFS LKSVKPLALF DSKGKNAFFK DLTSIQLLPS GEMDPNFISV RQQFLLKVVS
AAVQAQHSKD KDPSAEAANT HWKDLNWPGL AVDLAHHLQV SDDVIRRHYV GELYSHGADL
LGEEAIFQVQ DKEVLASQLL VLTGQRLAHA LFHTQTKEGM ELLARLPPTL CTWLKAMNPQ
DLQNTGVPIA ATAKLVHKVM ELLPEKHGQY SLALHLIDAV EAMATL
