RB3GP_MOUSE
ID RB3GP_MOUSE Reviewed; 981 AA.
AC Q80UJ7; Q3TPB6; Q6A0D7; Q8C4Y0; Q8C679; Q8C6A5; Q8K324;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 134.
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;
GN Name=Rab3gap1; Synonyms=Kiaa0066, Rab3gap;
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].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Heart, and Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/NJ; 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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15696165; DOI=10.1038/ng1517;
RA Aligianis I.A., Johnson C.A., Gissen P., Chen D., Hampshire D.,
RA Hoffmann K., Maina E.N., Morgan N.V., Tee L., Morton J., Ainsworth J.R.,
RA Horn D., Rosser E., Cole T.R.P., Stolte-Dijkstra I., Fieggen K.,
RA Clayton-Smith J., Megarbane A., Shield J.P., Newbury-Ecob R., Dobyns W.B.,
RA Graham J.M., Kjaer K.W., Warburg M., Bond J., Trembath R.C., Harris L.W.,
RA Takai Y., Mundlos S., Tannahill D., Woods C.G., Maher E.R.;
RT "Mutations of the catalytic subunit of RAB3GAP cause Warburg Micro
RT syndrome.";
RL Nat. Genet. 37:221-223(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-579 AND SER-581, 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: 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 (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. Interacts with LMAN1.
CC {ECO:0000250|UniProtKB:P69735, ECO:0000250|UniProtKB:Q15042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In neurons, it is
CC enriched in the synaptic soluble fraction. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the eye, it is highly expressed within the lens,
CC particularly in the anterior lens epithelium and in a ring
CC corresponding to the equatorial region where anterior cells are
CC differentiating into lens fibers. Also highly expressed in the retina.
CC {ECO:0000269|PubMed:15696165}.
CC -!- DEVELOPMENTAL STAGE: From 10 dpc to 12 dpc, it is weakly expressed
CC throughout the embryo. At 14.5 dpc, it is predominantly expressed in a
CC number of organ systems, including the central and peripheral nervous
CC systems. {ECO:0000269|PubMed:15696165}.
CC -!- SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172881; BAD32159.1; ALT_INIT; mRNA.
DR EMBL; AK076244; BAC36271.1; -; mRNA.
DR EMBL; AK076399; BAC36323.1; -; mRNA.
DR EMBL; AK080432; BAC37915.1; -; mRNA.
DR EMBL; AK164523; BAE37821.1; -; mRNA.
DR EMBL; BC028996; AAH28996.1; -; mRNA.
DR EMBL; BC046297; AAH46297.1; -; mRNA.
DR CCDS; CCDS15249.1; -.
DR RefSeq; NP_848805.2; NM_178690.4.
DR AlphaFoldDB; Q80UJ7; -.
DR BioGRID; 230504; 12.
DR IntAct; Q80UJ7; 6.
DR STRING; 10090.ENSMUSP00000042070; -.
DR iPTMnet; Q80UJ7; -.
DR PhosphoSitePlus; Q80UJ7; -.
DR SwissPalm; Q80UJ7; -.
DR EPD; Q80UJ7; -.
DR jPOST; Q80UJ7; -.
DR MaxQB; Q80UJ7; -.
DR PaxDb; Q80UJ7; -.
DR PeptideAtlas; Q80UJ7; -.
DR PRIDE; Q80UJ7; -.
DR ProteomicsDB; 300249; -.
DR Antibodypedia; 33565; 183 antibodies from 29 providers.
DR DNASU; 226407; -.
DR Ensembl; ENSMUST00000037649; ENSMUSP00000042070; ENSMUSG00000036104.
DR GeneID; 226407; -.
DR KEGG; mmu:226407; -.
DR UCSC; uc007clc.2; mouse.
DR CTD; 22930; -.
DR MGI; MGI:2445001; Rab3gap1.
DR VEuPathDB; HostDB:ENSMUSG00000036104; -.
DR eggNOG; KOG2390; Eukaryota.
DR GeneTree; ENSGT00390000006705; -.
DR HOGENOM; CLU_012561_1_0_1; -.
DR InParanoid; Q80UJ7; -.
DR OMA; IMTEDMH; -.
DR PhylomeDB; Q80UJ7; -.
DR TreeFam; TF314500; -.
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; 226407; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rab3gap1; mouse.
DR PRO; PR:Q80UJ7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80UJ7; protein.
DR Bgee; ENSMUSG00000036104; Expressed in interventricular septum and 224 other tissues.
DR ExpressionAtlas; Q80UJ7; baseline and differential.
DR Genevisible; Q80UJ7; MM.
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; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0043010; P:camera-type eye development; ISO:MGI.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:ParkinsonsUK-UCL.
DR GO; GO:0060325; P:face morphogenesis; ISO:MGI.
DR GO; GO:0021854; P:hypothalamus development; ISO:MGI.
DR GO; GO:0034389; P:lipid droplet organization; 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; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061646; P:positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903061; P:positive regulation of protein lipidation; ISS:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IC:ParkinsonsUK-UCL.
DR GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
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; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; TAS:ParkinsonsUK-UCL.
DR GO; GO:0048489; P:synaptic vesicle transport; NAS: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; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..981
FT /note="Rab3 GTPase-activating protein catalytic subunit"
FT /id="PRO_0000191656"
FT REGION 532..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15042"
FT CONFLICT 56
FT /note="G -> D (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="E -> K (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="R -> K (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="R -> G (in Ref. 1; BAD32159 and 3; AAH46297)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="C -> S (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..117
FT /note="HC -> TS (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="L -> Q (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="R -> P (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="IG -> LS (in Ref. 2; BAC37915)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="Q -> H (in Ref. 2; BAC36271)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="R -> P (in Ref. 2; BAC36323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 981 AA; 110198 MW; D74B8B22C3D58AEA CRC64;
MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GPSLGKPLEK GIFTSGTWEE
RSDEISFADF RFSVTHHYLV QESPDKERKD EELEDAIPQS MQDLLCMNND FPPRAHCLVR
WYGLREFVVI APAAHSDAVL SESKCNLLLS SISIALGNTG CQVPLFVQIH HKWRRMYMGE
CQGPGVRTDF EMVHLRKVPS QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RLTYVLQDWQ
QYFWPQQPPD IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
DLDPVQAPHW SVRVRKADNP QCLLGDFVTE FLKICRRKES TDEILGRSTF EEEGREVADI
THALSKLTEP APVPIHKLSV SNMVHTAKKK IRKHRGEESP LNSDVLNTIL LFLFPDAVSE
KPLDGTTSID NSIPAPEAGD YTLYNQFKSA PSDSLTYKLA LCLCMINFYH GGLKGVAHLW
QEFVLEMRFR WENNFLIPGL ASGSPDLRCC LLHQKLQMLN CCIERKKARD EGKKTSLSDS
TTSAYPGDAG KTGGQLGLDH LRDTEKEKGE VGKSWDSWSD SEEEFFECLS DTEDLKGNGQ
ESGKKGGPKE MANLKPEGRL HQHGKLTLLH NGEPLYIPVT QEPAPMTEDL LEEQSEVLAK
LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCFLEDFVR WYSPRDYIEE EVTDEKGNVV
LKGELSARMK IPSNMWVEAW ETAKPVPARR QRRLFDDTRE AEKVLHYLAM QKPADLARHL
LPCVIHAAVL KVKEEESLEN IPSVKKIIKQ IIAHSSKVLH FPNPEDKKLE EIILQITTVE
AIIARARSLK AKFGTEKCEH EEEKEGLERF VSCLLEQPEV SVTGAGRGHA GRIIHKLFVN
AQRAAAVALP EEELKKSGCP EERRQTLVSD FPPPAGRELI LRATVPRPAP YSKALPQRMY
SVLTKEDFRL AGAFSSDTSF F
