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Protein

Rab3 GTPase-activating protein non-catalytic subunit

Gene

Rab3gap2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Rab3 GTPase-activating complex specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters.1 Publication

GO - Molecular functioni

  • enzyme regulator activity Source: UniProtKB
  • GTPase activator activity Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rab3 GTPase-activating protein non-catalytic subunit
Alternative name(s):
Rab3 GTPase-activating protein 150 kDa subunit
Rab3-GAP p150
Short name:
Rab3-GAP150
Rab3-GAP regulatory subunit
Gene namesi
Name:Rab3gap2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1311518. Rab3gap2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13861386Rab3 GTPase-activating protein non-catalytic subunitPRO_0000191664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei448 – 4481PhosphoserineCombined sources
Modified residuei899 – 8991PhosphothreonineBy similarity
Modified residuei976 – 9761PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5U1Z0.
PRIDEiQ5U1Z0.

PTM databases

PhosphoSiteiQ5U1Z0.

Interactioni

Subunit structurei

The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex interacts with DMXL2.2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003216.

Structurei

3D structure databases

ProteinModelPortaliQ5U1Z0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab3-GAP regulatory subunit family.Curated

Phylogenomic databases

eggNOGiKOG2727. Eukaryota.
ENOG410XTJ2. LUCA.
HOGENOMiHOG000290717.
HOVERGENiHBG067039.
InParanoidiQ5U1Z0.
KOiK19937.
PhylomeDBiQ5U1Z0.

Family and domain databases

InterProiIPR026059. Rab3-gap_reg.
IPR029257. RAB3GAP2_C.
IPR032839. RAB3GAP_N.
[Graphical view]
PANTHERiPTHR12472. PTHR12472. 1 hit.
PfamiPF14656. RAB3GAP2_C. 1 hit.
PF14655. RAB3GAP2_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5U1Z0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACSIVQFCS FQDLQSARDF LFPQLREETP GALRRDPSKT SNWEDDSWGA
60 70 80 90 100
WEETEPQEPE EEGNTSKTQK HSWLQECVLS LSPTSDLMVI AREQKAAFLV
110 120 130 140 150
RKWKHSDKGK EEMQFAVGWS GSVSAEEGEY VTSALCIPLA SQKRSSTGRP
160 170 180 190 200
DWTCIVVGFT SGYVRFYTEG VLLLAQLLNE DRVLQLKCRT YEIPRHPGVT
210 220 230 240 250
EQNEELSILY PAAIVTIDGF SLFQSLRACR NQVAKAAASG NENIQPPPLA
260 270 280 290 300
YKKWGLQDID TIIDHASIGI MTLSPFDQMK TASNIGGFNA AIKNSPPAMS
310 320 330 340 350
QYITVGSSPF TGFFYALEGS TQPLLSHVAL AVASKLTSAL FSAASGWLGW
360 370 380 390 400
KSKHEEETVQ KQKPKMEPAT PLAVRFGLPD SRRHGESICL SPCNTLAAVT
410 420 430 440 450
DDFGRVILLD VARGIAIRMW KGYRDAQIGW IQIVEDLHER VPEKGDFSPF
460 470 480 490 500
GNTQGPSRVA QFLVIYAPRR GILEVWSTQQ GPRVGAFNVG KHCRLLYPGY
510 520 530 540 550
KIMGLNNVTS QSWQPQTYQI CLVDPVSASV KAVNVPFHLA LSDKKSERAK
560 570 580 590 600
DLHLVKKLAA LLRAKSPRPD SFEAEIKELI LDIKYPATKK QALESILASD
610 620 630 640 650
RVSFSCLRNV TQTSMDTLKN QELESVDEGL LQFCASKLKL LHLYESVSQL
660 670 680 690 700
NTLDFHSDTP FSDNDLAVLL RLDDKELLKL RALLEKYKQE NTKATVRFSE
710 720 730 740 750
DADGVLPVKT FLEYLDYEKD ALSIRKTSEE ECVALGSFFF WKCLHGESST
760 770 780 790 800
EDMCHTLESA GLSPQQLLSL LLSVWLSKEK DILDKPQSVC CLHTMLSLLS
810 820 830 840 850
KMKVAIDETW DSQSVSPWWQ QMRMACIQSE NNGAALLSAH VGHSVAAQMS
860 870 880 890 900
SSATDKKFSQ MVLDADAEAL TDSWEALSLD TEYWKLLLRQ LEDCLILQTL
910 920 930 940 950
LHSRASPPAA KASSPQTEPL PRLSVKKLLE GGKGGIADSV AKWIFKQDLS
960 970 980 990 1000
PELLKCANRE KDVENPDEPR EGIARSPPEV SEVETDLGAV PDLLRLAYEQ
1010 1020 1030 1040 1050
FPCSLELDVL HAHCCWEYVV QWNKDPEEAR FLVRSIEHLR HILNPHVQNG
1060 1070 1080 1090 1100
ISLMMWNTFL VKRFSAATYL MDKVGKSPKD RLCRRDVGMS DTALTSFLGS
1110 1120 1130 1140 1150
CLDLLQTSLE ADISRDEVQV PVLDTEDAWL SVEGPTSIVE LALEQKPIHY
1160 1170 1180 1190 1200
PLVEHHSILC SILYAAMSFS LKSVKPLALF DSKGKNAFFK DLTSIQLLPS
1210 1220 1230 1240 1250
GEMDPNFISV RQQFLLKVVS AAVQAQHSKD KDPSARAADT HGQDLNWTAL
1260 1270 1280 1290 1300
AVDLAHHLQV SEDVIRRHYV GELYSYGADL LGEEAILQVQ DKEVLASQLL
1310 1320 1330 1340 1350
VLTGQRLAHA LFHTQTKEGM ELLARLPPTL CTWLKAMNPQ DLQNTGVPVA
1360 1370 1380
ATAKLVHKVM ELLPEKHGQY SLALHLIEAV EAMATL
Length:1,386
Mass (Da):154,431
Last modified:April 12, 2005 - v2
Checksum:iB2C96FC7FEE56785
GO

Sequence cautioni

The sequence AAH86380.1 differs from that shown. Reason: Frameshift at position 1058. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1231 – 12311K → R in AAH86380 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03085350 Genomic DNA. No translation available.
AABR03089585 Genomic DNA. No translation available.
AABR03089113 Genomic DNA. No translation available.
AABR03089836 Genomic DNA. No translation available.
AABR03089287 Genomic DNA. No translation available.
AABR03086829 Genomic DNA. No translation available.
AABR03087362 Genomic DNA. No translation available.
BC086380 mRNA. Translation: AAH86380.1. Frameshift.
RefSeqiNP_001035244.2. NM_001040154.2.
UniGeneiRn.101730.

Genome annotation databases

GeneIDi289350.
KEGGirno:289350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03085350 Genomic DNA. No translation available.
AABR03089585 Genomic DNA. No translation available.
AABR03089113 Genomic DNA. No translation available.
AABR03089836 Genomic DNA. No translation available.
AABR03089287 Genomic DNA. No translation available.
AABR03086829 Genomic DNA. No translation available.
AABR03087362 Genomic DNA. No translation available.
BC086380 mRNA. Translation: AAH86380.1. Frameshift.
RefSeqiNP_001035244.2. NM_001040154.2.
UniGeneiRn.101730.

3D structure databases

ProteinModelPortaliQ5U1Z0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003216.

PTM databases

PhosphoSiteiQ5U1Z0.

Proteomic databases

PaxDbiQ5U1Z0.
PRIDEiQ5U1Z0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi289350.
KEGGirno:289350.

Organism-specific databases

CTDi25782.
RGDi1311518. Rab3gap2.

Phylogenomic databases

eggNOGiKOG2727. Eukaryota.
ENOG410XTJ2. LUCA.
HOGENOMiHOG000290717.
HOVERGENiHBG067039.
InParanoidiQ5U1Z0.
KOiK19937.
PhylomeDBiQ5U1Z0.

Miscellaneous databases

NextBioi629692.
PROiQ5U1Z0.

Family and domain databases

InterProiIPR026059. Rab3-gap_reg.
IPR029257. RAB3GAP2_C.
IPR032839. RAB3GAP_N.
[Graphical view]
PANTHERiPTHR12472. PTHR12472. 1 hit.
PfamiPF14656. RAB3GAP2_C. 1 hit.
PF14655. RAB3GAP2_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Molecular cloning and characterization of the noncatalytic subunit of the Rab3 subfamily-specific GTPase-activating protein."
    Nagano F., Sasaki T., Fukui K., Asakura T., Imazumi K., Takai Y.
    J. Biol. Chem. 273:24781-24785(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-54; 532-544 AND 1218-1229, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1053-1386.
    Tissue: Ovary.
  4. "Rabconnectin-3, a novel protein that binds both GDP/GTP exchange protein and GTPase-activating protein for Rab3 small G protein family."
    Nagano F., Kawabe H., Nakanishi H., Shinohara M., Deguchi-Tawarada M., Takeuchi M., Sasaki T., Takai Y.
    J. Biol. Chem. 277:9629-9632(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DMXL2.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-976, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRBGPR_RAT
AccessioniPrimary (citable) accession number: Q5U1Z0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: May 11, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.