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Protein

Rab3 GTPase-activating protein catalytic subunit

Gene

Rab3gap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable catalytic 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. 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • brain development Source: MGI
  • camera-type eye development Source: MGI
  • establishment of protein localization to endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • excitatory postsynaptic potential Source: ParkinsonsUK-UCL
  • face morphogenesis Source: MGI
  • hypothalamus development Source: MGI
  • lipid particle organization Source: MGI
  • positive regulation of autophagosome assembly Source: GO_Central
  • positive regulation of endoplasmic reticulum tubular network organization Source: ParkinsonsUK-UCL
  • positive regulation of gene expression Source: ParkinsonsUK-UCL
  • positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization Source: ParkinsonsUK-UCL
  • positive regulation of GTPase activity Source: ParkinsonsUK-UCL
  • positive regulation of protein lipidation Source: GO_Central
  • protein stabilization Source: ParkinsonsUK-UCL
  • regulation of calcium ion-dependent exocytosis of neurotransmitter Source: ParkinsonsUK-UCL
  • regulation of GTPase activity Source: MGI
  • regulation of Rab protein signal transduction Source: UniProtKB
  • regulation of short-term neuronal synaptic plasticity Source: ParkinsonsUK-UCL
  • regulation of synaptic vesicle priming Source: ParkinsonsUK-UCL
  • synaptic vesicle transport Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rab3 GTPase-activating protein catalytic subunit
Alternative name(s):
RAB3 GTPase-activating protein 130 kDa subunit
Rab3-GAP p130
Short name:
Rab3-GAP
Gene namesi
Name:Rab3gap1
Synonyms:Kiaa0066, Rab3gap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2445001. Rab3gap1.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: In neurons, it is enriched in the synaptic soluble fraction.By similarity

GO - Cellular componenti

  • cytoplasm Source: ParkinsonsUK-UCL
  • endoplasmic reticulum tubular network Source: ParkinsonsUK-UCL
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: MGI
  • lipid particle Source: MGI
  • postsynapse Source: GOC
  • protein complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 981980Rab3 GTPase-activating protein catalytic subunitPRO_0000191656Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei579 – 5791PhosphoserineCombined sources
Modified residuei581 – 5811PhosphoserineCombined sources
Modified residuei590 – 5901PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ80UJ7.
MaxQBiQ80UJ7.
PaxDbiQ80UJ7.
PRIDEiQ80UJ7.

PTM databases

iPTMnetiQ80UJ7.
PhosphoSiteiQ80UJ7.

Expressioni

Tissue specificityi

In the eye, it is highly expressed within the lens, particularly in the anterior lens epithelium and in a ring corresponding to the equatorial region where anterior cells are differentiating into lens fibers. Also highly expressed in the retina.1 Publication

Developmental stagei

From E10 to E12, it is weakly expressed throughout the embryo. At E14.5, it is predominantly expressed in a number of organ systems, including the central and peripheral nervous systems.1 Publication

Gene expression databases

BgeeiQ80UJ7.
CleanExiMM_RAB3GAP1.
GenevisibleiQ80UJ7. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230504. 9 interactions.
IntActiQ80UJ7. 7 interactions.
MINTiMINT-4114525.
STRINGi10090.ENSMUSP00000042070.

Structurei

3D structure databases

ProteinModelPortaliQ80UJ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab3-GAP catalytic subunit family.Curated

Phylogenomic databases

eggNOGiKOG2390. Eukaryota.
ENOG410Y2R4. LUCA.
GeneTreeiENSGT00390000006705.
HOVERGENiHBG079116.
InParanoidiQ80UJ7.
KOiK18270.
OMAiTRTCLLH.
OrthoDBiEOG783MTK.
TreeFamiTF314500.

Family and domain databases

InterProiIPR026147. Rab3-GAP_cat_su.
[Graphical view]
PANTHERiPTHR21422. PTHR21422. 2 hits.
PfamiPF13890. Rab3-GTPase_cat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80UJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GPSLGKPLEK
60 70 80 90 100
GIFTSGTWEE RSDEISFADF RFSVTHHYLV QESPDKERKD EELEDAIPQS
110 120 130 140 150
MQDLLCMNND FPPRAHCLVR WYGLREFVVI APAAHSDAVL SESKCNLLLS
160 170 180 190 200
SISIALGNTG CQVPLFVQIH HKWRRMYMGE CQGPGVRTDF EMVHLRKVPS
210 220 230 240 250
QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RLTYVLQDWQ QYFWPQQPPD
260 270 280 290 300
IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
310 320 330 340 350
DLDPVQAPHW SVRVRKADNP QCLLGDFVTE FLKICRRKES TDEILGRSTF
360 370 380 390 400
EEEGREVADI THALSKLTEP APVPIHKLSV SNMVHTAKKK IRKHRGEESP
410 420 430 440 450
LNSDVLNTIL LFLFPDAVSE KPLDGTTSID NSIPAPEAGD YTLYNQFKSA
460 470 480 490 500
PSDSLTYKLA LCLCMINFYH GGLKGVAHLW QEFVLEMRFR WENNFLIPGL
510 520 530 540 550
ASGSPDLRCC LLHQKLQMLN CCIERKKARD EGKKTSLSDS TTSAYPGDAG
560 570 580 590 600
KTGGQLGLDH LRDTEKEKGE VGKSWDSWSD SEEEFFECLS DTEDLKGNGQ
610 620 630 640 650
ESGKKGGPKE MANLKPEGRL HQHGKLTLLH NGEPLYIPVT QEPAPMTEDL
660 670 680 690 700
LEEQSEVLAK LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCFLEDFVR
710 720 730 740 750
WYSPRDYIEE EVTDEKGNVV LKGELSARMK IPSNMWVEAW ETAKPVPARR
760 770 780 790 800
QRRLFDDTRE AEKVLHYLAM QKPADLARHL LPCVIHAAVL KVKEEESLEN
810 820 830 840 850
IPSVKKIIKQ IIAHSSKVLH FPNPEDKKLE EIILQITTVE AIIARARSLK
860 870 880 890 900
AKFGTEKCEH EEEKEGLERF VSCLLEQPEV SVTGAGRGHA GRIIHKLFVN
910 920 930 940 950
AQRAAAVALP EEELKKSGCP EERRQTLVSD FPPPAGRELI LRATVPRPAP
960 970 980
YSKALPQRMY SVLTKEDFRL AGAFSSDTSF F
Length:981
Mass (Da):110,198
Last modified:July 27, 2011 - v4
Checksum:iD74B8B22C3D58AEA
GO

Sequence cautioni

The sequence BAD32159.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561G → D in BAC36271 (PubMed:16141072).Curated
Sequence conflicti64 – 641E → K in BAC36271 (PubMed:16141072).Curated
Sequence conflicti71 – 711R → K in BAC36271 (PubMed:16141072).Curated
Sequence conflicti88 – 881R → G in BAD32159 (PubMed:15368895).Curated
Sequence conflicti88 – 881R → G in AAH46297 (PubMed:15489334).Curated
Sequence conflicti106 – 1061C → S in BAC36271 (PubMed:16141072).Curated
Sequence conflicti116 – 1172HC → TS in BAC36271 (PubMed:16141072).Curated
Sequence conflicti124 – 1241L → Q in BAC36271 (PubMed:16141072).Curated
Sequence conflicti175 – 1751R → P in BAC36271 (PubMed:16141072).Curated
Sequence conflicti216 – 2172IG → LS in BAC37915 (PubMed:16141072).Curated
Sequence conflicti321 – 3211Q → H in BAC36271 (PubMed:16141072).Curated
Sequence conflicti619 – 6191R → P in BAC36323 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172881 mRNA. Translation: BAD32159.1. Different initiation.
AK076244 mRNA. Translation: BAC36271.1.
AK076399 mRNA. Translation: BAC36323.1.
AK080432 mRNA. Translation: BAC37915.1.
AK164523 mRNA. Translation: BAE37821.1.
BC028996 mRNA. Translation: AAH28996.1.
BC046297 mRNA. Translation: AAH46297.1.
CCDSiCCDS15249.1.
RefSeqiNP_848805.2. NM_178690.4.
UniGeneiMm.489713.

Genome annotation databases

EnsembliENSMUST00000037649; ENSMUSP00000042070; ENSMUSG00000036104.
GeneIDi226407.
KEGGimmu:226407.
UCSCiuc007clc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172881 mRNA. Translation: BAD32159.1. Different initiation.
AK076244 mRNA. Translation: BAC36271.1.
AK076399 mRNA. Translation: BAC36323.1.
AK080432 mRNA. Translation: BAC37915.1.
AK164523 mRNA. Translation: BAE37821.1.
BC028996 mRNA. Translation: AAH28996.1.
BC046297 mRNA. Translation: AAH46297.1.
CCDSiCCDS15249.1.
RefSeqiNP_848805.2. NM_178690.4.
UniGeneiMm.489713.

3D structure databases

ProteinModelPortaliQ80UJ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230504. 9 interactions.
IntActiQ80UJ7. 7 interactions.
MINTiMINT-4114525.
STRINGi10090.ENSMUSP00000042070.

PTM databases

iPTMnetiQ80UJ7.
PhosphoSiteiQ80UJ7.

Proteomic databases

EPDiQ80UJ7.
MaxQBiQ80UJ7.
PaxDbiQ80UJ7.
PRIDEiQ80UJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037649; ENSMUSP00000042070; ENSMUSG00000036104.
GeneIDi226407.
KEGGimmu:226407.
UCSCiuc007clc.2. mouse.

Organism-specific databases

CTDi22930.
MGIiMGI:2445001. Rab3gap1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG2390. Eukaryota.
ENOG410Y2R4. LUCA.
GeneTreeiENSGT00390000006705.
HOVERGENiHBG079116.
InParanoidiQ80UJ7.
KOiK18270.
OMAiTRTCLLH.
OrthoDBiEOG783MTK.
TreeFamiTF314500.

Miscellaneous databases

ChiTaRSiRab3gap1. mouse.
NextBioi378122.
PROiQ80UJ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ80UJ7.
CleanExiMM_RAB3GAP1.
GenevisibleiQ80UJ7. MM.

Family and domain databases

InterProiIPR026147. Rab3-GAP_cat_su.
[Graphical view]
PANTHERiPTHR21422. PTHR21422. 2 hits.
PfamiPF13890. Rab3-GTPase_cat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Heart and Skin.
  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].
    Strain: FVB/NJ.
    Tissue: Mammary tumor.
  4. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-579 AND SER-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRB3GP_MOUSE
AccessioniPrimary (citable) accession number: Q80UJ7
Secondary accession number(s): Q3TPB6
, Q6A0D7, Q8C4Y0, Q8C679, Q8C6A5, Q8K324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 27, 2011
Last modified: April 13, 2016
This is version 97 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.