RB3GP_XENLA
ID RB3GP_XENLA Reviewed; 978 AA.
AC Q642R9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Rab3 GTPase-activating protein catalytic subunit;
GN Name=rab3gap1; Synonyms=rab3gap;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable catalytic subunit of a GTPase activating protein
CC that has specificity for Rab3 subfamily. Rab3 proteins are involved in
CC regulated exocytosis of neurotransmitters and hormones. Specifically
CC converts active Rab3-GTP to the inactive form Rab3-GDP (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed
CC of RAB3GAP and RAB3GAP150. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.
CC {ECO:0000305}.
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DR EMBL; BC081089; AAH81089.1; -; mRNA.
DR RefSeq; NP_001087691.1; NM_001094222.1.
DR AlphaFoldDB; Q642R9; -.
DR SMR; Q642R9; -.
DR DNASU; 447515; -.
DR GeneID; 447515; -.
DR KEGG; xla:447515; -.
DR CTD; 447515; -.
DR Xenbase; XB-GENE-995564; rab3gap1.L.
DR OrthoDB; 536022at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 447515; Expressed in brain and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..978
FT /note="Rab3 GTPase-activating protein catalytic subunit"
FT /id="PRO_0000191659"
FT REGION 533..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 109800 MW; E827C8587ABAD3D8 CRC64;
MAADSDPESE VFEITDFTTA SEWERFISKV EEVLTEWKLI GETSNKPPEK GEYTSGVWEE
KGEEVLFADF RFSIRHHYLV QKSSEKEEKE DTGEDSIPVC MQDLLCTNND FPPVAHCLVR
WYGLREFVVI SPGANDAVIS ESKCNLLLSS VSIALGNTGC QVPLFVQVHQ KWRKLYVGEC
RGPGVRTDFE MVHLRKVPNQ YTHLSGLLDI FKSKIGCPLT ALPPVNIAIR FTYVLQDWQQ
YFWPQQPPDI DALIGGEVGG LEFGKLPFGA CEDPISELHL ATTWPCLTEG IIVDNDVYSD
LDPLQAPQWS VRVRKADNPQ CMLGDFVSEF FRLCRRKEST DELLGKSAFE ENGKEGADIS
QALSKLTEPA PVPIHKLSVT SMVHSARKKI RKHRGADESP LNNDVLNAIL FFLFPDTKSL
DGSEAKPSTS TGNISSQSES EDYNLYSQLK SAPSNSLTYK LALCLCMVNF YHGGVKGVAH
LWQEFVLEMR YRWENNFLIP GLANGSPDLK CCLLHQKLQM LNCCLERKKA RDEGKKGNPL
YSSSESSVNK TASDLLSPVE ADKSKYEVAK SWDSWSDSEE EFFECHSDTE ELKESGQESA
RKAKEETKEN PSPKPEGRLH QSGNLMLLNS GEPLYIPVTQ DPAPMTDDLL EEQSEVLAKL
GTSAEGAHLR ARMQSACLLS DMESFKAANP GCCLEDFVRW YSPRDYIEEE VMDDKGNKIF
KGELSARMKI PNNMWVEAWE TAKPIPARRQ RRLFDDTKEA EKVLHYLAVQ KPADLTRHLL
PCVIHAALLK LKEEEAAEDI PSGRKAIKQI ISHSSKVLRF PSPDDKKLED VISQISNVEA
AIARARSLKA KFAIDRCEKS EEREDLEKFV SCLLDQPEVP IIGAGRGAAG TIIHKMFVQR
ALTLAPVEEE PKRSSSSDDR RQTSGTDFPS PAGRELILRT SVPRPAPYSK VLPQRMYSVL
TKEDFRLTGA FSSDTSFF