ID RBGP1_PONAB Reviewed; 1069 AA.
AC Q5RAN1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Rab GTPase-activating protein 1;
DE AltName: Full=GAP and centrosome-associated protein;
DE AltName: Full=Rab6 GTPase-activating protein GAPCenA;
GN Name=RABGAP1 {ECO:0000250|UniProtKB:Q9Y3P9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH91179.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH91179.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a
CC role in microtubule nucleation by centrosome. May participate in a
CC RAB6A-mediated pathway involved in the metaphase-anaphase transition
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y3P9}.
CC -!- SUBUNIT: Interacts with RAB6A and tubulin gamma.
CC {ECO:0000250|UniProtKB:Q9Y3P9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y3P9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y3P9}.
CC Note=Predominantly cytosolic but also associated with the centrosome.
CC {ECO:0000250|UniProtKB:Q9Y3P9}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
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DR EMBL; CR858984; CAH91179.1; -; mRNA.
DR RefSeq; NP_001125691.1; NM_001132219.1.
DR AlphaFoldDB; Q5RAN1; -.
DR SMR; Q5RAN1; -.
DR STRING; 9601.ENSPPYP00000021947; -.
DR Ensembl; ENSPPYT00000022851.3; ENSPPYP00000021947.3; ENSPPYG00000019586.3.
DR GeneID; 100172613; -.
DR KEGG; pon:100172613; -.
DR CTD; 23637; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000157216; -.
DR InParanoid; Q5RAN1; -.
DR OMA; MHSMGYV; -.
DR OrthoDB; 2908929at2759; -.
DR Proteomes; UP000001595; Chromosome 9.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR CDD; cd01211; PTB_Rab6GAP; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR Gene3D; 1.10.10.750; Ypt/Rab-GAP domain of gyp1p, domain 1; 1.
DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR035969; Rab-GAP_TBC_sf.
DR PANTHER; PTHR47219:SF6; RAB GTPASE-ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1069
FT /note="Rab GTPase-activating protein 1"
FT /id="PRO_0000298781"
FT DOMAIN 142..298
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 566..752
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 798..1047
FT /evidence="ECO:0000255"
FT COMPBIAS 9..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 608
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 649
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P9"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AWA9"
FT MOD_RES 996
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P9"
SQ SEQUENCE 1069 AA; 121709 MW; AB6B268B1A12D230 CRC64;
MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL
QKELADVLMD PPMDDQPGEK ELVKRSQLDG EGDGPLSNQL SASSTINPVP LVGLQKPEMS
LPVKPGQGDS EASSPFTPVA DEDSVVFSKL TYLGCASVNA PRSEVEALRM MSILRSQCQI
SLDVTLSVPN VSEGIVRLLD PQTNTEIANY PIYKILFCVR GHDGTPESDC FAFTESHYNA
ELFRIHVFRC EIQEAVSRIL YSFATAFRRS AKQTPLSATA APQTPDSDIF TFSVSLEIKE
DDGKGYFSAV PKDKDRQCFK LRQGIDKKIV IYVQQTTNKE LAIERCFGLL LSPGKDVRNS
DMHLLDLESM GKSSDGKSYV ITGSWNPKSP HFQVVNEETP KDKVLFMTTA VDLVITEVQE
PVRFLLETKV RVCSPNERLF WPFSKRSTTE NFFLKLKQIK QKERKNNTDT LYEVVCLESE
SERERRKTTA SPSVRLPQSG SQSSVIPSPP EDDEEEDNDE PLLSGSGDVS KECAEKILET
WGELLSKWHL NLNVRPKQLS SLVRNGVPEA LRGEVWQLLA GCHNNDHLVE KYRILITKES
PQDSAITRDI NRTFPAHDYF KDTGGDGQDS LYKICKAYSV YDEEIGYCQG QSFLAAVLLL
HMPEEQAFSV LVKIMFDYGL RELFKQNFED LHCKFYQLER LMQEYIPDLY NHFLDISLEA
HMYASQWFLT LFTAKFPLYM VFHIIDLLLC EGISVIFNVA LGLLKTSKDD LLLTDFEGAL
KFFRVQLPKR YRSEENAKKL MELACNMKIS QKKLKKYEKE YHTMREQQAQ QEDPIERFER
ENRRLQEANM RLEQENDDLA HELVTSKIAL RKDLDNAEEK ADALNKELLM TKQKLIDAEE
EKRRLEEESA QLKEMCRREL DKAESEIKKN SSIIGDYKQI CSQLSERLEK QQTANKVEIE
KIRQKVDDCE RCREFFNKEG RVKGISSTKE VLDEDTDEEK ETLKNQLREM ELELAQTKLQ
LVEAECKIQD LEHHLGLALN EVQAAKKTWF NRTLSSIKTA TGVQGKETC
//
