AGAP1_XENLA
ID AGAP1_XENLA Reviewed; 864 AA.
AC Q6NRL1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1;
DE Short=AGAP-1;
DE AltName: Full=Centaurin-gamma-2;
DE Short=Cnt-g2;
GN Name=agap1; Synonyms=centg2;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein. Directly and specifically
CC regulates the adapter protein 3 (AP-3)-dependent trafficking of
CC proteins in the endosomal-lysosomal system (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with several subunits of the AP-3 protein
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates with the
CC endocytic compartment. {ECO:0000250}.
CC -!- DOMAIN: The PH domain mediates AP-3 binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
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DR EMBL; BC070738; AAH70738.1; -; mRNA.
DR RefSeq; NP_001084915.1; NM_001091446.1.
DR AlphaFoldDB; Q6NRL1; -.
DR SMR; Q6NRL1; -.
DR BioGRID; 101333; 1.
DR IntAct; Q6NRL1; 1.
DR MaxQB; Q6NRL1; -.
DR DNASU; 431967; -.
DR GeneID; 431967; -.
DR KEGG; xla:431967; -.
DR CTD; 431967; -.
DR Xenbase; XB-GENE-981026; agap1.L.
DR OrthoDB; 751525at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 431967; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; GTP-binding; GTPase activation; Metal-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Repeat;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..864
FT /note="Arf-GAP with GTPase, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000235915"
FT DOMAIN 346..591
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 612..732
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 771..800
FT /note="ANK 1"
FT REPEAT 804..833
FT /note="ANK 2"
FT ZN_FING 627..650
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 66..276
FT /note="Small GTPase-like"
FT REGION 266..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 122..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 864 AA; 95107 MW; 67AB37224F2C2895 CRC64;
MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERLDEP VLQNQIREHV IAIEDAFVNS
QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL
LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RLANYRNTSE IPMVLVGTQD
AISGSNPRVI DDSRARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI
GPCKSLPNSP SHTSVCSTQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPA
ASTPTPVRKQ SKRRSNLFTS RKGSDPDKDK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS
LNKEWKKKYV TLSDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSSCAPV
ASPKTNGLTK EVSGLQISPN TGNVTSSTSV TQMASGPSGI SLGSFSRMDG MHQRSYSVSS
ADQWSEGAVI TNSAISSDTG LGDSVCSSPS ISSTTSPKLD PPPSPHANRK KHRRKKSTSN
FKVDGLSSTA EEQEENFEFI IVSLTSQSWH FEATSYEERD AWVQAIESQI LASLQSCESS
KNKSRLTSQN EALALQSIRN LPGNSHCVDC DAQSPDWASL NLGALMCIEC SGIHRNLGTH
LSRVRSLDLD DWPPELIKVM SAIGNELANS VWEGSSQGHV KPCSESPREE KERWIRAKYE
QRLFLSPLPC RDLPLGQQLL RATAEEDLRA VILLLAHGSR EEVNETCGEG DRRTSLHLAC
RKGNVVLVQL LIWYGVDVMA RDFHGNTALA YAKQAVTSEV RELLLQYGCP DEQFVLMATP
NLSRKNNRNN NSNAGGSGLM PTLI
