ID U3JD05_FICAL Unreviewed; 827 AA.
AC U3JD05;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=ArfGAP with GTPase domain, ankyrin repeat and PH domain 1 {ECO:0000313|Ensembl:ENSFALP00000000659.2};
GN Name=AGAP1 {ECO:0000313|Ensembl:ENSFALP00000000659.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000000659.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000000659.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000000659.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC {ECO:0000256|ARBA:ARBA00005430}.
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DR AlphaFoldDB; U3JD05; -.
DR STRING; 59894.ENSFALP00000000659; -.
DR Ensembl; ENSFALT00000000663.2; ENSFALP00000000659.2; ENSFALG00000000637.2.
DR eggNOG; KOG0705; Eukaryota.
DR GeneTree; ENSGT00940000154793; -.
DR HOGENOM; CLU_007326_1_0_1; -.
DR Proteomes; UP000016665; Chromosome 7.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
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 CDD; cd08836; ArfGap_AGAP; 1.
DR CDD; cd04103; Centaurin_gamma; 1.
DR CDD; cd01250; PH_AGAP; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
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 PANTHER; PTHR45819:SF1; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 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 SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 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.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..827
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032426201"
FT DOMAIN 289..558
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 579..699
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 738..770
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 210..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91090 MW; 582D0A2569B1EB8C CRC64;
MNRSWMFLFS FVLFSIQGIV GNLASGKSAL VHRYLTGTYV QEESPEGGRF KKEIVVDGQS
YLLLIRDEGG PPEAQFAMWV DAVIFVFSLE DEVSFQTVYH YYSRMANYRN TSEIPMVLVG
TQDAISSTNP RVIDDARARK LSNDLKRCTY YETCATYGLN VERVFHDVAQ KIVSTKKKQQ
LSIGPCKSLP NSPSHSSVCS AQVSAVHISQ TSNGGGSLSD YSSSVPSTPS TSQKELRIDV
PPTANTPTPV RKQSKRRSNL FTSRKGSDPD KEKKVLESRT DSIGSGRAIP IKQGMLLKRS
GKSLNKEWKK KYVTLCDNGV LTYHPSLHDY MQNVHGKEID LLRTTVKVPG KRPPRATSAC
APISSPKTNG LSKDMSSLHI SPNSGNVTTS TSVSQMASGI SLVSFNSRPD GMHQRSYSVS
SADQWSEATV IANSGISSDT GLGDSVCSSP SISSTTSPKL DPPPSPHANR KKHRRKKSTS
NFKADGISGT AEAKRKAWKL NRVGSLRNIY SSSSTNTEEQ EENFEFIIVS LTGQTWHFEA
TTYEERDAWV QAIESQILAS LQSCESSKNK SRLTSQNEAM ALQSIRNIRG NSHCVDCEAQ
NPDWASLNLG ALICIECSGI HRNLGTHLSR VRSLDLDDWP IELIKVMSAI GNELANSVWE
ENSQGHVKPS PDSTREEKEL WIRAKYEQKL FLAPLQCLEL SLGQHLLRAT AEEDLRAVIL
LLAHGTRDEV NETCGDGDGR TALHLACRKG SVVLLQLLIW YGVDVMARDA HGNTALAYAR
QASSQECIDV LLQYGCPDER FALMATPNLS RKNNNRNNGG GRMPTII
//
