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Database: UniProt
Entry: A0A2I2U3J0_FELCA
LinkDB: A0A2I2U3J0_FELCA
Original site: A0A2I2U3J0_FELCA 
ID   A0A2I2U3J0_FELCA        Unreviewed;       836 AA.
AC   A0A2I2U3J0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 2.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=ArfGAP with GTPase domain, ankyrin repeat and PH domain 2 {ECO:0000313|Ensembl:ENSFCAP00000026994.2};
GN   Name=AGAP2 {ECO:0000313|Ensembl:ENSFCAP00000026994.2,
GN   ECO:0000313|VGNC:VGNC:59674};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000026994.2, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000026994.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000026994.2,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000026994.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000026994.2,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000026994.2}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000026994.2};
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   EMBL; AANG04003655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_011282386.1; XM_011284084.2.
DR   AlphaFoldDB; A0A2I2U3J0; -.
DR   Ensembl; ENSFCAT00000037494.3; ENSFCAP00000026994.2; ENSFCAG00000014695.6.
DR   GeneID; 101097254; -.
DR   CTD; 116986; -.
DR   VGNC; VGNC:59674; AGAP2.
DR   GeneTree; ENSGT00940000158956; -.
DR   OrthoDB; 1449795at2759; -.
DR   Proteomes; UP000011712; Chromosome B4.
DR   Bgee; ENSFCAG00000014695; Expressed in prefrontal cortex and 9 other cell types or tissues.
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:SF3; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 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:UP000011712};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          340..554
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          575..695
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          734..766
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          246..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..451
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   836 AA;  90384 MW;  B1BD6785418B1FEE CRC64;
     MHAQRQLAVA AVRAEVRRHE VAKQSLSRLR KLAERVGDPE LRNSIQASLD SVREAVVNSQ
     EWTLSRSIPE LRLGVLGDAR SGKSSLIHRF LTGSYQVLEK TESEQHKKEM LVDGQTHLVL
     IREEAGAPDA KFSGWADAVI LVFSLEDENS FQAVSRLHGQ LSSLRGEGRG GLALALVGTQ
     DRISASSPRV VGDARARALC ADMKRCSYYE TCATYGLNVD RVFQEVAQKV VTLRKQQQLL
     AACKSLPSSP SHSAASTPVA GQASNGGHTS DYSSSLPSSP NVGHRELRAE AAAVAGLSTP
     GSLHRAAKRR TSLFANRRGS DSEKRSLDSR GETTGSGRAI PIKQSFLLKR SGNSLNKEWK
     KKYVTLSSNG FLLYHPSIND YIHSTHGKEM DLLRTTVKVP GKRPPRAISA FGPSASINGL
     VKDMSTVQMG EGPEATTPTP SPSPSPSSLQ PPPDQTSKHL LKPDRNLARA LSTDCTPSGD
     LSPLSREPPP SPMVKKQRRK KLTTPSKTEG SAGQAEEENF EFLIVSSTGQ TWHFEAASFE
     ERDAWVQAIE SQILASLQCC ESSKVKLRTD SQSEAVAIQA IRNAKGNSTC VDCGAPNPTW
     ASLNLGALIC IECSGIHRNL GTHLSRVRSL DLDDWPRELT LVLTAIGNDM ANRVWESDTR
     GRTKPTRDSS REERESWIRA KYEQLLFLAP LGTPEEPLGR QLWAAVQAQD VATVLLLLAH
     ARHGPLDTSV EDPQLRSPLH LAAELAHVVI TQLLLWYGAD VAARDAQGHT ALFYARQAGS
     QLCADILLQH GCPGEGGSTA TTPSAATTPS ITATPSPRRR SSAASMGRAD APVALV
//
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