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Database: UniProt
Entry: A0A091VCX5_NIPNI
LinkDB: A0A091VCX5_NIPNI
Original site: A0A091VCX5_NIPNI 
ID   A0A091VCX5_NIPNI        Unreviewed;       762 AA.
AC   A0A091VCX5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein {ECO:0000256|RuleBase:RU369028};
DE            Short=Cnt-b {ECO:0000256|RuleBase:RU369028};
DE   AltName: Full=Centaurin-beta {ECO:0000256|RuleBase:RU369028};
DE   Flags: Fragment;
GN   ORFNames=Y956_07210 {ECO:0000313|EMBL:KFR00620.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR00620.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFR00620.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR00620.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC       (ARF6). {ECO:0000256|ARBA:ARBA00037592}.
CC   -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC       family. {ECO:0000256|RuleBase:RU369028}.
CC   -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC       4,5-bisphosphate (PIP2) and phosphatidic acid.
CC       {ECO:0000256|RuleBase:RU369028}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004481,
CC       ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481, ECO:0000256|RuleBase:RU369028}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- DOMAIN: PH domain binds phospholipids including phosphatidic acid,
CC       phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate
CC       (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate
CC       protein binding to PIP2 or PIP3 containing membranes.
CC       {ECO:0000256|RuleBase:RU369028}.
CC   -!- DOMAIN: The BAR domain mediates homodimerization, it can neither bind
CC       membrane nor impart curvature, but instead requires the neighboring PH
CC       domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}.
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DR   EMBL; KL410876; KFR00620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091VCX5; -.
DR   STRING; 128390.A0A091VCX5; -.
DR   eggNOG; KOG0521; Eukaryota.
DR   Proteomes; UP000053283; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08851; ArfGap_ACAP2; 1.
DR   CDD; cd07638; BAR_ACAP2; 1.
DR   CDD; cd13250; PH_ACAP; 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; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR045258; ACAP1/2/3-like.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
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; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23180:SF241; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU369028};
KW   GTPase activation {ECO:0000256|RuleBase:RU369028};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW   Repeat {ECO:0000256|RuleBase:RU369028};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369028};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          249..344
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          382..504
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          624..656
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          657..689
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          348..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..130
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        348..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFR00620.1"
FT   NON_TER         762
FT                   /evidence="ECO:0000313|EMBL:KFR00620.1"
SQ   SEQUENCE   762 AA;  85960 MW;  1C53EC683417DFEB CRC64;
     RAALEEVEGD VTELELKLDK LVKLCISMID TGKAFCTANK QFMNGIRDLA QYSCRDVLVE
     TSLTKFSDTL QEMINYHNIL FDQTQRSIKA QLQTFVKDDI RKFKDAKKQF EKVSEEKENA
     LVKNAQVQRN KQHEVEEATN ILTATRKCFR HIALDYVLQI NVLQSKRRAE ILKSMLSFMY
     AHLAFFHQGY DLFSELEPYM KDLGAQLDQL AVDAAKEKRD MEQKHSTIQQ KDYSSDDTKL
     EYNVDAANGI VMEGYLFKRA SNAFKTWNRR WFSIQNNQLV YQKKFKDNPT VVVEDLRLCT
     VKHCEDIERR FCFEVVSPTK SCMLQADSEK LRQAWIKAVQ TSIATAYREK GDESEKQEKK
     SSPSTGSLES GSETKEKLLK GESALQRVQC IPGNAACCDC GLADPRWASI NLGITLCIEC
     SGIHRSLGVH FSKVRSLTLD SWEPELLKLM CELGNDVINR IYEAKLEKVG VKKPQPGSQR
     QEKEAYIRAK YVERKFVEKQ PASVSLLESG TKVLPQSQEE KRHSGPEKSL LAGEQGAASQ
     KVQSSDSGIQ QSADDSREHL ASTISANSLY EPEVDKQESS VFCDSKQPSP GLQLYRAAFE
     KNLPDMAEAL AHGAEVNWVN VEENKATPLI QAVRGGSLVT CEFLLQNGAN VNIRDMKGRG
     PLHHATVLGH TGQVCLFLKR GANQHATDED GKDPLSIAVE AANADIVTLL RLARMNEEMR
     ESEGLYGQPG DEIYQDIFRD FSQMASNNPE KLNRFQQSDS QK
//
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