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Database: UniProt
Entry: A0A2D0RUF0_ICTPU
LinkDB: A0A2D0RUF0_ICTPU
Original site: A0A2D0RUF0_ICTPU 
ID   A0A2D0RUF0_ICTPU        Unreviewed;       777 AA.
AC   A0A2D0RUF0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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};
GN   Name=LOC108271227 {ECO:0000313|RefSeq:XP_017334127.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017334127.1};
RN   [1] {ECO:0000313|RefSeq:XP_017334127.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017334127.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_017334127.1; XM_017478638.3.
DR   AlphaFoldDB; A0A2D0RUF0; -.
DR   STRING; 7998.ENSIPUP00000036527; -.
DR   Ensembl; ENSIPUT00000037956; ENSIPUP00000036527; ENSIPUG00000024458.
DR   GeneID; 108271227; -.
DR   OMA; DWEPEIL; -.
DR   OrthoDB; 1449795at2759; -.
DR   Proteomes; UP000221080; Chromosome 10.
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; cd08835; ArfGap_ACAP; 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; 1.
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};
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}; 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          266..361
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          397..519
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          645..677
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          678..710
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          366..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  88043 MW;  A1F441011A5E6FA1 CRC64;
     MRITVDFEEC LRDSPRFRAT IEEVEGDVCE LESKLDKLVK LCIGMIDAGK AYVSANKQFV
     NGIRELAQQS AEDEVIESSL TKFAESLQEM TNYHTILFDQ AQRSIKSQLQ MFVKEDLRRF
     KESKKQFDKV SEEKEAALIK NAQAPRNKPH EVEEANGILS ATRKCFRHIV LDYVLQINLL
     QSKRQSEILK SMLSFMYAHL TFFHQGYDLF SELHPLMKHL GGQLEQLMID AAKDKRVMET
     KHSTIQQKDY SNDDTKLEYN VDAENGIIME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
     KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM MQADSEKLKQ AWIRAMQNSI
     ATAFRDRSDD SEKLDRKSSP STASLESDPR EKTLKGEGAL QKVMSIAGNS TCCDCGQPEP
     KWASINLGIT LCIQCSGIHR SLGVHFSKVR SLTLDTWEPE LLKLMCELGN GVINRIYEAR
     REELGARKPQ PGDSRQDVEL YIRGKYVDRR FIRMPSDEEL KLKIRALCVA QKRLSDSSEP
     QTRQATQHTH PQKTQPPSGA SVKSADSGIM NKADGSPMVV KTSHNHTDET QSSTCSSKEK
     LVFSEPKQFC PSLHLYWASF TRSLPDMAEA LAHGAKVNFI NTEEEKRSPL IMAVHGGSLV
     TCEFLLQNSA SVNQCDSQGR GPLHHATILG HTGQVCLFLK RGANQNAADI EDKTPLSIAV
     DAANADIVTL LRLAKMNEEM RESEGPYTGL TGNETYQDIF QDFSQMASDD PDKLHRF
//
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