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Database: UniProt
Entry: A0A401T667_CHIPU
LinkDB: A0A401T667_CHIPU
Original site: A0A401T667_CHIPU 
ID   A0A401T667_CHIPU        Unreviewed;      1592 AA.
AC   A0A401T667;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=chiPu_0016623 {ECO:0000313|EMBL:GCC38112.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC38112.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC38112.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC38112.1}.
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DR   EMBL; BEZZ01001113; GCC38112.1; -; Genomic_DNA.
DR   STRING; 137246.A0A401T667; -.
DR   OMA; CSGQSEM; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13253; PH1_ARAP; 1.
DR   CDD; cd13259; PH5_ARAP; 1.
DR   CDD; cd04385; RhoGAP_ARAP; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 5.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR037858; RhoGAP_ARAP.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45899:SF4; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 4.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 5.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 5.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 5.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          6..65
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          387..479
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          485..583
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          580..714
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   DOMAIN          795..908
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          919..1017
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1021..1202
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          1231..1325
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1338..1442
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          74..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1592 AA;  180775 MW;  970B780F0767991D CRC64;
     MASFSEEEGD IGDWLATIHL EKYRENFIQN GFYTPKDSIH FNNESLLQIG IKATGHRKRI
     LKLVQQRSLT PTDELLSTTS DELNGDRDRM LERSRADGDG KDNLNVIDAE PEEPVIKPIP
     KPRTLFNKNS STPKHQATTG SASGHNSNLV LPLEVFTPAE IAGDKPDLTE RQYSSSDENT
     VWTPSEEVVP KAEENIPPVP PRSNRGKPPA CFMPNTTTSF DSDQSGTQSI PSMSKPAENL
     KDMQCLSSFS SHSLPLMSLA DTTFAGEMVS NELYTEVVTS PERNRSQSFS VSTGKSLSRR
     PVPELPSMLT RPDITTLPPR KRLYEMDSAQ KSFQMKGDNT MAYSTIGEIP TNSPSTTEPS
     LYFTEESEDD QTISPYASFH AAPEQGKSMK CDWLEKLSPQ GSCVFQRRYV KFDGKCLMYF
     GNEKDPYPKG VIPLAVIQMA RAAKENKFEV VTSHRIFVFR AENEGQRNEW CTHLQNAVKE
     YHFSSSRRVG SMAFYQKYSC LEMKGYKSKV YGALCTDILW LYKNEQSFKT GIGITMIGVQ
     GSTIRDVNRK SFEIITPLKT FSFTAESERE KKEWIEALQD SIAETLSDYE VAEKIWSNKS
     NKACADCKAQ NPDWASINLC VVICKRCAGE HRGLGTNISK VQSLKLDTSI WSNEIVQLFI
     DLGNEKANQF WAARMTPGEE LDTDATTERR KEFIKLKYRD GTFRGPHPKF ATQDELIKAL
     CSAVNSSNLL QTVTQIFSEA GRMSFIDTDA CETFSLSPQS PTYPTGVQHP SLRTSEVLNS
     NSMVSMGIYS EITQSVSHCG YLYRTSAMTK LPSSKKCKDE FQKQWCSLDR SLLFYETDKS
     TEPIGTIKMN DIVCIGVSRP QSLANSGPTD RFRYTFEIFL TSEKLFQFGT DNPDSLQMWT
     SSIAKGFTGL SLHSFLNCQF DRIGKLRYKS MQNPGQWQEG WFILNKSNMK FCSEEGGLEE
     EIVNLKRLQE LTFTILNENS EKKEVLRLVD KERTLYLHGV TRLDYSVWCG DIQRAAGSRG
     NALSDQQLSR NDIPIIVDSC IAFITQYGLR HEGIYRKNGA KSRIKLLMDE FRKDARNVKL
     RTGEHFIEDV TDVLKRFFRE IDDPVFMMAF HLQWKEAAEI THKPQRLKQY KEIIRELPRV
     NRMTLAALIG HLYRVQKCAD LNQMCTKNLS LLFAPSLFQT DGKGEQEVRV VEDLIDNYVS
     VFDIDDDHVT QMDLENSLIT TWKDVQLSQA GDLIMEVYVE TKATDCCMTL KVSPTMTSEE
     LTNQVLDLKN ISSGEKEVWV TFEAIENGEL ERPLHPKEKV LEQALQWCKL AEPSSAYLVV
     KKLPAGEGGN LYSAIKSEAP KCGMLKCREE PPKLLSGNKF QERYFVLRDR KLLLFKDKKS
     SKPEREWSVL SLKVYLGIKK KLKAPTVQWG FTICSDKQQW FLCCSGQSEM WDWTASILRA
     QHDDLRPAIL RRHSSSDVSK QKFGTMPLIP IHGDDSNAMM LSANQTLRRL HARRTLSMFF
     PMKMQHDVFE QHEKDENTNN EPVYEEVQDV SGMLSINQDI TPVDTTSMLV AQLKSNSVAN
     SVSTLPAQEK FLQELSSAIH RKNELQHDFT NL
//
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