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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//