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Database: UniProt
Entry: C3ZGU2_BRAFL
LinkDB: C3ZGU2_BRAFL
Original site: C3ZGU2_BRAFL 
ID   C3ZGU2_BRAFL            Unreviewed;       865 AA.
AC   C3ZGU2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Ras GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BRAFLDRAFT_206850 {ECO:0000313|EMBL:EEN48318.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN48318.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN48318.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN48318.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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DR   EMBL; GG666620; EEN48318.1; -; Genomic_DNA.
DR   RefSeq; XP_002592307.1; XM_002592261.1.
DR   AlphaFoldDB; C3ZGU2; -.
DR   STRING; 7739.C3ZGU2; -.
DR   eggNOG; KOG3508; Eukaryota.
DR   InParanoid; C3ZGU2; -.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   CDD; cd08400; C2_Ras_p21A1; 1.
DR   CDD; cd13260; PH_RASA1; 1.
DR   CDD; cd11788; SH3_RasGAP; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR035652; RasGAP_SH3.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10194:SF146; RAS GTPASE-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..865
FT                   /note="Ras GTPase-activating protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002936382"
FT   DOMAIN          61..123
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          133..256
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          292..394
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          395..508
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          565..759
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
SQ   SEQUENCE   865 AA;  99026 MW;  B3B393F26D493A05 CRC64;
     MRFHDKALFL LCRIIAMCGD FYLGGRQFDS LSDLIGYYTI WACILKDEKL MYPVPPPEPV
     QSRRLVRAIL PYTRVPDTDE LSFEKSDVFM VHNTMDGGWL WVTSQRTNES GLVIRDLVEE
     LDFYADPHEG KEWFHGTITK EKAAQLLSGI FFSVYSAFLI RPSDSSPGDY SLFFRSNNMI
     QRFRITRQNH EEFEMGGHHY ATYSDILPIC YTTLLKFLVS CGNFIFSPFI PSSLDDIIKH
     YKTEQIVEGY TLGEPVPNKV GHEGQKIDFC VIAMIIFFFL KLVICTSYFN STVTVTWSLY
     FSGHRSKKWK NLFFILNGTE QHVYYFENEK RTKPKGLIDL NYASIYPVHE SLFGRPNCFQ
     TVVRALNDVT TTYLCADTAE LAKEWILAMR QFCTQPSNKQ SPLNAKRVKQ LRSLSVNVLD
     ARNLPVKHLP HPYCMLSLHD VHAARTQMRE GPNPLWSEEF VFEDLPREVE SFTLLLCSRA
     RRSKDAVVAS VYVPLSKLPN GQYVDEWYPV IPESPYKGDM GSIRIRAHYR SQLVLPLEEY
     AGLKQLIVSK EFHTIYALDK VCARDRSLLA SALLRVFRDE KKEAVLLQTL TTKEIANEDE
     SATLFRATTL ASTLMDQYMK MTAVPFLHQA VKDVITKIAD SKQSCELNPT KLEKGADVNS
     NLETLLSFLT EAVEAIFKAT ESCPSTLRYI FGCLQREVLK KWPDDTTMRT RVVSGFIFLR
     LICPAILNPR QFNLLAESPT PTAARTLTMV AKSLQNLANL VEFGAKEPYM EAVNPFIVKN
     KERMIMFLDE LAVRIPTSPC HLMCECVYVC ECNVPSYPEV TEKVKSDPSQ DLATLHQICL
     SHLTELQTLS TTQVRNHNTI KLQNF
//
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