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GACEE_DICDI
ID   GACEE_DICDI             Reviewed;         570 AA.
AC   Q54E35;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Rho GTPase-activating protein gacEE;
DE   AltName: Full=GTPase activating factor for raC protein EE;
GN   Name=gacEE; ORFNames=DDB_G0291840;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC       transduction pathway. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL61541.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000185; EAL61541.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_629952.1; XM_629950.1.
DR   AlphaFoldDB; Q54E35; -.
DR   SMR; Q54E35; -.
DR   STRING; 44689.DDB0233786; -.
DR   PaxDb; Q54E35; -.
DR   EnsemblProtists; EAL61541; EAL61541; DDB_G0291840.
DR   GeneID; 8628358; -.
DR   KEGG; ddi:DDB_G0291840; -.
DR   dictyBase; DDB_G0291840; gacEE.
DR   eggNOG; KOG1032; Eukaryota.
DR   eggNOG; KOG4270; Eukaryota.
DR   InParanoid; Q54E35; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR   Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR   PRO; PR:Q54E35; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.60.40.150; -; 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; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   Calcium; Cytoplasm; GTPase activation; Metal-binding; Reference proteome.
FT   CHAIN           1..570
FT                   /note="Rho GTPase-activating protein gacEE"
FT                   /id="PRO_0000380198"
FT   DOMAIN          127..233
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          224..343
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          381..567
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   BINDING         260
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         260
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         266
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         312
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         312
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         314
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         314
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         320
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ   SEQUENCE   570 AA;  65111 MW;  8943C4A453FE39E3 CRC64;
     MESVTTTIQC MGIKDSCNKK KIFQGGKSKI IEFQVKYENS DEVLNFQTTQ SAINKLISEL
     KKEIYSINLP ISNYSVTSSS ALQDINLLCQ CISSTPKIQR SLSFVNFIET ENNLTVSSTF
     IFDFIKNSDI SGVLLKTKNN NKRTKKERLC VIKYSRVLYY FSETGGGSST DINSTEVKKK
     RCKGLKFLDD CKITEKGENY FQLKTSNNET YVFTTPTNDE CDRWVTTINN CIDYITKSTY
     RVSGQVQGTV VKSRNLAAKD LNGKSDPFVI IKAEQQQHRT QTIYKSLNPQ FNEAFHFDIT
     KHQGYVYFFV WDEDKFKTAD FMGEVAVPLS LLPPNGSEIS LWLPLSPRNS KDKVSGDILI
     KIRYFFSPDQ IEVSPTSIYG NSLEAIVKNR PEICKNQVPN ILYQFIEFFE QHLNEEGLFR
     ICGNSTEIKF IKNQVNTDTQ ITFNPSSVHA YAGAFKLFFR ELPEPLFTFN QYDNLINLAK
     KSTELQPLIE IIKTFPICHL NVLKLLLPFF GKIAANSKSN LMNHSNLSIV FGPSFLRVKD
     ESHVNLMEMI LVNDIAKFVF ENSQQILKSI
 
 
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