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GACR_DICDI
ID   GACR_DICDI              Reviewed;         783 AA.
AC   Q54XT6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Rho GTPase-activating protein gacR;
DE   AltName: Full=GTPase activating factor for raC protein R;
GN   Name=gacR; ORFNames=DDB_G0278755;
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AAFI02000024; EAL67979.1; -; Genomic_DNA.
DR   RefSeq; XP_641917.1; XM_636825.1.
DR   AlphaFoldDB; Q54XT6; -.
DR   SMR; Q54XT6; -.
DR   STRING; 44689.DDB0233843; -.
DR   PaxDb; Q54XT6; -.
DR   EnsemblProtists; EAL67979; EAL67979; DDB_G0278755.
DR   GeneID; 8621676; -.
DR   KEGG; ddi:DDB_G0278755; -.
DR   dictyBase; DDB_G0278755; gacR.
DR   eggNOG; KOG4406; Eukaryota.
DR   HOGENOM; CLU_358064_0_0_1; -.
DR   InParanoid; Q54XT6; -.
DR   OMA; RPQSVMF; -.
DR   PhylomeDB; Q54XT6; -.
DR   Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR   Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR   Reactome; R-DDI-9013409; RHOJ GTPase cycle.
DR   Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR   PRO; PR:Q54XT6; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; GTPase activation; Reference proteome.
FT   CHAIN           1..783
FT                   /note="Rho GTPase-activating protein gacR"
FT                   /id="PRO_0000380216"
FT   DOMAIN          319..509
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          262..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          138..188
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        272..289
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  86060 MW;  57AD5D7F7B84F781 CRC64;
     MKKFNQTFSS VKDLIGNKKE TLTEFPDYIY KTKSLEDLKG YTRTLNLKLT KHSKTNQLLI
     EENKQLSEQI LLYSNLFINN EESSLNVCEP LSNVFKIVGE MINEIENYRQ TFEQSISQKW
     LQQLNEYGKS DCKDGQLAKN RFDKARLSFD EASEQFKQLR KKQNNINNEK LLEAEEDLDY
     ATQQFSDIAS ESLQTMDDII VKHNLDSFES ASSTIQSYKD FFQKGLDHCL SVQSDLEIQK
     HAMSKYKQQL LEKKKLRSTV VQFEQTNSSR TISLPPPPPP KPTSSTPSSS PSPSPSSSII
     NIHNNYIAMP KGNTKVFGMA LSTITEREKS DIPMIIDKSI QFLLLEENIT QEGIFRVSPN
     QKQLTDLKNN VNAGYITTLD GIDDAHLISS FVKAFLREMP IPLFTFDLYH SLVDCVINEE
     KYDCDKIKIS NAIVLVLQKL PKPNFLLAKS LISLLWKIST KSSQNKMTTS NLAVTVAPNV
     LYPKLLDIRS LTNANATIEF IISNFNNIFN NQLISNLYNN SCGVSGGSSG GGGGGGSSGG
     VANPRHSVLP PSLPARPQSV MFKNTPLSVN TSSSQSSSSS SSSSFASSAS PPPTPTKPPS
     SSSSPIITTT SPNSNTNINS NTSVNTNINP RHSVLPPSLP PKKISSSSNS LPSPPPPSSP
     SIPEKSQNNI TPTILSSSLS APTSPTTTTT TNPLRSSTGS PKPISNRVSM YLQNSNTGVP
     LPSQKPQRVI SNNNTTTNSR PLSNSLDLPP PLAPVGMPLE TLEPIQRNLT SNEAITISEV
     NWN
 
 
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