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RGA7_SCHPO
ID   RGA7_SCHPO              Reviewed;         695 AA.
AC   O94466;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable Rho-GTPase-activating protein 7;
GN   Name=rga7; ORFNames=SPBC23G7.08c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND SER-497, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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DR   EMBL; CU329671; CAA22624.1; -; Genomic_DNA.
DR   PIR; T39954; T39954.
DR   RefSeq; NP_595866.1; NM_001021771.2.
DR   AlphaFoldDB; O94466; -.
DR   SMR; O94466; -.
DR   BioGRID; 277161; 27.
DR   STRING; 4896.SPBC23G7.08c.1; -.
DR   iPTMnet; O94466; -.
DR   MaxQB; O94466; -.
DR   PaxDb; O94466; -.
DR   PRIDE; O94466; -.
DR   EnsemblFungi; SPBC23G7.08c.1; SPBC23G7.08c.1:pep; SPBC23G7.08c.
DR   GeneID; 2540635; -.
DR   KEGG; spo:SPBC23G7.08c; -.
DR   PomBase; SPBC23G7.08c; rga7.
DR   VEuPathDB; FungiDB:SPBC23G7.08c; -.
DR   eggNOG; KOG1450; Eukaryota.
DR   HOGENOM; CLU_010730_3_0_1; -.
DR   InParanoid; O94466; -.
DR   OMA; IADSGWQ; -.
DR   PhylomeDB; O94466; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR   Reactome; R-SPO-9013148; CDC42 GTPase cycle.
DR   Reactome; R-SPO-9013405; RHOD GTPase cycle.
DR   Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR   Reactome; R-SPO-9035034; RHOF GTPase cycle.
DR   PRO; PR:O94466; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030479; C:actin cortical patch; ISO:PomBase.
DR   GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; IDA:PomBase.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0032154; C:cleavage furrow; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR   GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR   GO; GO:0005096; F:GTPase activator activity; IMP:PomBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISO:PomBase.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:PomBase.
DR   GO; GO:0140278; P:mitotic division septum assembly; IMP:PomBase.
DR   GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; IMP:PomBase.
DR   GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IMP:PomBase.
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; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; GTPase activation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..695
FT                   /note="Probable Rho-GTPase-activating protein 7"
FT                   /id="PRO_0000097315"
FT   DOMAIN          33..307
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          506..692
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   695 AA;  76679 MW;  1DEAF1328D576263 CRC64;
     MLSAPSSSTT PASPPTSPPN TTSSDDFAVL KEPKVEAILN SELGLAILND RIKDYLLTCK
     ELAGFFKKRS ILEEESGKNL QKLAKSYLET FQSKHHSPQS FSASVITSME IHEQLANHSL
     TLQKTLSAFS DQVIEFHKNA ERKRKSIKEY AKKQENAYLE AVMQMDKSKS RFKGAETEYN
     RALDNKNTGD SQKKVGFFKP KSNAQLTKLE DEARLKAENA ESDMHSKIEN AQNVQKQLLC
     IHRPNYIKQF FSLQREIESS LIANYLRYTK LCESNTLLNG LTIRPQKPTP TNCGLQHALD
     NINANTDFVQ YVLHASIKHE DNKNPTDASK TKIIQPPSSY GTGSSAGKTN PPVNPTIKVT
     AAIPSPLQNT NPAPSTFPNP SVASPAFPNS STSNPSTAPA SASPLASTLK PSTANDTNGS
     SSSSSSNPRT SSPLASNAEN KPPVAQQSPP VLLPTLPPIQ TTTIQTSREV APPPSSINSN
     RAASPFRPTS VSPQPSSPTK SLLFGARLDA IILREHSNIP NIVMQCTSQV ENFGLNLQGI
     YRVPSSSARV NMLRSQFENN PLLQLHTPED YENDVHAVAD LLKIFFRELR EPLIPDNHQR
     DFIDAGNVED ESRRRDAVHR AINDLPDANY STIRHLTIHL AKIKENSDVN KMSTNNLAII
     WGPTIIKQAT IPEISSFSRT IEILIDYCFT IFDYD
 
 
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