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SLM1_SCHPO
ID   SLM1_SCHPO              Reviewed;         498 AA.
AC   O94447;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Cytoskeletal signaling protein slm1;
GN   Name=slm1; ORFNames=SPAC637.13c;
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-175 AND SER-312, 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).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21900489; DOI=10.1091/mbc.e11-07-0605;
RA   Kabeche R., Baldissard S., Hammond J., Howard L., Moseley J.B.;
RT   "The filament-forming protein Pil1 assembles linear eisosomes in fission
RT   yeast.";
RL   Mol. Biol. Cell 22:4059-4067(2011).
CC   -!- FUNCTION: Effector of the TORC2- and calcineurin-signaling pathways.
CC       Mediates actin polarization via inhibition of calcineurin-dependent
CC       transcription (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:21900489}.
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DR   EMBL; CU329670; CAA22592.1; -; Genomic_DNA.
DR   PIR; T39005; T39005.
DR   RefSeq; NP_594631.1; NM_001020059.2.
DR   AlphaFoldDB; O94447; -.
DR   SMR; O94447; -.
DR   BioGRID; 280088; 17.
DR   STRING; 4896.SPAC637.13c.1; -.
DR   iPTMnet; O94447; -.
DR   SwissPalm; O94447; -.
DR   MaxQB; O94447; -.
DR   PaxDb; O94447; -.
DR   PRIDE; O94447; -.
DR   EnsemblFungi; SPAC637.13c.1; SPAC637.13c.1:pep; SPAC637.13c.
DR   GeneID; 2543674; -.
DR   KEGG; spo:SPAC637.13c; -.
DR   PomBase; SPAC637.13c; slm1.
DR   VEuPathDB; FungiDB:SPAC637.13c; -.
DR   eggNOG; ENOG502QRAF; Eukaryota.
DR   HOGENOM; CLU_554501_0_0_1; -.
DR   InParanoid; O94447; -.
DR   OMA; ENNNRQD; -.
DR   PhylomeDB; O94447; -.
DR   PRO; PR:O94447; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0032126; C:eisosome; ISO:PomBase.
DR   GO; GO:0070250; C:mating projection membrane; IDA:PomBase.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:PomBase.
DR   GO; GO:1904600; P:actin fusion focus assembly; IMP:PomBase.
DR   GO; GO:0140253; P:cell-cell fusion; IMP:PomBase.
DR   CDD; cd13311; PH_Slm1; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR043453; Slm1_PH.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..498
FT                   /note="Cytoskeletal signaling protein slm1"
FT                   /id="PRO_0000310807"
FT   DOMAIN          300..405
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   498 AA;  56088 MW;  A50AF74C663953F1 CRC64;
     MELSGKSEFP TRTEIPNQAS NGDAVPNTDA YMGLCNSLTY RFEGWRHLVE NLIAFFKQLE
     STSKNNAKEY MKLSKVIVHP YKDANVFEEH GIQDIFAALR DQTAAIASDS EQISIQLPGT
     IINILELLRE DLREHCKKIA AEGTKGVKVV EKQRAETQKY LSLLDRALLP WRASSPPTVN
     IKNDPFIVDR QVLNCLARQV QEENNHSVAV AQLQEFSFRF EQNLIAKIKD TVKQFEGMMN
     QTHVKAINHL QEVVRVSEAQ TLAGEWTGYA KREPEFIHGS VPPRSVDAIK YPGKNDQPTV
     PIMAGYLIRK TSFLKKKQRG FYAFTHSGYL YEFKSSDSLQ DPEPEFALYI PDCLIGRPSE
     KKPKFKITGK DATKKIFGAR NDYAFRASNN TELMRWWEAL NTHIANVNYI QPLSNANGPS
     AVSDSDDDDD DPNDFRPAVE RQSSTMNTRM SQPSSAVNTN RSYGSEQIPS YADSQGNSGA
     NNNFIYNASA TGHNAWNV
 
 
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