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WSC1_SCHPO
ID   WSC1_SCHPO              Reviewed;         374 AA.
AC   P87179; Q9USB7; Q9USD8;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 3.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cell wall integrity and stress response component 1;
DE   Flags: Precursor;
GN   Name=wsc1; ORFNames=SPBC30B4.01c, SPBC3D6.14c;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 31-66 AND 136-345, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   O-MANNOSYLATION.
RX   PubMed=15948957; DOI=10.1111/j.1365-2958.2005.04692.x;
RA   Willer T., Brandl M., Sipiczki M., Strahl S.;
RT   "Protein O-mannosylation is crucial for cell wall integrity, septation and
RT   viability in fission yeast.";
RL   Mol. Microbiol. 57:156-170(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP   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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10759889}; Single-
CC       pass membrane protein {ECO:0000269|PubMed:10759889}.
CC   -!- PTM: O-mannosylated. {ECO:0000269|PubMed:15948957}.
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DR   EMBL; CU329671; CAB09116.1; -; Genomic_DNA.
DR   EMBL; AB027834; BAA87138.1; -; Genomic_DNA.
DR   EMBL; AB027890; BAA87194.1; -; Genomic_DNA.
DR   PIR; T40167; T40167.
DR   RefSeq; NP_595526.2; NM_001021435.3.
DR   AlphaFoldDB; P87179; -.
DR   SMR; P87179; -.
DR   BioGRID; 277485; 7.
DR   STRING; 4896.SPBC30B4.01c.1; -.
DR   iPTMnet; P87179; -.
DR   MaxQB; P87179; -.
DR   PaxDb; P87179; -.
DR   PRIDE; P87179; -.
DR   EnsemblFungi; SPBC30B4.01c.1; SPBC30B4.01c.1:pep; SPBC30B4.01c.
DR   GeneID; 2540969; -.
DR   KEGG; spo:SPBC30B4.01c; -.
DR   PomBase; SPBC30B4.01c; wsc1.
DR   VEuPathDB; FungiDB:SPBC30B4.01c; -.
DR   eggNOG; KOG4157; Eukaryota.
DR   HOGENOM; CLU_024893_0_1_1; -.
DR   InParanoid; P87179; -.
DR   OMA; GNCQLVC; -.
DR   PRO; PR:P87179; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:PomBase.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IC:PomBase.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:PomBase.
DR   GO; GO:1903338; P:regulation of cell wall organization or biogenesis; EXP:PomBase.
DR   InterPro; IPR002889; WSC_carb-bd.
DR   Pfam; PF01822; WSC; 1.
DR   SMART; SM00321; WSC; 1.
DR   PROSITE; PS51212; WSC; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..374
FT                   /note="Cell wall integrity and stress response component 1"
FT                   /id="PRO_0000041487"
FT   TOPO_DOM        30..292
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..374
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..119
FT                   /note="WSC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT   REGION          132..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   374 AA;  38398 MW;  C7942A0E0E47941E CRC64;
     MVFLNSSPFK GRLLFFVYLL IISTRLVAAD MNTQYGCYLV DSSLTEQGTF TYLDPAYCYN
     NICGGSDNIA FVAIRNNQCY CGSTLTATEV SSSLCTTPCP GYGSLMCGGD LYWSVYLTGN
     GVLQTTVSSS SVSSTTSSSS SSSPSSSSTT TTTSPSSSSS SSSSSSSSSS SSSSSSSSSS
     SSSSSSSSSS SSSSSSSSSS SSSSSSSVPI TSSTSSSHSS SSSSSSSSSS SSRPSSSSSF
     ITTMSSSTFI STVTVTPSSS SSSTSSEVPS STAALALNAS KASNHTSLNA GAIVGIVIGC
     VAFAVVMALC IFLYFYFRRF KIRMSDSANE GKYPSYASEL DSRLDPAMMN RKSSESLADS
     QDYSRKILRV TNLN
 
 
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