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ZDS1_SCHPO
ID   ZDS1_SCHPO              Reviewed;         938 AA.
AC   O14100;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Protein zds1;
DE   AltName: Full=Meiotically up-regulated gene 88 protein;
GN   Name=zds1; Synonyms=mug88; ORFNames=SPAC31F12.01, SPAC637.14;
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   FUNCTION IN MEIOSIS.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16322512; DOI=10.1534/genetics.105.050906;
RA   Yakura M., Ozoe F., Ishida H., Nakagawa T., Tanaka K., Matsuda H.,
RA   Kawamukai M.;
RT   "zds1, a novel gene encoding an ortholog of Zds1 and Zds2, controls sexual
RT   differentiation, cell wall integrity and cell morphology in fission
RT   yeast.";
RL   Genetics 172:811-825(2006).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Has a role in establishing cell polarity. Also required for
CC       maintenance of cell wall integrity, sexual differentiation, calcium
CC       tolerance and cell morphology. Involved in Ras-MAPK signaling pathway
CC       at cell cortex. Has a role in meiosis. {ECO:0000269|PubMed:16303567,
CC       ECO:0000269|PubMed:16322512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16322512,
CC       ECO:0000269|PubMed:16823372}. Note=Localizes to the septum and cell
CC       cortex.
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DR   EMBL; CU329670; CAA22593.1; -; Genomic_DNA.
DR   PIR; T38616; T38616.
DR   PIR; T39006; T39006.
DR   RefSeq; NP_594632.1; NM_001020060.2.
DR   AlphaFoldDB; O14100; -.
DR   BioGRID; 279619; 72.
DR   STRING; 4896.SPAC31F12.01.1; -.
DR   iPTMnet; O14100; -.
DR   MaxQB; O14100; -.
DR   PaxDb; O14100; -.
DR   PRIDE; O14100; -.
DR   EnsemblFungi; SPAC31F12.01.1; SPAC31F12.01.1:pep; SPAC31F12.01.
DR   GeneID; 2543190; -.
DR   KEGG; spo:SPAC31F12.01; -.
DR   PomBase; SPAC31F12.01; zds1.
DR   VEuPathDB; FungiDB:SPAC31F12.01; -.
DR   eggNOG; ENOG502RC08; Eukaryota.
DR   HOGENOM; CLU_312642_0_0_1; -.
DR   InParanoid; O14100; -.
DR   OMA; QYEMQHR; -.
DR   PhylomeDB; O14100; -.
DR   PRO; PR:O14100; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000935; C:division septum; IDA:PomBase.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; ISO:PomBase.
DR   GO; GO:0030437; P:ascospore formation; IGI:PomBase.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0071277; P:cellular response to calcium ion; IMP:PomBase.
DR   GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR   GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IMP:PomBase.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; NAS:PomBase.
DR   InterPro; IPR040206; Zds1/2.
DR   InterPro; IPR013941; ZDS1_C.
DR   PANTHER; PTHR28089; PTHR28089; 2.
DR   Pfam; PF08632; Zds_C; 1.
DR   SMART; SM01327; Zds_C; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Cytoplasm; Meiosis; Reference proteome.
FT   CHAIN           1..938
FT                   /note="Protein zds1"
FT                   /id="PRO_0000249236"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..610
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..738
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   938 AA;  103098 MW;  6E20EF9A8A16149A CRC64;
     MSSSSVSNTL SIETKSDPKD PAFVASQEST ECNEHDTTQL SGSSSEPLEN NSSLTRSTDD
     PSVEIRSKLV SPDNEANLLS DQNITISNEN NNENDTTEEA ETSSGNEAAD DEDSSSDAQS
     SVPSFSEIHD GMSEEELDKE RKTLTHLRRI SLQGADDPEI PTDWSVAMSP PETEQDASTL
     FWVPANLHPE LNPTGWKSFL DLQVKNLKSP TATDTSSSPL EHIRSLRRRK SLLSRQVKAD
     DAVINYQDGS PIVEKAYLKR HRSLRLNELE HLESLARDPH RMVSLVDGMS NGSPEDSPLL
     VSPNHFLQRS SRTTIRRTGA SIRTIHRGKT STLSGNRSHS ILQKPTDTSP LHKIEPISAD
     ELVESDDSRT SALSNSQNPS DDVENQSDQA LEVLSLTNPP KIDNASADTT LHKETNKIDK
     LYVSENKAES AVASESSLSE GTLALKAPAP ENKPEKSSTS KPPVPENKAE DSVVLKSSVP
     EDKSENSIAS KPSATEGIPE NAIALQSSVP ENKAEDSVVL KSSVPEDKSE DSVPSKSSVL
     EDKHENSVEI DKKADDSLPS NNKTEGYTPS VVREEKNYSE PNASPSVIPP RVPTPVPGRT
     LSPKPTRIPT PIPSSLNVSL ESSKKPEIFH ERHIPTPETG PNKPSKNNIL KSTQVPVTPK
     QKSSTANKGS TSSPSPPSSE SKKTKRSWGR LFVSGDSDKE HKEHKKDKQK KKNDQISSSS
     KSASSFKKDR DKESIFGSLF GSKKKQTEIP PVSSSPPHND APPKAKPISA PSELPNTTSV
     AEAKCQTVTD DEGTDQQSDE KSTEPKTFIP DKDYYWSRFP ICTERAIYRL SHIKLSNAHR
     PLFQQVLLSN FMYSYLDLIS RISSNRPMNN VQQSTAKPIR KDINGQQRRS EFSAENVKNE
     LENLSYQFGD QRKRNLNRKG STIHTVSQNI QKVSKNAK
 
 
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