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SPO3_SCHPO
ID   SPO3_SCHPO              Reviewed;        1028 AA.
AC   Q9US08;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Sporulation-specific protein 3;
GN   Name=spo3; ORFNames=SPAC607.10;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11739793; DOI=10.1091/mbc.12.12.3955;
RA   Nakamura T., Nakamura-Kubo M., Hirata A., Shimoda C.;
RT   "The Schizosaccharomyces pombe spo3+ gene is required for assembly of the
RT   forespore membrane and genetically interacts with psy1(+)-encoding
RT   syntaxin-like protein.";
RL   Mol. Biol. Cell 12:3955-3972(2001).
RN   [2]
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).
CC   -!- FUNCTION: Has a role in spore morphogenesis. Involved in the assembly
CC       of the forespore membrane. {ECO:0000269|PubMed:11739793}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11739793};
CC       Peripheral membrane protein {ECO:0000269|PubMed:11739793}. Prospore
CC       membrane {ECO:0000269|PubMed:11739793}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11739793}. Note=Associated with the plasma and
CC       forespore membranes.
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DR   EMBL; CU329670; CAB63797.1; -; Genomic_DNA.
DR   PIR; T50230; T50230.
DR   RefSeq; NP_593599.1; NM_001019030.2.
DR   AlphaFoldDB; Q9US08; -.
DR   BioGRID; 279938; 6.
DR   STRING; 4896.SPAC607.10.1; -.
DR   iPTMnet; Q9US08; -.
DR   PaxDb; Q9US08; -.
DR   PRIDE; Q9US08; -.
DR   EnsemblFungi; SPAC607.10.1; SPAC607.10.1:pep; SPAC607.10.
DR   GeneID; 2543520; -.
DR   KEGG; spo:SPAC607.10; -.
DR   PomBase; SPAC607.10; spo3.
DR   VEuPathDB; FungiDB:SPAC607.10; -.
DR   HOGENOM; CLU_298787_0_0_1; -.
DR   OMA; YNILANK; -.
DR   PRO; PR:Q9US08; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR   GO; GO:0070056; C:prospore membrane leading edge; IDA:PomBase.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
PE   4: Predicted;
KW   Cell membrane; Membrane; Reference proteome; Sporulation.
FT   CHAIN           1..1028
FT                   /note="Sporulation-specific protein 3"
FT                   /id="PRO_0000072138"
SQ   SEQUENCE   1028 AA;  119407 MW;  2FE1860008CFB59F CRC64;
     MGILSVIRIF IYCLIRLFSF NSRKRNSSID ELERGEINAF ACDKQNTPSP NSECRPLTPL
     NSPFRRTVEG DTANLQAPSP TACPSFDSAS SIKSSKEDIA CRKLSTERFF YSPNGIDEMK
     KQQQFKKIPT VSITEVEPAF IPSNMEQALF SEEPFVIQDD LSHQINLDDN RKFSRIQKNK
     LDPLITVNLV PIVNGENCFN FYETQMETNF LSPEFIKKPS MVDHKRDSEI NAVTAVSADG
     SFSPLTETLS STISTLSNDS LDGLSSQKNE FTGFNSNSEW IPNDTVDYIC NSDASSVVSN
     LSDFEDCFDQ FGVYDKEYEK KIEKTKRNFP KFQSSATYPP FSAHHQARRN NPQGFRNVKK
     RFQLFKDDCT ALTDSDFLDA LPFFNARVII ALYVEWRLRV YETMIIKGEE SLKNLQRARD
     GPHNKLWLGV FGNKDTIKKL SNYDRRAISN PYVSNHLNFN VRRVKSDTVY IPTILQLLRS
     STQLMTEQAF VASSNLKSTK GLRETRLIQK YKVKGDFEYV YAALYYAAFT QESTLKAVTI
     DDILSEDELE DWWYLNLRYT SFITPQLCFE FLDKEADSCR DRLTEVKSEP PKAVIYEEPL
     NKLSRFSSDR LFTSHELVAI AELISLNEPP LESGKKFYYE EFQKACQKKR DDYRYSPEIE
     FKAAFREKFL QSNEKVPFPR PGEIYEKRCD YFSKYACQNI FISKPLKRSG SIYEVFSDGI
     GRVIYGSVLD YEATRNNILL HFGFEIHCAP SEEELIEREE AFKDFHNMLS FKYSANEIYE
     FCGTHSRAEV HKNEVLKRMA YYLIDENKEI SILRRILSLR IVEPTTSFTR YEYDLWRTFY
     PDVLYLNYSK SGRIPTGSPY IMNGQWRKDL CVSTPPMVDI NSALFPHWFK LSASNLFAGA
     EHAGLNRQKP DKIDLDLYEP LPENSYLVAA ELRVLRALRH KNPENIPLLE KWEVRALHQL
     MAKIRKYYTV PTDYLSLRMD GLQAMLRKRE YMSCYTFNYF DYACLMDHAY RLYEGFNNQV
     VNLPPRIM
 
 
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