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PSY1_SCHPO
ID   PSY1_SCHPO              Reviewed;         284 AA.
AC   Q9USH7;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Syntaxin-like protein psy1;
GN   Name=psy1; Synonyms=sso1; ORFNames=SPCC825.03c;
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], 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11739793};
CC       Single-pass type IV membrane protein {ECO:0000269|PubMed:11739793}.
CC       Prospore membrane {ECO:0000269|PubMed:11739793}. Note=During vegetative
CC       growth located at the plasma membrane. As meiosis II is initiated
CC       located at the forespore membrane.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; CU329672; CAB58411.1; -; Genomic_DNA.
DR   PIR; T41624; T41624.
DR   RefSeq; NP_588053.1; NM_001023045.2.
DR   AlphaFoldDB; Q9USH7; -.
DR   SMR; Q9USH7; -.
DR   BioGRID; 275943; 11.
DR   STRING; 4896.SPCC825.03c.1; -.
DR   SwissPalm; Q9USH7; -.
DR   MaxQB; Q9USH7; -.
DR   PaxDb; Q9USH7; -.
DR   EnsemblFungi; SPCC825.03c.1; SPCC825.03c.1:pep; SPCC825.03c.
DR   GeneID; 2539377; -.
DR   KEGG; spo:SPCC825.03c; -.
DR   PomBase; SPCC825.03c; psy1.
DR   VEuPathDB; FungiDB:SPCC825.03c; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   HOGENOM; CLU_042423_0_1_1; -.
DR   InParanoid; Q9USH7; -.
DR   OMA; RWICFIL; -.
DR   PhylomeDB; Q9USH7; -.
DR   Reactome; R-SPO-114516; Disinhibition of SNARE formation.
DR   Reactome; R-SPO-199992; trans-Golgi Network Vesicle Budding.
DR   Reactome; R-SPO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   PRO; PR:Q9USH7; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR   GO; GO:0044853; C:plasma membrane raft; IDA:PomBase.
DR   GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR   GO; GO:0070056; C:prospore membrane leading edge; IDA:PomBase.
DR   GO; GO:0070057; C:prospore membrane spindle pole body attachment site; IDA:PomBase.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0030437; P:ascospore formation; IGI:PomBase.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   CDD; cd00179; SynN; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; PTHR19957; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Coiled coil; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..284
FT                   /note="Syntaxin-like protein psy1"
FT                   /id="PRO_0000210269"
FT   TRANSMEM        260..280
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          181..243
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          23..57
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   284 AA;  32550 MW;  C7E3AB14A61CB256 CRC64;
     MNKANDYTLG VEMIPLSMGE FFEEIDHIRD AIRQIEDNVG RIEMLHQQSL QEIDEANIAA
     TTRHLEGYTS DTRRLQTSVQ LAIRSLESQN MQLPPDNDTA TRKTQTEAVK KKFMDQIRHF
     LQIEKTYRAQ YEQRMRRQLE IANPRATEDD FQTAINEENG GQVFAQALLR SNRSGEARTA
     LREVQERHAD IKRIERTIAE LAQLFQDMAT MVQEQEPMVD KIVTDAVNVR TNMGEGTQHM
     DRAIKSARAA RKKKWICFGI CVVIICVIVA VLCGVLIPVL GNRH
 
 
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