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PUN1_SCHPO
ID   PUN1_SCHPO              Reviewed;         288 AA.
AC   O13729;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=SUR7 family protein pun1;
GN   Name=pun1; Synonyms=sur7; ORFNames=SPAC15A10.09c;
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   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: Contributes to the wild-type cellular response to nitrogen
CC       stress through signaling pathways that regulate the expression of genes
CC       involved in amino acid biosynthesis. Required for wild-type filamentous
CC       growth, cell growth, and cell-cell adhesion (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}. Cell membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:16823372}.
CC       Cell septum {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SUR7 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB10106.1; -; Genomic_DNA.
DR   PIR; T37709; T37709.
DR   RefSeq; NP_594296.1; NM_001019719.2.
DR   AlphaFoldDB; O13729; -.
DR   BioGRID; 279198; 12.
DR   STRING; 4896.SPAC15A10.09c.1; -.
DR   MaxQB; O13729; -.
DR   PaxDb; O13729; -.
DR   EnsemblFungi; SPAC15A10.09c.1; SPAC15A10.09c.1:pep; SPAC15A10.09c.
DR   GeneID; 2542748; -.
DR   KEGG; spo:SPAC15A10.09c; -.
DR   PomBase; SPAC15A10.09c; pun1.
DR   VEuPathDB; FungiDB:SPAC15A10.09c; -.
DR   eggNOG; ENOG502QRB5; Eukaryota.
DR   HOGENOM; CLU_1190478_0_0_1; -.
DR   InParanoid; O13729; -.
DR   OMA; ILCIINQ; -.
DR   PhylomeDB; O13729; -.
DR   PRO; PR:O13729; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISM:PomBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0044853; C:plasma membrane raft; ISO:PomBase.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   InterPro; IPR009571; SUR7/Rim9-like_fungi.
DR   Pfam; PF06687; SUR7; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Golgi apparatus; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..288
FT                   /note="SUR7 family protein pun1"
FT                   /id="PRO_0000116645"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..288
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   288 AA;  31450 MW;  AEAA2FB34926B1B3 CRC64;
     MGMGFNPIKA LFTGIGTVCV GVGALLSILC IINQTQHNIA FQNIYFIQLN TTSIFSVANQ
     TAVVNNTSNL LNELTGTLVD TLETYIDQGA TDLIEQVEQE MKDVSELPDW YSIGLWNYCQ
     GNSSDYTNPT YCSTPSPSYY FNPLTMLETS INNATGSQIN ITLPSEVDLG LKVLKGACYA
     MRAMYILGFI FFALTIVSIV ISCLPFFGPL FLNVFSFFAT IFTFIAAVIA VATYRIAISE
     LEKNIEILNI PIVLGKKIYA YSFLSAAAGL AACILYFIGN LTSGYSPL
 
 
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