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MNN9_SCHPO
ID   MNN9_SCHPO              Reviewed;         337 AA.
AC   O36022;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Mannan polymerase complex subunit mnn9;
GN   Name=mnn9 {ECO:0000250|UniProtKB:P39107}; ORFNames=SPAC4F10.10c;
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] {ECO:0000312|EMBL:CAB11713.1}
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] {ECO:0000305}
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: Required for the addition of the long alpha 1,6-mannose
CC       backbone of N-linked glycans on cell wall and periplasmic proteins.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P39107}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16823372}. Note=Cis-Golgi. Recycles between
CC       endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P39107,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family. {ECO:0000255}.
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DR   EMBL; CU329670; CAB11713.1; -; Genomic_DNA.
DR   PIR; T38814; T38814.
DR   RefSeq; NP_594753.1; NM_001020180.2.
DR   AlphaFoldDB; O36022; -.
DR   SMR; O36022; -.
DR   BioGRID; 279680; 6.
DR   STRING; 4896.SPAC4F10.10c.1; -.
DR   CAZy; GT62; Glycosyltransferase Family 62.
DR   MaxQB; O36022; -.
DR   PaxDb; O36022; -.
DR   PRIDE; O36022; -.
DR   EnsemblFungi; SPAC4F10.10c.1; SPAC4F10.10c.1:pep; SPAC4F10.10c.
DR   GeneID; 2543252; -.
DR   KEGG; spo:SPAC4F10.10c; -.
DR   PomBase; SPAC4F10.10c; mnn9.
DR   VEuPathDB; FungiDB:SPAC4F10.10c; -.
DR   eggNOG; ENOG502QRPX; Eukaryota.
DR   HOGENOM; CLU_017872_4_0_1; -.
DR   InParanoid; O36022; -.
DR   OMA; LVYHYNE; -.
DR   PhylomeDB; O36022; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O36022; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR   GO; GO:0000136; C:mannan polymerase complex; IPI:PomBase.
DR   GO; GO:0140497; C:mannan polymerase II complex; ISO:PomBase.
DR   GO; GO:0000030; F:mannosyltransferase activity; IMP:PomBase.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..337
FT                   /note="Mannan polymerase complex subunit mnn9"
FT                   /id="PRO_0000316855"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P39107, ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..337
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P39107, ECO:0000255"
SQ   SEQUENCE   337 AA;  38297 MW;  4309DAA98590478A CRC64;
     MRVYNKSRIV GQLLFVALGI TFIYYLFTPS VNSNAKVQIE NRGGNSYEIY DMNKITESSD
     PIRNKEEVLI LTPIARFYPQ YWKNLLELDY PRNLISLGFI VPSSKDGAKV HRELRNAINA
     VQKGPGDKRF ADVKILIQDS DLSSGQSEAE RHKFSAQKER RGKLAATRNT LLLSTLKPST
     SWVLWLDSDI VETPSTLIQD LAEHNEDVLV ANCFQKQGDK LTPYDFNSWV DSQTAQELAS
     HMDRDEILLE GYAELPTYRM LMAKIYEEHK DPSTIMALDG VGTTALLVKA SVHRDGALFP
     TFPFYHLIES EGFAKMAKRL GHGVYGLPYY LVFHHNE
 
 
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