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MU157_SCHPO
ID   MU157_SCHPO             Reviewed;         509 AA.
AC   Q10449;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Meiotically up-regulated gene 157 protein;
GN   Name=mug157; ORFNames=SPAC12B10.16c;
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   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 meiosis. {ECO:0000269|PubMed:16303567}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329670; CAA94706.1; -; Genomic_DNA.
DR   PIR; T37583; T37583.
DR   RefSeq; NP_594648.1; NM_001020076.2.
DR   AlphaFoldDB; Q10449; -.
DR   SMR; Q10449; -.
DR   BioGRID; 279642; 2.
DR   STRING; 4896.SPAC12B10.16c.1; -.
DR   CAZy; GH125; Glycoside Hydrolase Family 125.
DR   MaxQB; Q10449; -.
DR   PaxDb; Q10449; -.
DR   EnsemblFungi; SPAC12B10.16c.1; SPAC12B10.16c.1:pep; SPAC12B10.16c.
DR   GeneID; 2543213; -.
DR   KEGG; spo:SPAC12B10.16c; -.
DR   PomBase; SPAC12B10.16c; mug157.
DR   VEuPathDB; FungiDB:SPAC12B10.16c; -.
DR   eggNOG; ENOG502QR7D; Eukaryota.
DR   HOGENOM; CLU_023537_1_1_1; -.
DR   InParanoid; Q10449; -.
DR   OMA; QVFECKY; -.
DR   PhylomeDB; Q10449; -.
DR   PRO; PR:Q10449; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004559; F:alpha-mannosidase activity; ISM:PomBase.
DR   GO; GO:0019309; P:mannose catabolic process; IC:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR008313; GH125.
DR   PANTHER; PTHR31047; PTHR31047; 1.
DR   Pfam; PF06824; Glyco_hydro_125; 1.
DR   PIRSF; PIRSF028846; UCP028846; 1.
DR   SMART; SM01149; DUF1237; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Meiosis; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Meiotically up-regulated gene 157 protein"
FT                   /id="PRO_0000116615"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   509 AA;  57153 MW;  296347FA498AFE19 CRC64;
     MKYWQAILFF LFGIAFANNL NIPWKACPNY KTYSGRRHYP ATGPLRLPFQ RPATSCRTFH
     SKSVEQTIED VKEQLEDEDL ARLFENCMPN TLDTTIRWHA ADSHNPQTLV ITGDIPAEWI
     RDSANQLLPY LPLAKSDSPL ATLILGAIQT QAEMLIQFPY CNAFQPPKQS FLSGNDNGQS
     DRVTPAYDPA VVFECKYELD SLASFLKLSY TYWLYTKDQS IFTVKWLAAV ERIIQVLEEQ
     SSPSFDEKTG LPKDPVYTFL RNTDSGTETL GLAGRGFPLN ANASLIRSAF RPSDDACVLQ
     YFIPANAMMV VELSHLNQML QASGHADIAR TALVWANKIQ KGIDQHGIVD HPKFGKVYAY
     EVDGYGSILF MDDANVPSLL SLPYLGFVER DDPVYVNTRK MILSSEGNPY YLKGKVISGI
     GGPHIGLRNV WPMSLIVQAL TSDDDDEIMS LLDVLKHSTA GLGLMHESVD VSSFKSFTRP
     WFSWANSLFA ELILDLLERK PHLLKKNAS
 
 
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