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VPS45_SCHPO
ID   VPS45_SCHPO             Reviewed;         558 AA.
AC   Q09805;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Vacuolar protein sorting-associated protein 45;
GN   Name=vps45; ORFNames=SPAC2G11.03c;
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 [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).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17287531; DOI=10.1534/genetics.107.070946;
RA   Miyatake M., Kuno T., Kita A., Katsura K., Takegawa K., Uno S., Nabata T.,
RA   Sugiura R.;
RT   "Valproic acid affects membrane trafficking and cell-wall integrity in
RT   fission yeast.";
RL   Genetics 175:1695-1705(2007).
CC   -!- FUNCTION: Vacuolar protein sorting-associated protein involved in
CC       Golgi-to-vacuole protein transport. {ECO:0000269|PubMed:17287531}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: displays an accumulation of abnormal vesicular
CC       structures and leads to valproic acid sensitivity.
CC       {ECO:0000269|PubMed:17287531}.
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA91168.1; -; Genomic_DNA.
DR   PIR; S62458; S62458.
DR   RefSeq; NP_593083.1; NM_001018481.2.
DR   AlphaFoldDB; Q09805; -.
DR   SMR; Q09805; -.
DR   BioGRID; 277987; 1.
DR   STRING; 4896.SPAC2G11.03c.1; -.
DR   MaxQB; Q09805; -.
DR   PaxDb; Q09805; -.
DR   EnsemblFungi; SPAC2G11.03c.1; SPAC2G11.03c.1:pep; SPAC2G11.03c.
DR   GeneID; 2541485; -.
DR   KEGG; spo:SPAC2G11.03c; -.
DR   PomBase; SPAC2G11.03c; vps45.
DR   VEuPathDB; FungiDB:SPAC2G11.03c; -.
DR   eggNOG; KOG1299; Eukaryota.
DR   HOGENOM; CLU_013933_3_1_1; -.
DR   InParanoid; Q09805; -.
DR   OMA; VHQLNNA; -.
DR   PhylomeDB; Q09805; -.
DR   PRO; PR:Q09805; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000149; F:SNARE binding; ISM:PomBase.
DR   GO; GO:0048210; P:Golgi vesicle fusion to target membrane; ISO:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.1910; -; 1.
DR   Gene3D; 3.40.50.2060; -; 1.
DR   Gene3D; 3.90.830.10; -; 1.
DR   InterPro; IPR043154; Sec-1-like_dom1.
DR   InterPro; IPR043127; Sec-1-like_dom3a.
DR   InterPro; IPR001619; Sec1-like.
DR   InterPro; IPR027482; Sec1-like_dom2.
DR   InterPro; IPR036045; Sec1-like_sf.
DR   PANTHER; PTHR11679; PTHR11679; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR   SUPFAM; SSF56815; SSF56815; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Membrane; Nucleus; Protein transport; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..558
FT                   /note="Vacuolar protein sorting-associated protein 45"
FT                   /id="PRO_0000206317"
SQ   SEQUENCE   558 AA;  63552 MW;  2C138B7CDF5CFEA1 CRC64;
     MDLVSASQSY FKRIFQEVSD LKILLLEEDT TKIVSSCITQ SNLLEQQIYL TVLLGNKREK
     LRHLKCVAFL RPTPTTLRLL CEELRDPKYA EYHLYFTNVI PKSFLERLAE SDDFEAVKSI
     QEFFLDYLVV NNDLASFNIP HIIEDSPDNW QDGAFHRTHQ GIISLLLSLK KKPVIRYDNN
     SLLCLKLAEE VSYTIQHESQ LFNFRKPDTA PILLLLDRKN DPITPLLTQW TYQAMVHELF
     GIDNGRVSFS NSTSDNEKST EIVLNPTLDP FYKETRFDNF GDLGVKIKDY VSHLQTKSTK
     KASEIESIAD MKQFLEAYPE YRRLSGNVSK HVSLVSEISQ VVQRENLLEV GEVEQSLVCN
     EPQSTDFNDI QRLLFSNISE NTKLRLAALY SLRFERIDPA KVSALQQMLI AGGVNPLKVS
     VIPTLLHVAG YSFRQGDVFP PSNLFSRARS GLKGLRGVEN VYIQHNPFLK SILLDLIQGR
     LKETTHPFLN SETRAQTSNE KPQDIIVVIV GGATYEEAHF VSEFNATQPG VRIILAGTTI
     LNSTAYIDDI MYMSTRIK
 
 
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