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YEH1_SCHPO
ID   YEH1_SCHPO              Reviewed;         945 AA.
AC   O13944; Q9P7N7; Q9US66;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Oxysterol-binding protein homolog C23H4.01c;
GN   ORFNames=SPAC23H4.01c, SPAP27G11.01;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 391-607, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-419; SER-421 AND
RP   SER-503, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11656.1; -; Genomic_DNA.
DR   EMBL; AB028015; BAA87319.1; -; Genomic_DNA.
DR   RefSeq; NP_593405.2; NM_001018838.2.
DR   AlphaFoldDB; O13944; -.
DR   SMR; O13944; -.
DR   BioGRID; 278287; 1.
DR   STRING; 4896.SPAC23H4.01c.1; -.
DR   iPTMnet; O13944; -.
DR   MaxQB; O13944; -.
DR   PaxDb; O13944; -.
DR   PRIDE; O13944; -.
DR   EnsemblFungi; SPAC23H4.01c.1; SPAC23H4.01c.1:pep; SPAC23H4.01c.
DR   GeneID; 2541796; -.
DR   KEGG; spo:SPAC23H4.01c; -.
DR   PomBase; SPAC23H4.01c; -.
DR   VEuPathDB; FungiDB:SPAC23H4.01c; -.
DR   eggNOG; KOG1737; Eukaryota.
DR   HOGENOM; CLU_007105_4_0_1; -.
DR   InParanoid; O13944; -.
DR   OMA; WHLRASN; -.
DR   PhylomeDB; O13944; -.
DR   Reactome; R-SPO-192105; Synthesis of bile acids and bile salts.
DR   PRO; PR:O13944; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR   GO; GO:0008142; F:oxysterol binding; ISO:PomBase.
DR   GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR   GO; GO:0120015; F:sterol transfer activity; ISO:PomBase.
DR   GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0035621; P:ER to Golgi ceramide transport; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0030011; P:maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0015918; P:sterol transport; ISO:PomBase.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   InterPro; IPR037239; OSBP_sf.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041680; PH_8.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR10972; PTHR10972; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF15409; PH_8; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF101576; SSF101576; 1.
DR   SUPFAM; SSF144000; SSF144000; 1.
DR   PROSITE; PS50866; GOLD; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lipid transport; Lipid-binding; Phosphoprotein;
KW   Reference proteome; Transport.
FT   CHAIN           1..945
FT                   /note="Oxysterol-binding protein homolog C23H4.01c"
FT                   /id="PRO_0000100392"
FT   DOMAIN          1..131
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   DOMAIN          149..243
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          396..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   945 AA;  106810 MW;  B8E264181310A4BF CRC64;
     METVEIRSKS LLIQWLTVES NSLLSWQLHV KRKSIKFDIY HKKNDTSSLL DGSNKNTDRS
     ILHTKRQHTH EAGIKKLSAA GLELFYQGER CMSEKPSEGS VYIENGGLYA FVFDNTFSKT
     KPKTVTFLLT AQPYNGPRIP NASVHGSPKQ IISGTLLKKR RKKGQGYARR YFTLNMVEGT
     ISYYANENSS VMRGKIPLSI AVISVAAETH EINVDSGVEL WNLRAHTHQD WLRWCNALEK
     AKNSQTSSKL VVDERTQESS SNQLVSIYSR LRECLDIAQL YRTSRIKSAS SHNFSVPEIR
     IQLPGDAKEN KETRTSVEIT AAENAQAAVT LRKVTRQLGS LLHELECFIQ HHEYTKERTA
     QSSPSSRMSM DSNFEQHWYD AEDYESTTSQ LNHYSESGAH AADATKSSVA HNEKVEDISD
     SDIPIMKTSS NSTSLDADRD SDTSSISDTS SNSSAPHEQL NATSLASTVD ESSRSPPLPE
     VESNKENDIK RKQPFHDLMD SSSPDDSSFA NAKSDEEVQK PSVSKNIADG AVISIPKPLT
     PKPSDSNSLY PLPHSKVGRR KNIPAITVPP PSILSILRKN IGKDISSIPA PVVSNEPCNL
     LQRCAEDLEY SNMLDKANEC DDDIKIFYVA AFAVSNFSNM RHKERSVRKV FSPLLGETFE
     LVREDRNYRF LAEKVCHRPL IIACHAESRN WIWNHSPKPI QKFWGKSVEL NTLGPVTIKL
     ACGTEFSFMK PACFLKNVAI GEKYVEPYDH MEIVDETTGD KAVIRFKSGG MFSGRSEDVL
     VTVIRSNGEE DPKCLQGKWT SHLDFVNTDE GNVIERIWEV GPLVDKPEDH CGMTVFAAQM
     NEITDLEKDK LPPTDTRLRP DQRYRENNDL DHAEPLKLEL EQKQRERRKE MEEKDIKWEP
     RWFVPSVAGD DEDEDGSGPI WQLKKENNYW ESRENSTWSS CPKLW
 
 
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