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YCKF_SCHPO
ID   YCKF_SCHPO              Reviewed;         494 AA.
AC   Q9Y7P2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Uncharacterized protein C1450.15;
GN   ORFNames=SPCC1450.15;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- FUNCTION: Acts in the GPI biosynthetic pathway between GlcNAc-PI
CC       synthesis and GPI transfer to protein. Required for the formation of
CC       complete GPI precursors CP1 and CP2 (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGF family. {ECO:0000305}.
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DR   EMBL; CU329672; CAB40182.2; -; Genomic_DNA.
DR   PIR; T40997; T40997.
DR   RefSeq; NP_588314.2; NM_001023304.2.
DR   AlphaFoldDB; Q9Y7P2; -.
DR   SMR; Q9Y7P2; -.
DR   BioGRID; 275857; 1.
DR   STRING; 4896.SPCC1450.15.1; -.
DR   SwissPalm; Q9Y7P2; -.
DR   MaxQB; Q9Y7P2; -.
DR   PaxDb; Q9Y7P2; -.
DR   PRIDE; Q9Y7P2; -.
DR   EnsemblFungi; SPCC1450.15.1; SPCC1450.15.1:pep; SPCC1450.15.
DR   GeneID; 2539289; -.
DR   KEGG; spo:SPCC1450.15; -.
DR   PomBase; SPCC1450.15; -.
DR   VEuPathDB; FungiDB:SPCC1450.15; -.
DR   eggNOG; KOG1210; Eukaryota.
DR   eggNOG; KOG3144; Eukaryota.
DR   HOGENOM; CLU_552265_0_0_1; -.
DR   InParanoid; Q9Y7P2; -.
DR   OMA; RQECILY; -.
DR   Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q9Y7P2; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047560; F:3-dehydrosphinganine reductase activity; ISO:PomBase.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; ISO:PomBase.
DR   GO; GO:0006666; P:3-keto-sphinganine metabolic process; ISO:PomBase.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR   CDD; cd08939; KDSR-like_SDR_c; 1.
DR   InterPro; IPR009580; GPI_biosynthesis_protein_Pig-F.
DR   InterPro; IPR045022; KDSR-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF06699; PIG-F; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..494
FT                   /note="Uncharacterized protein C1450.15"
FT                   /id="PRO_0000339877"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   494 AA;  55644 MW;  5F975D43D9DA4F99 CRC64;
     MGFWGRNSFE ADKKHILVTG GSQGLGKAIA KELVLRGANV TIVARTVTKL QEAVAELSDS
     KIHEDQQVSF ESVDLTSYES VHSMIERLPF CPDHVVHCAG SCIPGFFTEL DPSVFEKQMR
     QNYLASVYVC HAAIRRMKEI SPSYSRRILL VGSLLSSLPI IGYSAYSPVK AAVRNLADSL
     RQECILYDIE VSVYLPSTIL SPGYEQENTL KPELVLQMEG MDSVQTCEEA ASHCMTGLDR
     GDFLIANEST GHLMKNHCRN SSPHDNPILE YLFALVSLLA WPFYRRKLDS LVYQYALEKG
     YRQPSSSRNS WIFTLLLTFT QLTIFYLSLN CLIENPYRML RNTFPIWFIM QTLQIYIQSP
     RPPLTPKRLL AGAASMLIGS LLISFILVAF GAPLLHDFHL TYFCALTLSV FTVYPLASTL
     AFNTEQWQRF LTLKSFNVIG SMQLRSWGPI IGAWFGAFPI PLDWDRPWQA WPITIVIGAF
     LGYAFAAIVG EILQ
 
 
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