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KTR7_YEAST
ID   KTR7_YEAST              Reviewed;         517 AA.
AC   P40504; D6VVK1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Probable mannosyltransferase KTR7;
DE            EC=2.4.1.-;
GN   Name=KTR7; OrderedLocusNames=YIL085C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9090056;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<267::aid-yea72>3.0.co;2-k;
RA   Lussier M., Sdicu A.-M., Winnett E., Vo D.H., Sheraton J., Duesterhoeft A.,
RA   Storms R.K., Bussey H.;
RT   "Completion of the Saccharomyces cerevisiae genome sequence allows
RT   identification of KTR5, KTR6 and KTR7 and definition of the nine-membered
RT   KRE2/MNT1 mannosyltransferase gene family in this organism.";
RL   Yeast 13:267-274(1997).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Possible glycosyltransferase that transfers an alpha-D-
CC       mannosyl residue from GDP-mannose into lipid-linked oligosaccharide,
CC       forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 2890 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
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DR   EMBL; Z46728; CAA86709.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08467.1; -; Genomic_DNA.
DR   PIR; S49795; S49795.
DR   RefSeq; NP_012181.3; NM_001179433.3.
DR   AlphaFoldDB; P40504; -.
DR   SMR; P40504; -.
DR   BioGRID; 34907; 50.
DR   DIP; DIP-4677N; -.
DR   IntAct; P40504; 3.
DR   MINT; P40504; -.
DR   STRING; 4932.YIL085C; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   MaxQB; P40504; -.
DR   PaxDb; P40504; -.
DR   PRIDE; P40504; -.
DR   EnsemblFungi; YIL085C_mRNA; YIL085C; YIL085C.
DR   GeneID; 854724; -.
DR   KEGG; sce:YIL085C; -.
DR   SGD; S000001347; KTR7.
DR   VEuPathDB; FungiDB:YIL085C; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   GeneTree; ENSGT00940000176287; -.
DR   HOGENOM; CLU_024327_2_0_1; -.
DR   InParanoid; P40504; -.
DR   OMA; YQHSTIQ; -.
DR   BioCyc; YEAST:YIL085C-MON; -.
DR   PRO; PR:P40504; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40504; protein.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000030; F:mannosyltransferase activity; ISS:SGD.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR   GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:SGD.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002685; Glyco_trans_15.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31121; PTHR31121; 1.
DR   Pfam; PF01793; Glyco_transf_15; 2.
DR   PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..517
FT                   /note="Probable mannosyltransferase KTR7"
FT                   /id="PRO_0000208248"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        45..517
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          45..85
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          86..517
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        367
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   517 AA;  61438 MW;  3E02FA8AA5456DEF CRC64;
     MAIRLNPKVR RFLLDKCRQK RYGFLFLGCI FAILYCMGTW PFFAKDIVHD PNNLPYSLQD
     YSTDKDEPFF RGCTDTKLYL QNPAYSKMNA SFVMLTRNEE IEDVLKTMRS IEGHFNKWFK
     YPYVFLNDDP FTDHFKDQIQ AATNATVEFG TVDEIMWEFP AKVRNSLQFK ASLEDQNDRG
     IMYGNMESYH KMCRFYSGIF YKHPLVSKYE WYWRIEPDVD FFCDISYDPF FEMAKHNKKY
     GFTVLITELY WTVPNLFRTT KSFIKKTAGL KENLGTLWKL FTFNYNILDT DDEEISRWVN
     FPWDAKPKLT EKLMVDFLLE NHGQVNNEED LEGIQYLVER ARSKVPMLED SLEGEDYNLC
     HFWSNFEIAR VDLFDNEIYN AYFKFLEESG GFWTERWGDA PIHSIGLGMT LDLEDVHYFR
     DIGYRHSSLQ HCPKNALQSQ ENLNTFDEGY NFGCGCRCVC PKKGEDIEDH STPCMDIFFE
     LLHGREYEKE FPGCYKPSIK DKDVIEEIRR ENFRVIE
 
 
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