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KTR6_YEAST
ID   KTR6_YEAST              Reviewed;         446 AA.
AC   P54070; D6W3W1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Mannosyltransferase KTR6;
DE            EC=2.4.1.-;
DE   AltName: Full=Mannosylphosphate transferase MNN6;
GN   Name=KTR6; Synonyms=MNN6; OrderedLocusNames=YPL053C; ORFNames=LPE19C;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=S288c / GRF88;
RX   PubMed=9218445; DOI=10.1074/jbc.272.29.18117;
RA   Wang X.-H., Nakayama K., Shimma Y., Tanaka A., Jigami Y.;
RT   "MNN6, a member of the KRE2/MNT1 family, is the gene for mannosylphosphate
RT   transfer in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 272:18117-18124(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
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   [4]
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   [5]
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: Glycosyltransferase that transfers an alpha-D-mannosyl
CC       residue from GDP-mannose into lipid-linked oligosaccharide, forming an
CC       alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for addition of
CC       mannosylphosphate in yeast mannan. Recognizes any oligosaccharides with
CC       at least one alpha-1,2-linked mannobiose unit.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 4380 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; U43922; AAC49761.1; -; Genomic_DNA.
DR   EMBL; U39205; AAB68312.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11377.1; -; Genomic_DNA.
DR   PIR; S61089; S61089.
DR   RefSeq; NP_015272.1; NM_001183867.1.
DR   AlphaFoldDB; P54070; -.
DR   SMR; P54070; -.
DR   BioGRID; 36127; 73.
DR   DIP; DIP-5329N; -.
DR   IntAct; P54070; 4.
DR   STRING; 4932.YPL053C; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   MaxQB; P54070; -.
DR   PaxDb; P54070; -.
DR   PRIDE; P54070; -.
DR   EnsemblFungi; YPL053C_mRNA; YPL053C; YPL053C.
DR   GeneID; 856054; -.
DR   KEGG; sce:YPL053C; -.
DR   SGD; S000005974; KTR6.
DR   VEuPathDB; FungiDB:YPL053C; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   GeneTree; ENSGT00940000176287; -.
DR   HOGENOM; CLU_024327_1_0_1; -.
DR   InParanoid; P54070; -.
DR   OMA; NCNCDQG; -.
DR   BioCyc; MetaCyc:YPL053C-MON; -.
DR   BioCyc; YEAST:YPL053C-MON; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:P54070; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P54070; protein.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000031; F:mannosylphosphate transferase activity; IMP: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; IMP:SGD.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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; 1.
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..446
FT                   /note="Mannosyltransferase KTR6"
FT                   /id="PRO_0000208247"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..446
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          30..114
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          115..446
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  52128 MW;  72F06428B8722803 CRC64;
     MHVLLSKKIA RFLLISFVFV LALMVTINHP KTKQMSEQYV TPYLPKSLQP IAKISAEEQR
     RIQSEQEEAE LKQSLEGEAI RNATVNAIKE KIKSYGGNET TLGFMVPSYI NHRGSPPKAC
     FVSLITERDS MTQILQSIDE VQVKFNKNFA YPWVFISQGE LDGMKQEMIR QAITDSMNGD
     PELINIKFAE IPADEWVYPE WIDENKAAES LISLANVPDG DSRAVRYQAR YFAGFFWRHP
     VLDEFDWYWR VDPGIKLYCD IDHDLFRWMQ DEGKVFGFTL SMSEAKEANE KIWDVTKKFA
     KDFPKFISEN NFKSFITKKD SEDFNNCEFT SNFEIGNLNF YRSPAYRKFF NYIDEEGGIF
     YWKWSDSIIH TIGLSMLLPK DKIHFFENIG FHYDKYNNCP LNDDIWNQYN CNCDQGNDFT
     FRSGSCGGHY FDIMKKDKPE GWDRLP
 
 
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