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KTR5_YEAST
ID   KTR5_YEAST              Reviewed;         522 AA.
AC   P53966; D6W1F0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Probable mannosyltransferase KTR5;
DE            EC=2.4.1.-;
GN   Name=KTR5; OrderedLocusNames=YNL029C; ORFNames=N2755;
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=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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 450 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; Z71305; CAA95891.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10516.1; -; Genomic_DNA.
DR   PIR; S62941; S62941.
DR   RefSeq; NP_014369.3; NM_001182868.3.
DR   AlphaFoldDB; P53966; -.
DR   SMR; P53966; -.
DR   BioGRID; 35798; 40.
DR   DIP; DIP-6646N; -.
DR   IntAct; P53966; 1.
DR   STRING; 4932.YNL029C; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   iPTMnet; P53966; -.
DR   MaxQB; P53966; -.
DR   PaxDb; P53966; -.
DR   PRIDE; P53966; -.
DR   TopDownProteomics; P53966; -.
DR   EnsemblFungi; YNL029C_mRNA; YNL029C; YNL029C.
DR   GeneID; 855703; -.
DR   KEGG; sce:YNL029C; -.
DR   SGD; S000004974; KTR5.
DR   VEuPathDB; FungiDB:YNL029C; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   GeneTree; ENSGT00940000176287; -.
DR   HOGENOM; CLU_024327_2_0_1; -.
DR   InParanoid; P53966; -.
DR   OMA; AFVITMY; -.
DR   BioCyc; YEAST:G3O-33066-MON; -.
DR   ChiTaRS; KTR5; yeast.
DR   PRO; PR:P53966; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53966; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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:0097502; P:mannosylation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-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..522
FT                   /note="Probable mannosyltransferase KTR5"
FT                   /id="PRO_0000208246"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..522
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          38..82
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          83..522
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   522 AA;  61728 MW;  3F9D75D3F09D4110 CRC64;
     MLLIRRTINA FLGCIHCNLT ATCILIAFVI TMYVVLVSEP ASVDGTMGNF LPFSKMDLAT
     KRDRPFYSNC VNTQDYLLNP SYIKQNASFV MLTRNGELED VIKTINSIEE HFNQWFHYPY
     VFLNDQPFEE DFKAKVRDVT VGALVEFGTI DEISWNFPSD VKDTFEFYNA IEDQGDRSIL
     YGNLESYHKM CRFYSGLFYK HPLVQKYEWY WRLEPDVEFF CDITYDPFLE MLRTNKKYGF
     TIIIPELYWT VPNLFRHTKS FISQKGVTLG SLWKLFTKDY DIFESDDPEL RDWINYDFQA
     KAKISEKIAI EQLLKKGDDF QQINDDKEGI MNLIHKARSR KHIVEDKFFN EEYNLCHFWS
     NFEIARLSVF DNDIYNSFFQ YLEKSGGFWK ERWGDAPVHS IGLSLTLDLD DVHYFRDIGY
     RHSTIQHCPH NAMGNEEFSY LASDSKFKRK NAAYDEGREF GCGCRCRCPK KKREIEDSMG
     FCVNIWVNLL NQQRGHERHV EALNGNEMEE HIREDYLRQF GN
 
 
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