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KTR2_YEAST
ID   KTR2_YEAST              Reviewed;         425 AA.
AC   P33550; D6VXC2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Probable mannosyltransferase KTR2;
DE            EC=2.4.1.-;
GN   Name=KTR2; OrderedLocusNames=YKR061W;
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.
RX   PubMed=8256512; DOI=10.1002/yea.320091004;
RA   Lussier M., Camirand A., Sdicu A.-M., Bussey H.;
RT   "KTR2: a new member of the KRE2 mannosyltransferase gene family.";
RL   Yeast 9:1057-1063(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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).
CC   -!- FUNCTION: Involved in N-linked glycosylation. 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   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
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DR   EMBL; L17083; AAA16119.1; -; Unassigned_DNA.
DR   EMBL; Z28286; CAA82140.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09212.1; -; Genomic_DNA.
DR   PIR; S38193; S38193.
DR   RefSeq; NP_012987.3; NM_001179851.3.
DR   AlphaFoldDB; P33550; -.
DR   SMR; P33550; -.
DR   BioGRID; 34192; 106.
DR   IntAct; P33550; 1.
DR   MINT; P33550; -.
DR   STRING; 4932.YKR061W; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   iPTMnet; P33550; -.
DR   MaxQB; P33550; -.
DR   PaxDb; P33550; -.
DR   PRIDE; P33550; -.
DR   EnsemblFungi; YKR061W_mRNA; YKR061W; YKR061W.
DR   GeneID; 853935; -.
DR   KEGG; sce:YKR061W; -.
DR   SGD; S000001769; KTR2.
DR   VEuPathDB; FungiDB:YKR061W; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   GeneTree; ENSGT00940000176287; -.
DR   HOGENOM; CLU_024327_4_2_1; -.
DR   InParanoid; P33550; -.
DR   OMA; CPSAYYM; -.
DR   BioCyc; YEAST:G3O-32029-MON; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:P33550; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P33550; protein.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IDA:SGD.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; 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   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..425
FT                   /note="Probable mannosyltransferase KTR2"
FT                   /id="PRO_0000208243"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        34..425
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          34..89
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          90..425
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   425 AA;  50651 MW;  CF48E73E5BB0F832 CRC64;
     MQICKVFLTQ VKKLLFVSLL FCLIAQTCWL ALVPYQRQLS LDSYFFRRSR EVSSRYDFTR
     RRHMNQTLKL SSNTYNDEPL NKTKGIKNQR ENATLLMLVR NWELSGALRS MRSLEDRFNK
     NYQYDWTFLN DVPFDQEFIE ATTAMASGRT QYALIPAEDW NRPSWINETL FEEALQLMEE
     KNILYGGSKS YRNMCRFNSG FFFRQKILDP YDFYFRVEPD VEYFCDFPYD PFKVMRQNNK
     KYGFVITMYE YEDTIPSLWE AVEEYLEETE SADIDMESNA FGFVSNFDFI GKSFGVIDSN
     SGYNLCHFWT NFEIGDLNFF RSEKYIRFFE YLDSKGGFYY ERWGDAPVHS IAASLLLKKD
     EIIHFDELGY KHMPFGTCPS AYYLRLQQRC LCDSNHPDNI DLNVISCLRR WWKDGSGKYF
     LKHDS
 
 
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