OCH1_YEAST
ID OCH1_YEAST Reviewed; 480 AA.
AC P31755; D6VUA1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Initiation-specific alpha-1,6-mannosyltransferase {ECO:0000305};
DE EC=2.4.1.232 {ECO:0000269|PubMed:1628616, ECO:0000269|PubMed:17042779};
DE AltName: Full=Outer chain elongation protein 1 {ECO:0000303|PubMed:1628616};
GN Name=OCH1 {ECO:0000303|PubMed:1523886};
GN Synonyms=NGD29 {ECO:0000303|PubMed:7649302};
GN OrderedLocusNames=YGL038C {ECO:0000312|SGD:S000003006};
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], DISRUPTION PHENOTYPE, GLYCOSYLATION,
RP SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=EHF-2C;
RX PubMed=1628616; DOI=10.1002/j.1460-2075.1992.tb05316.x;
RA Nakayama K., Nagasu T., Shimma Y., Kuromitsu J.-R., Jigami Y.;
RT "OCH1 encodes a novel membrane bound mannosyltransferase: outer chain
RT elongation of asparagine-linked oligosaccharides.";
RL EMBO J. 11:2511-2519(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1523886; DOI=10.1002/yea.320080705;
RA Nagasu T., Shimma Y., Nakanishi Y., Kuromitsu J., Iwama K., Nakayama K.,
RA Suzuki K., Jigami Y.;
RT "Isolation of new temperature-sensitive mutants of Saccharomyces cerevisiae
RT deficient in mannose outer chain elongation.";
RL Yeast 8:535-547(1992).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8253757; DOI=10.1016/s0021-9258(19)74320-8;
RA Nakanishi-Shindo Y., Nakayama K., Tanaka A., Toda Y., Jigami Y.;
RT "Structure of the N-linked oligosaccharides that show the complete loss of
RT alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3
RT mutants of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:26338-26345(1993).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7649302; DOI=10.1016/0014-5793(95)00789-c;
RA Lehle L., Eiden A., Lehnert K., Haselbeck A., Kopetzki E.;
RT "Glycoprotein biosynthesis in Saccharomyces cerevisiae: ngd29, an N-
RT glycosylation mutant allelic to och1 having a defect in the initiation of
RT outer chain formation.";
RL FEBS Lett. 370:41-45(1995).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8601597; DOI=10.1083/jcb.132.6.985;
RA Harris S.L., Waters M.G.;
RT "Localization of a yeast early Golgi mannosyltransferase, Och1p, involves
RT retrograde transport.";
RL J. Cell Biol. 132:985-998(1996).
RN [9]
RP INDUCTION.
RX PubMed=11036637; DOI=10.1016/s0076-6879(00)26049-7;
RA Horecka J., Sprague G.F. Jr.;
RT "Use of imidazoleglycerolphosphate dehydratase (His3) as a biological
RT reporter in yeast.";
RL Methods Enzymol. 326:107-119(2000).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=10880465; DOI=10.1093/genetics/155.3.1005;
RA Cullen P.J., Schultz J., Horecka J., Stevenson B.J., Jigami Y.,
RA Sprague G.F. Jr.;
RT "Defects in protein glycosylation cause SHO1-dependent activation of a
RT STE12 signaling pathway in yeast.";
RL Genetics 155:1005-1018(2000).
RN [11]
RP INDUCTION.
RX PubMed=11854400; DOI=10.1091/mbc.01-09-0434;
RA Li S., Dean S., Li Z., Horecka J., Deschenes R.J., Fassler J.S.;
RT "The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the
RT transcription factor, Skn7p.";
RL Mol. Biol. Cell 13:412-424(2002).
RN [12]
RP INDUCTION.
RX PubMed=11754484; DOI=10.1002/yea.801;
RA Cui Z., Horecka J., Jigami Y.;
RT "Cdc4 is involved in the transcriptional control of OCH1, a gene encoding
RT alpha-1,6-mannosyltransferase in Saccharomyces cerevisiae.";
RL Yeast 19:69-77(2002).
RN [13]
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).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=15229219; DOI=10.1074/jbc.m405500200;
RA Bruinsma P., Spelbrink R.G., Nothwehr S.F.;
RT "Retrograde transport of the mannosyltransferase Och1p to the early Golgi
RT requires a component of the COG transport complex.";
RL J. Biol. Chem. 279:39814-39823(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=14676282; DOI=10.1242/jcs.00858;
RA Karhinen L., Makarow M.;
RT "Activity of recycling Golgi mannosyltransferases in the yeast endoplasmic
RT reticulum.";
RL J. Cell Sci. 117:351-358(2004).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP DOMAIN, AND MUTAGENESIS OF ASP-187.
RX PubMed=17042779; DOI=10.1111/j.1742-4658.2006.05505.x;
RA Kitajima T., Chiba Y., Jigami Y.;
RT "Saccharomyces cerevisiae alpha1,6-mannosyltransferase has a catalytic
RT potential to transfer a second mannose molecule.";
RL FEBS J. 273:5074-5085(2006).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=21622726; DOI=10.1093/glycob/cwr073;
RA Hirayama H., Suzuki T.;
RT "Metabolism of free oligosaccharides is facilitated in the och1Delta mutant
RT of Saccharomyces cerevisiae.";
RL Glycobiology 21:1341-1348(2011).
RN [18]
RP FUNCTION.
RX PubMed=21979948; DOI=10.1074/jbc.m111.251371;
RA Chantret I., Kodali V.P., Lahmouich C., Harvey D.J., Moore S.E.;
RT "Endoplasmic reticulum-associated degradation (ERAD) and free
RT oligosaccharide generation in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 286:41786-41800(2011).
CC -!- FUNCTION: Mannosyltransferase involved in outer chain elongation of
CC asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). Adds
CC the first alpha-1,6-mannose to the Man(8)GlcNAc(2) and Man(9)GlcNAc(2),
CC but not Man(5)GlcNAc(2), endoplasmic reticulum intermediates.
CC Represents the first enzymatic event required for synthesis of outer
CC chain mannose linkages on yeast secretory proteins. Has also the
CC potential to transfer a second alpha-1,6-mannose to the Man(8)GlcNAc(2)
CC core oligosaccharide. {ECO:0000269|PubMed:1523886,
CC ECO:0000269|PubMed:1628616, ECO:0000269|PubMed:17042779,
CC ECO:0000269|PubMed:21979948, ECO:0000269|PubMed:7649302,
CC ECO:0000269|PubMed:8253757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-mannosyl residue from GDP-mannose into
CC lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-
CC mannose linkage.; EC=2.4.1.232; Evidence={ECO:0000269|PubMed:1628616,
CC ECO:0000269|PubMed:17042779};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17042779};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17042779};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14676282, ECO:0000269|PubMed:1628616}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:8601597,
CC ECO:0000303|PubMed:1628616}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:14676282, ECO:0000269|PubMed:15229219,
CC ECO:0000269|PubMed:1628616}; Single-pass type II membrane protein
CC {ECO:0000303|PubMed:1628616}. Note=Is recycled between the trans-Golgi
CC network and a late compartment of the endoplasmic reticulum.
CC {ECO:0000269|PubMed:14676282}.
CC -!- INDUCTION: Expression is regulated by SKN7, SLN1, and CDC4.
CC {ECO:0000269|PubMed:11036637, ECO:0000269|PubMed:11754484,
CC ECO:0000269|PubMed:11854400}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000303|PubMed:17042779}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1628616}.
CC -!- DISRUPTION PHENOTYPE: Stops growing at the early stage of bud formation
CC and rapidly loses viability at the non-permissive temperature. Exhibits
CC a defect in the initiation of the mannose outer chain. Leads to
CC accumulation of free forms of oligosaccharides (fOSs).
CC {ECO:0000269|PubMed:10880465, ECO:0000269|PubMed:1523886,
CC ECO:0000269|PubMed:1628616, ECO:0000269|PubMed:21622726,
CC ECO:0000269|PubMed:7649302, ECO:0000269|PubMed:8253757}.
CC -!- MISCELLANEOUS: Present with 9490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
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DR EMBL; D11095; BAA01869.1; -; Genomic_DNA.
DR EMBL; Z72560; CAA96740.1; -; Genomic_DNA.
DR EMBL; AY692749; AAT92768.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08062.1; -; Genomic_DNA.
DR PIR; S22701; S22701.
DR RefSeq; NP_011477.1; NM_001180903.1.
DR AlphaFoldDB; P31755; -.
DR BioGRID; 33209; 40.
DR DIP; DIP-8030N; -.
DR STRING; 4932.YGL038C; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR MaxQB; P31755; -.
DR PaxDb; P31755; -.
DR PRIDE; P31755; -.
DR EnsemblFungi; YGL038C_mRNA; YGL038C; YGL038C.
DR GeneID; 852845; -.
DR KEGG; sce:YGL038C; -.
DR SGD; S000003006; OCH1.
DR VEuPathDB; FungiDB:YGL038C; -.
DR eggNOG; ENOG502QW2I; Eukaryota.
DR GeneTree; ENSGT00940000176653; -.
DR HOGENOM; CLU_022381_5_2_1; -.
DR InParanoid; P31755; -.
DR OMA; AFVKHNF; -.
DR BioCyc; MetaCyc:G3O-30552-MON; -.
DR BioCyc; YEAST:G3O-30552-MON; -.
DR PRO; PR:P31755; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P31755; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:SGD.
DR GO; GO:0000136; C:mannan polymerase complex; IBA:GO_Central.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039367; Och1-like.
DR PANTHER; PTHR31834; PTHR31834; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..480
FT /note="Initiation-specific alpha-1,6-mannosyltransferase"
FT /id="PRO_0000080563"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:1628616"
FT TRANSMEM 16..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:1628616"
FT TOPO_DOM 31..480
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8601597,
FT ECO:0000303|PubMed:1628616"
FT MOTIF 187..189
FT /note="DXD motif"
FT /evidence="ECO:0000303|PubMed:17042779"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 187
FT /note="D->A: Loss of mannosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17042779"
SQ SEQUENCE 480 AA; 55156 MW; 6B0ACA09A9B17E72 CRC64;
MSRKLSHLIA TRKSKTIVVT VLLIYSLLTF HLSNKRLLSQ FYPSKDDFKQ TLLPTTSHSQ
DINLKKQITV NKKKNQLHNL RDQLSFAFPY DSQAPIPQRV WQTWKVGADD KNFPSSFRTY
QKTWSGSYSP DYQYSLISDD SIIPFLENLY APVPIVIQAF KLMPGNILKA DFLRYLLLFA
RGGIYSDMDT MLLKPIDSWP SQNKSWLNNI IDLNKPIPYK NSKPSLLSSD EISHQPGLVI
GIEADPDRDD WSEWYARRIQ FCQWTIQAKP GHPILRELIL NITATTLASV QNPGVPVSEM
IDPRFEEDYN VNYRHKRRHD ETYKHSELKN NKNVDGSDIM NWTGPGIFSD IIFEYMNNVL
RYNSDILLIN PNLNKNDEEG SESATTPAKD VDNDTLSKST RKFYKKISES LQSSNSMPWE
FFSFLKEPVI VDDVMVLPIT SFSPDVGQMG AQSSDDKMAF VKHMFSGSWK EDADKNAGHK
