HOC1_YEAST
ID HOC1_YEAST Reviewed; 396 AA.
AC P47124; D6VWP5; E9P8X6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Putative glycosyltransferase HOC1;
DE EC=2.4.-.-;
DE AltName: Full=M-Pol II subunit Hoc1p;
DE AltName: Full=Mannan polymerase II complex HOC1 subunit;
GN Name=HOC1; OrderedLocusNames=YJR075W; ORFNames=J1830;
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 SUBCELLULAR LOCATION.
RX PubMed=9055074; DOI=10.1093/genetics/145.3.637;
RA Neiman A.M., Mhaiskar V., Manus V., Galibert F., Dean N.;
RT "Saccharomyces cerevisiae HOC1, a suppressor of pkc1, encodes a putative
RT glycosyltransferase.";
RL Genetics 145:637-645(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-11, AND SUBUNIT.
RX PubMed=9434768; DOI=10.1006/bbrc.1997.7888;
RA Hashimoto H., Yoda K.;
RT "Novel membrane protein complexes for protein glycosylation in the yeast
RT Golgi apparatus.";
RL Biochem. Biophys. Res. Commun. 241:682-686(1997).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, AND ACTIVITY OF
RP M-POL II COMPLEX.
RX PubMed=9430634; DOI=10.1093/emboj/17.2.423;
RA Jungmann J., Munro S.;
RT "Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with
RT alpha-1,6-mannosyltransferase activity.";
RL EMBO J. 17:423-434(1998).
RN [8]
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: The M-Pol II complex possesses alpha-1,6-mannosyltransferase
CC activity and is probably involved in the elongation of the mannan
CC backbone of N-linked glycans on cell wall and periplasmic proteins.
CC -!- SUBUNIT: Component of the M-Pol II complex composed of ANP1, MNN9,
CC MNN10, MNN11 and HOC1. {ECO:0000269|PubMed:9430634,
CC ECO:0000269|PubMed:9434768}.
CC -!- INTERACTION:
CC P47124; P32629: ANP1; NbExp=2; IntAct=EBI-8430, EBI-2595;
CC P47124; P50108: MNN10; NbExp=3; IntAct=EBI-8430, EBI-11043;
CC P47124; P46985: MNN11; NbExp=2; IntAct=EBI-8430, EBI-11052;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:9055074, ECO:0000269|PubMed:9430634}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:9055074,
CC ECO:0000269|PubMed:9430634}.
CC -!- MISCELLANEOUS: Present with 7160 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; U62942; AAB49938.1; -; Genomic_DNA.
DR EMBL; Z49575; CAA89603.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39300.1; -; Genomic_DNA.
DR EMBL; AY692827; AAT92846.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08861.1; -; Genomic_DNA.
DR PIR; S57094; S57094.
DR RefSeq; NP_012609.3; NM_001181733.3.
DR AlphaFoldDB; P47124; -.
DR SMR; P47124; -.
DR BioGRID; 33831; 548.
DR ComplexPortal; CPX-1839; alpha-1,6-mannosyltransferase complex, M-Pol II variant.
DR DIP; DIP-918N; -.
DR IntAct; P47124; 9.
DR MINT; P47124; -.
DR STRING; 4932.YJR075W; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR iPTMnet; P47124; -.
DR MaxQB; P47124; -.
DR PaxDb; P47124; -.
DR PRIDE; P47124; -.
DR EnsemblFungi; YJR075W_mRNA; YJR075W; YJR075W.
DR GeneID; 853538; -.
DR KEGG; sce:YJR075W; -.
DR SGD; S000003836; HOC1.
DR VEuPathDB; FungiDB:YJR075W; -.
DR eggNOG; ENOG502QW2I; Eukaryota.
DR GeneTree; ENSGT00940000176653; -.
DR HOGENOM; CLU_022381_5_0_1; -.
DR InParanoid; P47124; -.
DR OMA; WIPENVS; -.
DR BioCyc; MetaCyc:YJR075W-MON; -.
DR BioCyc; YEAST:YJR075W-MON; -.
DR PRO; PR:P47124; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47124; protein.
DR GO; GO:0000136; C:mannan polymerase complex; IDA:UniProtKB.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; TAS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006080; P:substituted mannan metabolic process; TAS: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 Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9434768"
FT CHAIN 2..396
FT /note="Putative glycosyltransferase HOC1"
FT /id="PRO_0000080564"
FT TOPO_DOM 2..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..396
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 393
FT /note="V -> E (in Ref. 5; AAT92846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 46297 MW; 8BF77385510DE6B0 CRC64;
MAKTTKRASS FRRLMIFAII ALISLAFGVR YLFHNSNATD LQKILQNLPK EISQSINSAN
NIQSSDSDLV QHFESLAQEI RHQQEVQAKQ FDKQRKILEK KIQDLKQTPP EATLRERIAM
TFPYDSHVKF PAFIWQTWSN DEGPERVQDI KGMWESKNPG FAHEVLNHDV INALVHHYFY
SIPEILETYE ALPSIILKID FFKYLILLVH GGVYADIDTF PVQPIPNWIP EELSPSDIGL
IVGVEEDAQR ADWRTKYIRR LQFGTWIIQA KPGHPVLREI ISRIIETTLQ RKRDDQLNVN
LRNDLNIMSW TGSGLWTDTI FTYFNDFMRS GVREKVTWKL FHNLNQPKLL SDVLVFPKFS
FNCPNQIDND DPHKKFYFIT HLASQFWKNT PKVEQK