ID   OMH1_SCHPO              Reviewed;         390 AA.
AC   O60160;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=O-glycoside alpha-1,2-mannosyltransferase omh1;
DE            EC=2.4.1.-;
GN   Name=omh1; ORFNames=SPBC19C7.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19054127; DOI=10.1111/j.1567-1364.2008.00458.x;
RA   Ikeda Y., Ohashi T., Tanaka N., Takegawa K.;
RT   "Identification and characterization of a gene required for alpha1,2-
RT   mannose extension in the O-linked glycan synthesis pathway in
RT   Schizosaccharomyces pombe.";
RL   FEMS Yeast Res. 9:115-125(2009).
CC   -!- FUNCTION: Mannosyltransferase involved in O-glycosylation of cell wall
CC       and secreted proteins. Plays a major role in extending alpha-1,2-linked
CC       mannose in the O-glycan pathway. {ECO:0000269|PubMed:19054127}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16823372}. Golgi apparatus
CC       {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19054127}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA19580.1; -; Genomic_DNA.
DR   PIR; T39818; T39818.
DR   RefSeq; NP_596168.1; NM_001022088.2.
DR   AlphaFoldDB; O60160; -.
DR   SMR; O60160; -.
DR   BioGRID; 277229; 21.
DR   STRING; 4896.SPBC19C7.12c.1; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   MaxQB; O60160; -.
DR   PaxDb; O60160; -.
DR   PRIDE; O60160; -.
DR   EnsemblFungi; SPBC19C7.12c.1; SPBC19C7.12c.1:pep; SPBC19C7.12c.
DR   GeneID; 2540706; -.
DR   KEGG; spo:SPBC19C7.12c; -.
DR   PomBase; SPBC19C7.12c; omh1.
DR   VEuPathDB; FungiDB:SPBC19C7.12c; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_4_1_1; -.
DR   InParanoid; O60160; -.
DR   OMA; FMQMNNK; -.
DR   PhylomeDB; O60160; -.
DR   PRO; PR:O60160; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IDA:PomBase.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:PomBase.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; ISO:PomBase.
DR   GO; GO:0044845; P:chain elongation of O-linked mannose residue; IMP:PomBase.
DR   GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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   Endoplasmic reticulum; Glycosyltransferase; Golgi apparatus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..390
FT                   /note="O-glycoside alpha-1,2-mannosyltransferase omh1"
FT                   /id="PRO_0000316587"
FT   ACT_SITE        279
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   390 AA;  46514 MW;  0A9E5C7959275E1A CRC64;
     MVRLPRKFKR VLLLVVLLTL VVFVRFKKQY IPTISVFEGS LIDNRDTLSY FNISNLEPSE
     RSEWLPNKRV NAAFVTLARN EDLNDLLKSI RKLEKTFNHK YHYGWVFLNN EEFSDEFKEH
     VIEAVSGKCE FGLVPQEQWS IPEYIDQDKM HENWKKLQEL GILYADKESY RHMCRFESGF
     FYRHPLVQKY EYYWRVEPSV DFFCDLDFDP FAYMKENNKA YAFTITVTEY SETIPSLWPS
     TKEFIKMHPN ALHPNNALNF ISNDDGETYN GCHFWTNFEI AKVDFWESEV YSKYFDYLDK
     SGNFFYERWG DAPVHSIAVS LFADRDNIHF FNEIGYWHPG SGHCPLDDAT RAKCDCDPYE
     SIDYNGWSCL DKFYTAFEMP FPENWSFYSH