ID   OMH3_SCHPO              Reviewed;         378 AA.
AC   O74546;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=O-glycoside alpha-1,2-mannosyltransferase homolog 3;
DE            EC=2.4.1.-;
GN   Name=omh3; ORFNames=SPCC777.07;
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   IDENTIFICATION.
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: Probable mannosyltransferase involved in O-glycosylation of
CC       cell wall and secreted proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA20711.1; -; Genomic_DNA.
DR   PIR; T11713; T11713.
DR   RefSeq; NP_588253.1; NM_001023243.2.
DR   AlphaFoldDB; O74546; -.
DR   SMR; O74546; -.
DR   BioGRID; 276149; 4.
DR   STRING; 4896.SPCC777.07.1; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   MaxQB; O74546; -.
DR   PaxDb; O74546; -.
DR   EnsemblFungi; SPCC777.07.1; SPCC777.07.1:pep; SPCC777.07.
DR   PomBase; SPCC777.07; omh3.
DR   VEuPathDB; FungiDB:SPCC777.07; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_4_2_1; -.
DR   InParanoid; O74546; -.
DR   OMA; CECYPEN; -.
DR   PhylomeDB; O74546; -.
DR   PRO; PR:O74546; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; ISS:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; ISO:PomBase.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; ISO: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   GO; GO:0035269; P:protein O-linked mannosylation; ISO:PomBase.
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; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..378
FT                   /note="O-glycoside alpha-1,2-mannosyltransferase homolog 3"
FT                   /id="PRO_0000316585"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..378
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        276
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   378 AA;  44478 MW;  D852A136B925F70C CRC64;
     MGIPKSSIYF CILLFCIISF YLQSSKDGPK ELKVKYVFLK KATAKQRGES SLTDSDYFPK
     QPNMNATLFM LCRNRDIKDA LVSIQSVEDR FNHRYHYPWT FMNDAPFTKE FITATSKMVS
     GDATYVQLNN EEWGIPINID LNRMLKSIRD MTDDKVIYGF SLSYRIMCRF NSGFFYRNKA
     LSHYDYYWRV EPGVEYSCDI PYDPFRKLSD ENKAYGFVIS MTDYYETLPS LWNVTRDFIH
     QNPQYLAQNN SLDFIVNDHQ GLSGDYNLCH FWSNFEIANL NFFRSPAYTD YFAHLDKNYG
     FFYERWGDAP VHSLAASLFL NKSQIHYFED FGYYHLPWYH CPTDVQSHAT ARCLCDPTGT
     IDYLPFSCAI KWLENINS