ID   OMH2_SCHPO              Reviewed;         372 AA.
AC   O42944;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=O-glycoside alpha-1,2-mannosyltransferase homolog 2;
DE            EC=2.4.1.-;
GN   Name=omh2; ORFNames=SPBC16H5.09c;
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}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA17907.1; -; Genomic_DNA.
DR   PIR; T39616; T39616.
DR   RefSeq; NP_595938.1; NM_001021846.2.
DR   AlphaFoldDB; O42944; -.
DR   SMR; O42944; -.
DR   BioGRID; 276450; 3.
DR   STRING; 4896.SPBC16H5.09c.1; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   SwissPalm; O42944; -.
DR   MaxQB; O42944; -.
DR   PaxDb; O42944; -.
DR   PRIDE; O42944; -.
DR   EnsemblFungi; SPBC16H5.09c.1; SPBC16H5.09c.1:pep; SPBC16H5.09c.
DR   GeneID; 2539904; -.
DR   KEGG; spo:SPBC16H5.09c; -.
DR   PomBase; SPBC16H5.09c; omh2.
DR   VEuPathDB; FungiDB:SPBC16H5.09c; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_4_1_1; -.
DR   InParanoid; O42944; -.
DR   OMA; PFTHCPH; -.
DR   PhylomeDB; O42944; -.
DR   PRO; PR:O42944; -.
DR   Proteomes; UP000002485; Chromosome II.
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; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..372
FT                   /note="O-glycoside alpha-1,2-mannosyltransferase homolog 2"
FT                   /id="PRO_0000316584"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..372
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        271
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   372 AA;  44346 MW;  9AA5568F7C833AE3 CRC64;
     MRISRLLIRV LLGFVILFIT YILFPSIPKA LVNTLNVYKL EERLNYYNDR LLDGNLKSKE
     LENATFVTLA RNADLYDLIE TINIYENRFN SKHNYPWVFL NDEPFTRTFE VVMSRLTSGP
     TYFGVVNSSE WDIPKWIDMD IAHSNWNRLS REGVLYGGMK SYRQMCRYFS GFFWRHPLLD
     PYKYYWRVEP STKLLCEVNK DPFRQLRLLN KTYGFVITLF EIGQTVPSLW NSTLEFIEKY
     PETLAKNNLW EWISDDNGKK FSHCHFWSNF EIADLDFFRS DSYRKYFDFL DKKGGFFYER
     WGDAPVHSIA LSLFLDRNKL HYFDEIGYSH APLLHCPRKG RCFCKPEEID LSSNSSCIAR
     FINLTNEDYD EL