ID   PMT1_SCHPO              Reviewed;         893 AA.
AC   O13898;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
DE            EC=2.4.1.109;
GN   Name=ogm1; Synonyms=oma1; ORFNames=SPAC22A12.07c;
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15809069; DOI=10.1016/j.bbrc.2005.03.033;
RA   Tanaka N., Fujita Y., Suzuki S., Morishita M., Giga-Hama Y., Shimoda C.,
RA   Takegawa K.;
RT   "Characterization of O-mannosyltransferase family in Schizosaccharomyces
RT   pombe.";
RL   Biochem. Biophys. Res. Commun. 330:813-820(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=15948957; DOI=10.1111/j.1365-2958.2005.04692.x;
RA   Willer T., Brandl M., Sipiczki M., Strahl S.;
RT   "Protein O-mannosylation is crucial for cell wall integrity, septation and
RT   viability in fission yeast.";
RL   Mol. Microbiol. 57:156-170(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC       on proteins. Required for normal cell growth and septum formation.
CC       Shown to actively O-mannosylate wsc1. {ECO:0000269|PubMed:15809069,
CC       ECO:0000269|PubMed:15948957}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC         O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC         Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC         ChEBI:CHEBI:137321; EC=2.4.1.109;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC         3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC         H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC         ChEBI:CHEBI:137323; EC=2.4.1.109;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15809069}. Nucleus membrane
CC       {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15809069}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB16577.1; -; Genomic_DNA.
DR   PIR; T38147; T38147.
DR   RefSeq; NP_593237.1; NM_001018634.2.
DR   AlphaFoldDB; O13898; -.
DR   SMR; O13898; -.
DR   BioGRID; 277924; 5.
DR   STRING; 284812.O13898; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; O13898; 4 sites, No reported glycans.
DR   iPTMnet; O13898; -.
DR   MaxQB; O13898; -.
DR   PaxDb; 4896-SPAC22A12-07c-1; -.
DR   EnsemblFungi; SPAC22A12.07c.1; SPAC22A12.07c.1:pep; SPAC22A12.07c.
DR   GeneID; 2541418; -.
DR   KEGG; spo:SPAC22A12.07c; -.
DR   PomBase; SPAC22A12.07c; ogm1.
DR   VEuPathDB; FungiDB:SPAC22A12.07c; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   HOGENOM; CLU_008438_2_1_1; -.
DR   InParanoid; O13898; -.
DR   OMA; WAPYILE; -.
DR   PhylomeDB; O13898; -.
DR   BRENDA; 2.4.1.109; 5613.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O13898; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0012505; C:endomembrane system; IDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IMP:PomBase.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:PomBase.
DR   GO; GO:0044845; P:chain elongation of O-linked mannose residue; IMP:PomBase.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IGI:PomBase.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR027005; GlyclTrfase_39-like.
DR   InterPro; IPR003342; Glyco_trans_39/83.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR032421; PMT_4TMC.
DR   PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF02366; PMT; 1.
DR   Pfam; PF16192; PMT_4TMC; 1.
DR   SMART; SM00472; MIR; 3.
DR   SUPFAM; SSF82109; MIR domain; 1.
DR   PROSITE; PS50919; MIR; 3.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..893
FT                   /note="Dolichyl-phosphate-mannose--protein
FT                   mannosyltransferase 1"
FT                   /id="PRO_0000121499"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        573..593
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        610..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        643..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        671..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          310..364
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          374..433
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          443..499
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   REGION          785..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..802
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         451
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        665
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        720
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   893 AA;  101335 MW;  67047E4D896A3568 CRC64;
     MDKQSTFQDP KEKHRIQRDV KLSRPRKRFS FLDYVVVIFL TVVAFCVRAQ RLMNPAKVVF
     EELRYYNYAV DYVNNKLLMD VYPPLGKLLF SLVAALTGNK YELNTLDEPG QQYPFTDVAY
     SMRLFTCLLG SLLVPLMYGT VYFPTKSKTA ASLAALFVIF DNGLITMSRY IMIEIPALYF
     MSLTAFYWSV YEAQQKRPFS LRWHTSLLST GVALGLALST KLSAMFTFGW LLILAAFHLW
     NLLGDLSVPM YRIVKHLFSY IFYLIGVPIT VYLAVFAVHS HIAYKASVAD AFLPPEHRHA
     LAGNRFDDQF ADVAYGSLVT IRNAIPEHGY LHSSELLYPE GTEQQIISLV DEPNQNALWI
     IEHEHSQDNN RSNIELLKDG SVVRLRHVMT GRALHSHEHK PIVSNNDWQL EASAYGGFGF
     EGDANDLFRI QILEKKSKHA TSNGTVETLN TKFRLIHVFA NCELMSSHRR FPDWGDYQRE
     VTCCRNCVER STTWFIESNY HDGLPSDSRK ITYRKPGFLE SFVEHNKLMW LKDRKMGDGH
     VYESSALTWP LLLGPLRFFY EQHLQVFFMG NPFVWYSVIS LVAFFVIVQI FCLARWNLGY
     NDFGPSAFHY NYNIGKFVVA WLLHWAPYIL ETDRVFLYHY LPALYFGIAA LGVSWSFLGN
     AVFGNRTAYK ALSVIIMALM FLVYRLYSPF TYMTTLTKSS CRALELKGSW NFHCNTYLDN
     LSDYKFSSDA GETYFEKAAP HPFVYSEDTA KKSEGDTPLN KNLNDYYPSW DQRVEAGYKL
     AAQQKAEQEA REAAEKAASE AAERSSSEAA ASSSSESVAA ASVEAERLAM EADEFNGASE
     TVDGASVEAE RSAMEAAALN NAAESTEVVG SSPESVASEQ EENVAESAQA RVE
//