PMT1_SCHPO
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 03-AUG-2022, entry version 153.
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; 4896.SPAC22A12.07c.1; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR iPTMnet; O13898; -.
DR MaxQB; O13898; -.
DR PaxDb; O13898; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; IPR027004; PMT1/PTM5.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR PANTHER; PTHR10050:SF50; PTHR10050:SF50; 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; SSF82109; 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
