PMT2_SCHPO
ID PMT2_SCHPO Reviewed; 739 AA.
AC Q9C100;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
DE EC=2.4.1.109;
GN Name=ogm2; Synonyms=oma2; ORFNames=SPAPB1E7.09;
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).
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000269|PubMed:15809069}.
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}.
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; CU329670; CAC36926.1; -; Genomic_DNA.
DR RefSeq; NP_594135.1; NM_001019559.2.
DR AlphaFoldDB; Q9C100; -.
DR SMR; Q9C100; -.
DR BioGRID; 280071; 4.
DR STRING; 4896.SPAPB1E7.09.1; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR iPTMnet; Q9C100; -.
DR MaxQB; Q9C100; -.
DR PaxDb; Q9C100; -.
DR PRIDE; Q9C100; -.
DR EnsemblFungi; SPAPB1E7.09.1; SPAPB1E7.09.1:pep; SPAPB1E7.09.
DR GeneID; 2543657; -.
DR KEGG; spo:SPAPB1E7.09; -.
DR PomBase; SPAPB1E7.09; ogm2.
DR VEuPathDB; FungiDB:SPAPB1E7.09; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; Q9C100; -.
DR OMA; DANDVWR; -.
DR PhylomeDB; Q9C100; -.
DR BRENDA; 2.4.1.109; 5613.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9C100; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0012505; C:endomembrane system; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
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:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
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; PTHR10050; 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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Nucleus; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..739
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 2"
FT /id="PRO_0000237686"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 332..386
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 399..455
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 463..521
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 739 AA; 85037 MW; F0F0BBD35D889252 CRC64;
MSYEQLHAQS GQLRQRFPSK HSEIEDEVAN EKEELKDATK SALGEVKTNK KYYILGYFLV
PLLLTVIAGF VRVWKIADSN VVIWDEAHFG KFASYYLKHE FYFDVHPPLG KMLNAVAGKL
VGYDGSFDFS SGATYPEDLN YKFMRLWNAA FGTLCIPLVY FTALNFNYSF LAATLCTLMV
ALDNHLATIS RFILLDSMLL FFIISTFFCL SRYHVYHKAP FTFYWFKWLF LTGVCIGCVC
SVKLVGLFIT AVVGLYTVDE LWCLLNDKRV TWKAYAGHWI ARVCLLIFLP ILIYAFTFWI
QFAVLYRSGP GDAQMPSLFQ ARLEGSPLTK NPIDLMYGSK FTLKSRNPTG ALLHSHVQTY
PEGSEQQQVT GYHHKDGNNE WMFVPTHGVA YNYEENDPMN PILNGSVVRL IHPFTNRNLH
THKIPAPLNK RMYEVSGYGL GDVGDEKDYW IVNILYDTAH RDAYNVRSLS TVFQLYNPVV
GCYLSSSSSS LPSWGFGQIE MYCDPDPDPS NTDTQWNVEE HINPRLPEGS INDYPSSFWS
DFLHLNRAML RANNGLIPDE DKLDALRSEA YQWPFLLATL RMCGWGDNQI KYLLVGNPVA
YWFATSSLIV FALFVVGAVL AWRRRVLRWS QEACDTFHYA GIYPFLGWFF NYLPYYIMGR
VLYVHHYEPS YALSTFTAAF VVDWFTKKMP KIVRVVVFIS LYAIIAGVFI YFKDVTFGMH
GPASDFHRLR WLNSWNVHD
