ID   PMT4_SCHPO              Reviewed;         778 AA.
AC   O42933; Q9US82;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 4;
DE            EC=2.4.1.109;
GN   Name=ogm4; Synonyms=oma4; ORFNames=SPBC16C6.09;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-105, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
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   [4]
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   [5]
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).
CC   -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC       on proteins. Required for normal cell wall and septum formation.
CC       {ECO:0000269|PubMed:15809069, 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:10759889, ECO:0000269|PubMed:15809069,
CC       ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15809069,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA16916.1; -; Genomic_DNA.
DR   EMBL; AB027986; BAA87290.1; -; Genomic_DNA.
DR   PIR; T39560; T39560.
DR   RefSeq; NP_596807.1; NM_001023828.2.
DR   AlphaFoldDB; O42933; -.
DR   SMR; O42933; -.
DR   BioGRID; 276312; 4.
DR   STRING; 284812.O42933; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; O42933; 2 sites, No reported glycans.
DR   iPTMnet; O42933; -.
DR   MaxQB; O42933; -.
DR   PaxDb; 4896-SPBC16C6-09-1; -.
DR   EnsemblFungi; SPBC16C6.09.1; SPBC16C6.09.1:pep; SPBC16C6.09.
DR   GeneID; 2539761; -.
DR   KEGG; spo:SPBC16C6.09; -.
DR   PomBase; SPBC16C6.09; ogm4.
DR   VEuPathDB; FungiDB:SPBC16C6.09; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   HOGENOM; CLU_008438_0_0_1; -.
DR   InParanoid; O42933; -.
DR   OMA; NCHLNAP; -.
DR   PhylomeDB; O42933; -.
DR   BRENDA; 2.4.1.109; 5613.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O42933; -.
DR   Proteomes; UP000002485; Chromosome II.
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:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:PomBase.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IMP: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:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF02366; PMT; 1.
DR   Pfam; PF16192; PMT_4TMC; 1.
DR   SMART; SM00472; MIR; 2.
DR   SUPFAM; SSF82109; MIR domain; 1.
DR   PROSITE; PS50919; MIR; 3.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..778
FT                   /note="Dolichyl-phosphate-mannose--protein
FT                   mannosyltransferase 4"
FT                   /id="PRO_0000121500"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        644..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        669..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        726..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          336..396
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          408..467
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          474..529
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   778 AA;  90091 MW;  7A0A79377D2AA8A2 CRC64;
     MASKSEKAVK KAQKLSKEPS VELTDTKSSD NVTPKQKSPN STEEDVSLNL KTLKAKKFKL
     AFVLITVLSF ITRFWNLNLP GEVVFDEVHF GKFASYYLQG KYFFDLHPPF AKLLLALVAK
     LAGYDGHYLF DNIGDNYKDN GVPYVTIRAW PALLSSLVPP VVFLIMKESG YDLLACIVSS
     SLVLFDNAHV TEGRLILLDA TLLFSMVCAI YCYVRFFKLR HTPFSRPWWA WLFFTGFFLS
     CTISTKYVGF FTFLSIGLSV CLELWYLWDI KTGLTVERFF QHFLARFFCL IFFPFLFFLF
     WFYMHFNILT ISGPGDSFMS LEFQETLSDN PITANSTILN YYDIVTIKHM GTNAFLHSHP
     EKYPIPYDDG RISSGGQQVT GYQFDDENNY WMILPADHYD PPIEAKLNVP VKNMDYIKLH
     HVGTNTDLMT HDVASPYHPT NEEFTTVSVD ESAGKKHEYT LFQVVMSDNT DPQRPLYTKA
     SSFKLIHKLT HVAMWSDPKP LPDWAFKQLE INGAKNIQTG SIFWTFDDII GLKDSRLKKE
     KKIPKKLPFW KKYLELQLTM FRQNNMLTEF HPYSSNPSDW FTLHHGIAFW AKSEENKQIY
     LLGNPIGWWI IAGTVLSTTV VAAAEILLRQ RGIRTLPETV RNHFYRSTMF FYMTYVFHYL
     PFFIMGRQLF LHHYLPAHLA GSLLVGAFIQ LACRKSFRSP VSAGVPIPKD VDEKGHSKCH
     RKYGHVIELI CTLLLIFVVI YCFTFFAPMT YGDKSLSVDE WTRRKWLDSW VFQYQKQN
//