PMT4_SCHPO
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 03-AUG-2022, entry version 157.
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; 4896.SPBC16C6.09.1; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR iPTMnet; O42933; -.
DR MaxQB; O42933; -.
DR PaxDb; O42933; -.
DR PRIDE; O42933; -.
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; FWTQNDT; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 2.
DR SUPFAM; SSF82109; SSF82109; 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
