ID   PMT4_YEAST              Reviewed;         762 AA.
AC   P46971; D6VWW2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 4;
DE            EC=2.4.1.109 {ECO:0000269|PubMed:17470820};
GN   Name=PMT4 {ECO:0000303|PubMed:8585318};
GN   OrderedLocusNames=YJR143C {ECO:0000312|SGD:S000003904};
GN   ORFNames=J2176;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8585318; DOI=10.1002/yea.320111403;
RA   Immervoll T., Gentzsch M., Tanner W.;
RT   "PMT3 and PMT4, two new members of the protein-O-mannosyltransferase gene
RT   family of Saccharomyces cerevisiae.";
RL   Yeast 11:1345-1351(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=8918452; DOI=10.1002/j.1460-2075.1996.tb00961.x;
RA   Gaentzsch M., Tanner W.;
RT   "The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae
RT   is vital.";
RL   EMBO J. 15:5752-5759(1996).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9184828; DOI=10.1093/glycob/7.4.481;
RA   Gentzsch M., Tanner W.;
RT   "Protein-O-glycosylation in yeast: protein-specific mannosyltransferases.";
RL   Glycobiology 7:481-486(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=10366591; DOI=10.1083/jcb.145.6.1177;
RA   Sanders S.L., Gentzsch M., Tanner W., Herskowitz I.;
RT   "O-glycosylation of Axl2/Bud10p by Pmt4p is required for its stability,
RT   localization, and function in daughter cells.";
RL   J. Cell Biol. 145:1177-1188(1999).
RN   [7]
RP   SUBUNIT.
RX   PubMed=12551906; DOI=10.1074/jbc.m212582200;
RA   Girrbach V., Strahl S.;
RT   "Members of the evolutionarily conserved PMT family of protein O-
RT   mannosyltransferases form distinct protein complexes among themselves.";
RL   J. Biol. Chem. 278:12554-12562(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=14742720; DOI=10.1091/mbc.e03-07-0511;
RA   Proszynski T.J., Simons K., Bagnat M.;
RT   "O-glycosylation as a sorting determinant for cell surface delivery in
RT   yeast.";
RL   Mol. Biol. Cell 15:1533-1543(2004).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14673142; DOI=10.1128/mcb.24.1.46-57.2004;
RA   Lommel M., Bagnat M., Strahl S.;
RT   "Aberrant processing of the WSC family and Mid2p cell surface sensors
RT   results in cell death of Saccharomyces cerevisiae O-mannosylation
RT   mutants.";
RL   Mol. Cell. Biol. 24:46-57(2004).
RN   [11]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [12]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17470820; DOI=10.1073/pnas.0700374104;
RA   Hutzler J., Schmid M., Bernard T., Henrissat B., Strahl S.;
RT   "Membrane association is a determinant for substrate recognition by PMT4
RT   protein O-mannosyltransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7827-7832(2007).
RN   [13]
RP   INTERACTION WITH RCR1.
RX   PubMed=17213653; DOI=10.1271/bbb.60446;
RA   Imai K., Noda Y., Adachi H., Yoda K.;
RT   "Peculiar protein-protein interactions of the novel endoplasmic reticulum
RT   membrane protein Rcr1 and ubiquitin ligase Rsp5.";
RL   Biosci. Biotechnol. Biochem. 71:249-252(2007).
CC   -!- FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation
CC       which is essential for cell wall rigidity. Forms a homodimeric complex
CC       to transfer mannose from Dol-P-mannose to Ser or Thr residues on
CC       proteins. Specifically acts on secretory proteins with an ER-luminally
CC       oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1,
CC       AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176.
CC       {ECO:0000269|PubMed:10366591, ECO:0000269|PubMed:14673142,
CC       ECO:0000269|PubMed:17470820, ECO:0000269|PubMed:9184828}.
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         Evidence={ECO:0000269|PubMed:17470820};
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         Evidence={ECO:0000269|PubMed:17470820};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBUNIT: Forms a functional homodimer and may form a heterodimer with
CC       PMT6. Interacts with RCR1. {ECO:0000269|PubMed:12551906,
CC       ECO:0000269|PubMed:17213653, ECO:0000303|PubMed:9184828}.
CC   -!- INTERACTION:
CC       P46971; P46971: PMT4; NbExp=2; IntAct=EBI-13585, EBI-13585;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to diminished MID2 O-mannosylation.
CC       {ECO:0000269|PubMed:14673142}.
CC   -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC       {ECO:0000305}.
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DR   EMBL; X83798; CAA58729.1; -; Genomic_DNA.
DR   EMBL; Z49643; CAA89676.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08928.1; -; Genomic_DNA.
DR   PIR; S60415; S60415.
DR   RefSeq; NP_012677.1; NM_001181801.1.
DR   AlphaFoldDB; P46971; -.
DR   SMR; P46971; -.
DR   BioGRID; 33899; 172.
DR   ComplexPortal; CPX-3039; PMT4 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR   DIP; DIP-2549N; -.
DR   IntAct; P46971; 5.
DR   MINT; P46971; -.
DR   STRING; 4932.YJR143C; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; P46971; 1 site, No reported glycans.
DR   GlyGen; P46971; 1 site.
DR   iPTMnet; P46971; -.
DR   MaxQB; P46971; -.
DR   PaxDb; 4932-YJR143C; -.
DR   PeptideAtlas; P46971; -.
DR   EnsemblFungi; YJR143C_mRNA; YJR143C; YJR143C.
DR   GeneID; 853608; -.
DR   KEGG; sce:YJR143C; -.
DR   AGR; SGD:S000003904; -.
DR   SGD; S000003904; PMT4.
DR   VEuPathDB; FungiDB:YJR143C; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   GeneTree; ENSGT00940000158049; -.
DR   HOGENOM; CLU_008438_0_0_1; -.
DR   InParanoid; P46971; -.
DR   OMA; NCHLNAP; -.
DR   OrthoDB; 5489060at2759; -.
DR   BioCyc; YEAST:YJR143C-MONOMER; -.
DR   BRENDA; 2.4.1.109; 984.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 853608; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P46971; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P46971; Protein.
DR   GO; GO:0097586; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex; IPI:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; ISS:ComplexPortal.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IMP:SGD.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IDA:ComplexPortal.
DR   GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IGI:SGD.
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; 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   Reference proteome; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..762
FT                   /note="Dolichyl-phosphate-mannose--protein
FT                   mannosyltransferase 4"
FT                   /id="PRO_0000121494"
FT   TOPO_DOM        1..53
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..166
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..189
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..217
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..283
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..593
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        594..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        615..635
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        636..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        657..716
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        717..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        738..762
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          331..391
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          399..458
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          464..521
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        759
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   762 AA;  87966 MW;  0FBBEB283BBC0CBA CRC64;
     MSVPKKRNHG KLPPSTKDVD DPSLKYTKAA PKCEQVAEHW LLQPLPEPES RYSFWVTIVT
     LLAFAARFYK IWYPKEVVFD EVHFGKFASY YLERSYFFDV HPPFAKMMIA FIGWLCGYDG
     SFKFDEIGYS YETHPAPYIA YRSFNAILGT LTVPIMFNTL KELNFRAITC AFASLLVAID
     TAHVTETRLI LLDAILIISI AATMYCYVRF YKCQLRQPFT WSWYIWLHAT GLSLSFVIST
     KYVGVMTYSA IGFAAVVNLW QLLDIKAGLS LRQFMRHFSK RLNGLVLIPF VIYLFWFWVH
     FTVLNTSGPG DAFMSAEFQE TLKDSPLSVD SKTVNYFDII TIKHQDTDAF LHSHLARYPQ
     RYEDGRISSA GQQVTGYTHP DFNNQWEVLP PHGSDVGKGQ AVLLNQHIRL RHVATDTYLL
     AHDVASPFYP TNEEITTVTL EEGDGELYPE TLFAFQPLKK SDEGHVLKSK TVSFRLFHVD
     TSVALWTHND ELLPDWGFQQ QEINGNKKVI DPSNNWVVDE IVNLDEVRKV YIPKVVKPLP
     FLKKWIETQK SMFEHNNKLS SEHPFASEPY SWPGSLSGVS FWTNGDEKKQ IYFIGNIIGW
     WFQVISLAVF VGIIVADLIT RHRGYYALNK MTREKLYGPL MFFFVSWCCH YFPFFLMARQ
     KFLHHYLPAH LIACLFSGAL WEVIFSDCKS LDLEKDEDIS GASYERNPKV YVKPYTVFLV
     CVSCAVAWFF VYFSPLVYGD VSLSPSEVVS REWFDIELNF SK
//