PMT4_YEAST
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 03-AUG-2022, entry version 185.
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}; 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; 145.
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 iPTMnet; P46971; -.
DR MaxQB; P46971; -.
DR PaxDb; P46971; -.
DR PRIDE; P46971; -.
DR EnsemblFungi; YJR143C_mRNA; YJR143C; YJR143C.
DR GeneID; 853608; -.
DR KEGG; sce:YJR143C; -.
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; FWTQNDT; -.
DR BioCyc; YEAST:YJR143C-MON; -.
DR BRENDA; 2.4.1.109; 984.
DR UniPathway; UPA00378; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 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 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
