ID   PMT3_YEAST              Reviewed;         753 AA.
AC   P47190; D6W319;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 3 {ECO:0000305};
DE            EC=2.4.1.109 {ECO:0000250|UniProtKB:P31382};
GN   Name=PMT3 {ECO:0000303|PubMed:8585318};
GN   OrderedLocusNames=YOR321W {ECO:0000312|SGD:S000005848};
GN   ORFNames=O6148 {ECO:0000312|SGD:S000005848};
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896266;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA   Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA   Schweizer M.;
RT   "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT   XV reveals regions of similarity to chromosomes I and XIII.";
RL   Yeast 12:1021-1031(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
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   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
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   INTERACTION WITH PMT5 AND PMT1.
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   [7]
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   [8]
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   [9]
RP   INDUCTION.
RX   PubMed=21231968; DOI=10.1111/j.1365-2958.2011.07537.x;
RA   Arroyo J., Hutzler J., Bermejo C., Ragni E., Garcia-Cantalejo J.,
RA   Botias P., Piberger H., Schott A., Sanz A.B., Strahl S.;
RT   "Functional and genomic analyses of blocked protein O-mannosylation in
RT   baker's yeast.";
RL   Mol. Microbiol. 79:1529-1546(2011).
CC   -!- FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation
CC       which is essential for cell wall rigidity. Forms a heterodimeric
CC       complex with PMT5 and more rarely with PMT1 to transfer mannose from
CC       Dol-P-mannose to Ser or Thr residues on proteins. Seems to have
CC       redundant activity to PMT2. {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:0000250|UniProtKB:P31382};
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:0000250|UniProtKB:P31382};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBUNIT: PMT3 and PMT5 form a functional heterodimer. Forms also a
CC       minor complex with PMT1. {ECO:0000269|PubMed:12551906}.
CC   -!- INTERACTION:
CC       P47190; P33775: PMT1; NbExp=3; IntAct=EBI-13579, EBI-13567;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Specifically induced upon tunicamycin, DTT as well as
CC       rhodanine-3-acetic acid derivative OGT2468 treatment.
CC       {ECO:0000269|PubMed:21231968}.
CC   -!- DISRUPTION PHENOTYPE: Affects O-mannosylation activity only when PTM1
CC       and PTM2 are absent. {ECO:0000269|PubMed:9184828}.
CC   -!- MISCELLANEOUS: Present with 2720 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; X83797; CAA58728.1; -; Genomic_DNA.
DR   EMBL; X90565; CAA62176.1; -; Genomic_DNA.
DR   EMBL; Z75229; CAA99641.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11085.1; -; Genomic_DNA.
DR   PIR; S58331; S58331.
DR   RefSeq; NP_014966.1; NM_001183741.1.
DR   PDB; 6ZQQ; X-ray; 1.90 A; A/B/C/D=331-532.
DR   PDBsum; 6ZQQ; -.
DR   AlphaFoldDB; P47190; -.
DR   SMR; P47190; -.
DR   BioGRID; 34707; 150.
DR   ComplexPortal; CPX-3037; PMT1-PMT3 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR   ComplexPortal; CPX-3040; PMT5-PMT3 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR   DIP; DIP-5158N; -.
DR   IntAct; P47190; 5.
DR   STRING; 4932.YOR321W; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; P47190; 3 sites, No reported glycans.
DR   GlyGen; P47190; 3 sites.
DR   iPTMnet; P47190; -.
DR   MaxQB; P47190; -.
DR   PaxDb; 4932-YOR321W; -.
DR   PeptideAtlas; P47190; -.
DR   EnsemblFungi; YOR321W_mRNA; YOR321W; YOR321W.
DR   GeneID; 854499; -.
DR   KEGG; sce:YOR321W; -.
DR   AGR; SGD:S000005848; -.
DR   SGD; S000005848; PMT3.
DR   VEuPathDB; FungiDB:YOR321W; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   GeneTree; ENSGT00940000156829; -.
DR   HOGENOM; CLU_008438_5_0_1; -.
DR   InParanoid; P47190; -.
DR   OMA; WEVSAYG; -.
DR   OrthoDB; 5489060at2759; -.
DR   BioCyc; YEAST:YOR321W-MONOMER; -.
DR   BRENDA; 2.4.1.109; 984.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 854499; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P47190; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P47190; Protein.
DR   GO; GO:0097583; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex; IDA:SGD.
DR   GO; GO:0097585; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt3p dimer complex; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:ComplexPortal.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISA:SGD.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; ISS:ComplexPortal.
DR   GO; GO:0006493; P:protein O-linked glycosylation; ISA:SGD.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IGI:SGD.
DR   GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; NAS:ComplexPortal.
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:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 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   3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Membrane; Reference proteome; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..753
FT                   /note="Dolichyl-phosphate-mannose--protein
FT                   mannosyltransferase 3"
FT                   /id="PRO_0000121493"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..148
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..174
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..235
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..602
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        624..639
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        661..665
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        666..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        687..703
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        704..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        725..753
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          332..387
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          401..457
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          465..523
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        397
FT                   /note="E -> H (in Ref. 1; CAA58728)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        567
FT                   /note="D -> N (in Ref. 1; CAA58728)"
FT                   /evidence="ECO:0000305"
FT   TURN            337..339
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          341..346
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          353..360
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          368..375
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   HELIX           378..380
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          382..385
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          409..414
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          420..427
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          434..440
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          443..445
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   HELIX           448..450
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          452..459
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   TURN            470..472
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          473..479
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   TURN            480..482
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          485..492
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   HELIX           495..497
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          501..506
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   HELIX           514..516
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
FT   STRAND          518..524
FT                   /evidence="ECO:0007829|PDB:6ZQQ"
SQ   SEQUENCE   753 AA;  86323 MW;  F076473B41EB6CBA CRC64;
     MPYRVATGYS EKSTDDDLIW RTPIVKEELE DADNFLKDDA ELYDKVKNES AVSHLDTIVM
     PIIFTVLGMF TRMYKIGRNN HVVWDEAHFG KFGSYYLRHE FYHDVHPPLG KMLVGLSGYL
     AGYNGSWDFP SGEVYPDYID YVKMRLFQAM FSSLCVPLAY FTGRAIGFSR LSVWLFTILV
     IFENSYATLG KFILLDSMLL FFTVSSYFCL AKFHTMRKSP FSARWWLWLC LTGLNLGCAI
     SVKMVGLFII SVVGIYTISE LWNLLSDRSV SWKVYVNHWL ARIFGLIIIP VCVFLLCFKI
     HFDLLSNSGP GDSTMPSLFQ ASLNGTKVGK GPRDVALGSS IISIKNQALG GALLHSHVQP
     FPEGSEQQQV TVYGYSDANN EWFFQRIRGV EPWTDAENKT IEFVKGGEMY RLMHRLTGKN
     LHTHEVPAPI SKSEYEVSAY GDVDLGDYKD NWIIEIVEQV GEEDPTLLHP LSTSFRIKNS
     ILGCYLAQSG KHLPEWGFRQ GEVVCLKHAS KRDKRTWWNI ETHENERLPQ GEDFVYPKTS
     FFRNFMQLNS AMMATNNALV PNPEKFDGIA SSAWQWPTLN VGVRLCEWSE KSIKYFLLGS
     PASVWPSSIA VCALIIHVIF LTLKWQRQCV ILSDPVERDV FVMAAFYPLL AWLLHYMPFV
     VMSRVVYAHH YLPTLYFALM ILSYYFDMIT KRWATRNTGK FLRLGAYIVY GSIVIAGFFY
     FSPFSFGMDG PVDDYAYLAW LPTWQIVEDI RNT
//