PMT3_YEAST
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 03-AUG-2022, entry version 177.
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}.
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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 iPTMnet; P47190; -.
DR MaxQB; P47190; -.
DR PaxDb; P47190; -.
DR PRIDE; P47190; -.
DR EnsemblFungi; YOR321W_mRNA; YOR321W; YOR321W.
DR GeneID; 854499; -.
DR KEGG; sce:YOR321W; -.
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; DYAYLAW; -.
DR BioCyc; YEAST:YOR321W-MON; -.
DR BRENDA; 2.4.1.109; 984.
DR UniPathway; UPA00378; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISA:SGD.
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; IC:ComplexPortal.
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 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
