PMT5_YEAST
ID PMT5_YEAST Reviewed; 743 AA.
AC P52867; D6VRQ5; Q92181;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 5 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775};
GN Name=PMT5 {ECO:0000303|PubMed:8923743};
GN OrderedLocusNames=YDL093W {ECO:0000312|SGD:S000002251};
GN ORFNames=D2399 {ECO:0000303|PubMed:8923743};
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].
RC STRAIN=ATCC 204508 / S288c;
RA Dommaschk U.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INTERACTION WITH PMT3 AND PMT2.
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 [6]
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).
CC -!- FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation
CC which is essential for cell wall rigidity. Forms a heterodimeric
CC complex with PMT3 and more rarely with PMT2 to transfer mannose from
CC Dol-P-mannose to Ser or Thr residues on proteins.
CC {ECO:0000303|PubMed:12551906}.
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:P33775};
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:P33775};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: PMT3 and PMT5 form a functional heterodimer. Forms also a
CC minor complex with PMT2. {ECO:0000269|PubMed:12551906}.
CC -!- INTERACTION:
CC P52867; P31382: PMT2; NbExp=2; IntAct=EBI-13591, EBI-13573;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; X92759; CAA63414.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64918.1; -; Genomic_DNA.
DR EMBL; Z74142; CAA98661.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11765.1; -; Genomic_DNA.
DR PIR; S67635; S67635.
DR RefSeq; NP_010190.1; NM_001180152.1.
DR AlphaFoldDB; P52867; -.
DR SMR; P52867; -.
DR BioGRID; 31967; 103.
DR ComplexPortal; CPX-3038; PMT5-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR ComplexPortal; CPX-3040; PMT5-PMT3 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR DIP; DIP-5025N; -.
DR IntAct; P52867; 5.
DR MINT; P52867; -.
DR STRING; 4932.YDL093W; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR iPTMnet; P52867; -.
DR MaxQB; P52867; -.
DR PaxDb; P52867; -.
DR PRIDE; P52867; -.
DR EnsemblFungi; YDL093W_mRNA; YDL093W; YDL093W.
DR GeneID; 851464; -.
DR KEGG; sce:YDL093W; -.
DR SGD; S000002251; PMT5.
DR VEuPathDB; FungiDB:YDL093W; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000176667; -.
DR HOGENOM; CLU_008438_2_1_1; -.
DR InParanoid; P52867; -.
DR OMA; MEFANDI; -.
DR BioCyc; YEAST:YDL093W-MON; -.
DR BRENDA; 2.4.1.109; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P52867; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P52867; protein.
DR GO; GO:0097584; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p 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; ISS:SGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS: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; IPR027004; PMT1/PTM5.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR PANTHER; PTHR10050:SF50; PTHR10050:SF50; 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..743
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 5"
FT /id="PRO_0000121495"
FT TOPO_DOM 1..46
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..158
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..231
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..583
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..646
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..743
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 320..374
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 384..444
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 454..510
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 743 AA; 84776 MW; E75625C236AC6A68 CRC64;
MNKEHLLKVD PIPDVTIKRG PLRSFLITKP CDNLSSLRTV TSSKEKLLVG CLLIFTAIVR
LHNISLPNSV VFGENEVGTF VSQYVNNIFF TDVHPPLVAM LYATVSSVFG YKGLFNYGNI
GTEYTANVPY VAMRFFSATL GIVSVLVLYL TLRVSGVKIA VAAICAVCFA IENSFVTLSR
FTLIEGPFVF FMACAVYFFR RSELYLPNSC KANKSLLAAS IALGFAVSSK WAGLFTIAWA
GIIVLWRVWF MIGDLSRPIG SSIKYMAFQF TCLLAIPAFI YFLIFSVHIK TLNVNGISSS
FFPAEFRKTL KYNNVIKETV AEVAVGSAVS LNHVGTAGGY LHSHLHNYPA GSMQQQVTLY
PHIDQNNKWI IELAEHPNEN VTSFQNLTDG TIIKLRQLKN GCRLHSHDHK PPVSQNADWQ
KEVSCYGYEG FEGDINDDWI IEIDKKRSEP GPAQEHIRAI ETKFRLKHYL TGCYLFSHPE
KLPEWGFGQQ EVTCAYFARE DLTSWYIEEN ENEISLPNPE KVSYKKMSFW QKFVAIHKFM
FYLNNYMDTS HAYSSEPKTW PLMLRGIDFW NENGREVYFL GNAVLWWSVT AFICTFIIGV
AVELLAWKLG VNILRDKHII NFHYQVFQYL LGFAAHYFPY FFVGQKLFLY DYLPAYYFGI
LAFGHALDLI STYISNKRNN TGYIVVAIFM VVCFYFFSEH SPLIYATGWS SNLCKRSKWL
GSWDFYCNSL LLSDSHYELN AES
