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Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC 2.4.1.109)

 PMT1_YEAST              Reviewed;         817 AA.
P33775; D6VRQ4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
22-NOV-2017, entry version 164.
RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1 {ECO:0000305};
EC=2.4.1.109 {ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:8367478};
Name=PMT1 {ECO:0000303|PubMed:8367478};
OrderedLocusNames=YDL095W {ECO:0000312|SGD:S000002253};
ORFNames=D2390 {ECO:0000312|SGD:S000002253};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE,
IDENTIFICATION, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=8367478; DOI=10.1073/pnas.90.17.8164;
Strahl-Bolsinger S., Immervoll T., Deutzmann R., Tanner W.;
"PMT1, the gene for a key enzyme of protein O-glycosylation in
Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 90:8164-8168(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8923743;
DOI=10.1002/(SICI)1097-0061(199610)12:13<1377::AID-YEA35>3.0.CO;2-R;
Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
Jimenez A., Remacha M.A.;
"The sequence of a 16,691 bp segment of Saccharomyces cerevisiae
chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes,
and five new open reading frames.";
Yeast 12:1377-1384(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, AND INTERACTION WITH PMT2.
PubMed=8543034; DOI=10.1016/0014-5793(95)01324-5;
Gentzsch M., Immervoll T., Tanner W.;
"Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-
mannosyltransferases Pmt1p and Pmt2p function as heterodimer.";
FEBS Lett. 377:128-130(1995).
[6]
DISRUPTION PHENOTYPE.
PubMed=8918452;
Gaentzsch M., Tanner W.;
"The PMT gene family: protein O-glycosylation in Saccharomyces
cerevisiae is vital.";
EMBO J. 15:5752-5759(1996).
[7]
FUNCTION.
PubMed=9466258; DOI=10.1046/j.1365-2958.1998.00660.x;
Bourdineaud J.P., van der Vaart J.M., Donzeau M., de Sampaio G.,
Verrips C.T., Lauquin G.J.;
"Pmt1 mannosyl transferase is involved in cell wall incorporation of
several proteins in Saccharomyces cerevisiae.";
Mol. Microbiol. 27:85-98(1998).
[8]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=10085156; DOI=10.1074/jbc.274.13.9068;
Strahl-Bolsinger S., Scheinost A.;
"Transmembrane topology of pmt1p, a member of an evolutionarily
conserved family of protein O-mannosyltransferases.";
J. Biol. Chem. 274:9068-9075(1999).
[9]
FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF ARG-64;
GLU-78; ARG-138 AND LEU-408.
PubMed=10764776; DOI=10.1074/jbc.M001771200;
Girrbach V., Zeller T., Priesmeier M., Strahl-Bolsinger S.;
"Structure-function analysis of the dolichyl phosphate-mannose:
protein O-mannosyltransferase ScPmt1p.";
J. Biol. Chem. 275:19288-19296(2000).
[10]
INTERACTION WITH PMT2 AND PMT3.
PubMed=12551906; DOI=10.1074/jbc.M212582200;
Girrbach V., Strahl S.;
"Members of the evolutionarily conserved PMT family of protein O-
mannosyltransferases form distinct protein complexes among
themselves.";
J. Biol. Chem. 278:12554-12562(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[13]
FUNCTION.
PubMed=18182384; DOI=10.1093/jb/mvm249;
Hirayama H., Fujita M., Yoko-o T., Jigami Y.;
"O-mannosylation is required for degradation of the endoplasmic
reticulum-associated degradation substrate Gas1*p via the
ubiquitin/proteasome pathway in Saccharomyces cerevisiae.";
J. Biochem. 143:555-567(2008).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 77-ASP-GLU-78;
GLU-78; TYR-88 AND PRO-100.
PubMed=21956107; DOI=10.1074/jbc.M111.281196;
Lommel M., Schott A., Jank T., Hofmann V., Strahl S.;
"A conserved acidic motif is crucial for enzymatic activity of protein
O-mannosyltransferases.";
J. Biol. Chem. 286:39768-39775(2011).
[15]
FUNCTION OF THE PMT1-PMT2 COMPLEX, AND INTERACTION WITH PMT2; EMP24;
ERV25; ERP1; ERP2; CDC48; HRD1; USA1; YOS9; ERO1; PDI1; UBR1; CUE4;
DFM1 AND TED1.
PubMed=21147851; DOI=10.1242/jcs.072181;
Goder V., Melero A.;
"Protein O-mannosyltransferases participate in ER protein quality
control.";
J. Cell Sci. 124:144-153(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Protein O-mannosyltransferase involved in O-
glycosylation which is essential for cell wall rigidity. Forms a
heterodimeric complex with PMT2 and more rarely with PMT3 to
transfer mannose from Dol-P-mannose to Ser or Thr residues on
proteins. The PMT1-PMT2 complex participates in oxidative protein
folding, ER-associated protein degradation (ERAD), as well as ER
export. Required for incorporation of proteins in the cell wall.
{ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:18182384,
ECO:0000269|PubMed:8367478, ECO:0000269|PubMed:8543034,
ECO:0000269|PubMed:9466258}.
-!- CATALYTIC ACTIVITY: Dolichyl D-mannosyl phosphate + protein =
dolichyl phosphate + O-D-mannosylprotein.
{ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:8367478}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000305}.
-!- SUBUNIT: PMT1 and PMT2 form a functional heterodimer. The complex
interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1,
ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and
TED1. Forms also a minor complex with PMT3.
{ECO:0000269|PubMed:12551906, ECO:0000269|PubMed:21147851,
ECO:0000269|PubMed:8543034}.
-!- INTERACTION:
P31382:PMT2; NbExp=4; IntAct=EBI-13567, EBI-13573;
P47190:PMT3; NbExp=3; IntAct=EBI-13567, EBI-13579;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000303|PubMed:10085156}; Multi-pass membrane protein
{ECO:0000269|PubMed:10085156}.
-!- DOMAIN: The large luminal loop 5 is essential for
mannosyltransferase activity but not for PMT1-PMT2 complex
formation. {ECO:0000269|PubMed:10764776}.
-!- DISRUPTION PHENOTYPE: Affects glycosylation of chitinase and
increases sensitivity to calcofluor white and caffeine.
{ECO:0000269|PubMed:8918452}.
-!- MISCELLANEOUS: Present with 41500 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L19169; AAA02928.1; -; Unassigned_DNA.
EMBL; X95644; CAA64917.1; -; Genomic_DNA.
EMBL; Z74144; CAA98663.1; -; Genomic_DNA.
EMBL; BK006938; DAA11764.1; -; Genomic_DNA.
PIR; A47716; A47716.
RefSeq; NP_010188.1; NM_001180154.1.
ProteinModelPortal; P33775; -.
BioGrid; 31966; 202.
DIP; DIP-7911N; -.
IntAct; P33775; 2.
MINT; MINT-2787975; -.
STRING; 4932.YDL095W; -.
CAZy; GT39; Glycosyltransferase Family 39.
iPTMnet; P33775; -.
MaxQB; P33775; -.
PRIDE; P33775; -.
EnsemblFungi; YDL095W; YDL095W; YDL095W.
GeneID; 851462; -.
KEGG; sce:YDL095W; -.
EuPathDB; FungiDB:YDL095W; -.
SGD; S000002253; PMT1.
GeneTree; ENSGT00870000137379; -.
HOGENOM; HOG000157526; -.
InParanoid; P33775; -.
KO; K00728; -.
OMA; MSSEFQA; -.
OrthoDB; EOG092C0JF4; -.
BioCyc; YEAST:YDL095W-MONOMER; -.
BRENDA; 2.4.1.109; 984.
UniPathway; UPA00378; -.
PRO; PR:P33775; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0097582; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex; IDA:SGD.
GO; GO:0097583; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:SGD.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
GO; GO:0032527; P:protein exit from endoplasmic reticulum; IGI:SGD.
GO; GO:0035269; P:protein O-linked mannosylation; IDA:SGD.
GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
InterPro; IPR027005; GlyclTrfase_39-like.
InterPro; IPR003342; Glyco_trans_39/83.
InterPro; IPR036300; MIR_dom_sf.
InterPro; IPR016093; MIR_motif.
InterPro; IPR032421; PMT_4TMC.
PANTHER; PTHR10050; PTHR10050; 1.
Pfam; PF02815; MIR; 1.
Pfam; PF02366; PMT; 1.
Pfam; PF16192; PMT_4TMC; 1.
SMART; SM00472; MIR; 3.
SUPFAM; SSF82109; SSF82109; 1.
PROSITE; PS50919; MIR; 3.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
Reference proteome; Repeat; Transferase; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 817 Dolichyl-phosphate-mannose--protein
mannosyltransferase 1.
/FTId=PRO_0000121491.
TOPO_DOM 2 50 Cytoplasmic.
{ECO:0000269|PubMed:10085156}.
TRANSMEM 51 70 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 71 135 Lumenal. {ECO:0000269|PubMed:10085156}.
TRANSMEM 136 154 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 155 179 Cytoplasmic.
{ECO:0000269|PubMed:10085156}.
TRANSMEM 180 200 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 201 234 Lumenal. {ECO:0000269|PubMed:10085156}.
TRANSMEM 235 259 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 260 273 Cytoplasmic.
{ECO:0000269|PubMed:10085156}.
TRANSMEM 274 291 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 292 584 Lumenal. {ECO:0000269|PubMed:10085156}.
TRANSMEM 585 605 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 606 685 Cytoplasmic.
{ECO:0000269|PubMed:10085156}.
TRANSMEM 686 710 Helical. {ECO:0000269|PubMed:10085156}.
TOPO_DOM 711 817 Lumenal. {ECO:0000269|PubMed:10085156}.
DOMAIN 324 378 MIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 388 448 MIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 459 514 MIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 743 743 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 64 64 R->A: Reduces mannosyltransferase
activity. {ECO:0000269|PubMed:10764776}.
MUTAGEN 77 78 DE->AA: Impairs mannosyltransferase
activity. {ECO:0000269|PubMed:21956107}.
MUTAGEN 78 78 E->A: Decreases substrate-binding and
reduces mannosyltransferase activity.
{ECO:0000269|PubMed:10764776,
ECO:0000269|PubMed:21956107}.
MUTAGEN 88 88 Y->A: Moderately decreases complex
formation with PMT2.
{ECO:0000269|PubMed:21956107}.
MUTAGEN 100 100 P->A: Moderately decreases complex
formation with PMT2.
{ECO:0000269|PubMed:21956107}.
MUTAGEN 138 138 R->A: Impairs complex formation with
PMT2. {ECO:0000269|PubMed:10764776}.
MUTAGEN 408 408 L->A: Reduces mannosyltransferase
activity. {ECO:0000269|PubMed:10764776}.
SEQUENCE 817 AA; 92675 MW; 6309BBA71BAD8D21 CRC64;
MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK LLVACLAVFT
AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP LAKMLYAGVA SLGGFQGDFD
FENIGDSFPS TTPYVLMRFF SASLGALTVI LMYMTLRYSG VRMWVALMSA ICFAVENSYV
TISRYILLDA PLMFFIAAAV YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT
VTWVGLLCIW RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH NYPAGSEQQQ
STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF HTVTRCRLHS HDHKPPVSES
SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK NSAPGVAQER VIALDTKFRL RHAMTGCYLF
SHEVKLPAWG FEQQEVTCAS SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES
HKKMWHINKN LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ MFLHHYLPAY
YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF FKSFSPIIYG TPWTQELCQK
SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE SQPAATSTVE EITIEGDGPS YEDLMNEDGK
KIFKDTEGNE LDPEVVKKML EEEGANILKV EKRAVLE


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