PMT7_YEAST
ID PMT7_YEAST Reviewed; 662 AA.
AC Q06644; D6VST6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775};
GN Name=PMT7 {ECO:0000312|SGD:S000002715};
GN OrderedLocusNames=YDR307W {ECO:0000312|SGD:S000002715};
GN ORFNames=D9740.4 {ECO:0000312|SGD:S000002715};
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 [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 [2]
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 [3]
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: Probable protein O-mannosyltransferase involved in O-
CC glycosylation which is essential for cell wall rigidity. Transfers
CC mannose from Dol-P-mannose to Ser or Thr residues on proteins.
CC {ECO:0000250|UniProtKB:P33775}.
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 -!- 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; U28374; AAB64743.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12146.1; -; Genomic_DNA.
DR PIR; S61193; S61193.
DR RefSeq; NP_010593.3; NM_001180615.3.
DR AlphaFoldDB; Q06644; -.
DR SMR; Q06644; -.
DR BioGRID; 32360; 120.
DR DIP; DIP-5150N; -.
DR IntAct; Q06644; 22.
DR MINT; Q06644; -.
DR STRING; 4932.YDR307W; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR MaxQB; Q06644; -.
DR PaxDb; Q06644; -.
DR PRIDE; Q06644; -.
DR EnsemblFungi; YDR307W_mRNA; YDR307W; YDR307W.
DR GeneID; 851902; -.
DR KEGG; sce:YDR307W; -.
DR SGD; S000002715; PMT7.
DR VEuPathDB; FungiDB:YDR307W; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_2_1_1; -.
DR InParanoid; Q06644; -.
DR OMA; RRINCSR; -.
DR BioCyc; YEAST:G3O-29866-MON; -.
DR BRENDA; 2.4.1.109; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q06644; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06644; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
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 PANTHER; PTHR10050; PTHR10050; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 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..662
FT /note="Probable dolichyl-phosphate-mannose--protein
FT mannosyltransferase 7"
FT /id="PRO_0000121497"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..195
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..482
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..617
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 289..344
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 359..418
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 432..488
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 662 AA; 77570 MW; 9083D1DF765A3AE5 CRC64;
MKDLRLQGPY RKYIPYNIFQ QCGIGHLKTL DYIFAFLIVI TNFTLIWKSH SSSFWNRPWD
NNSEQELSQL IQFYLDKAFY IHELPPFTIQ FYSIIRRLKI AENLRYVSLF LNSSTLGFLF
LITRRINCSR LISATGLLIL SNWETFRNEG TIISFDSLEW CLFSVVIYSF ISISIAKLGT
TNWFANVITL SISLGLAISS KFIGIVTWAF VILSFVRQFD RLISDVKVTT IQIIKFVILC
LLFVLIIPGS IFIISYSNLL SNFKTDTPQF SKYMSTYFKS YLRGPQVQPS RLYYGSTITL
RHLDSMVGYL ASHDISYPSD VDEQLVALSF EEFAADNEWL IEHPTLNLSF SEVYHADQLI
PVEFGQSIKL RHKSTGKLLR ASTAKPPISE QDYDFQISCT KDSNYEGGMD ERWDVLLIKD
EINNDKKDNA DDKYIKPLQS EIRFYNNGQR CGLLGHDLRL PEWGRFEQEV LCMEYPVIPR
TTFLIDSVQL PVDFQVPMIE YYIGKISSSA EFNHTLSWSQ FLYLFKEYIF KQYKYNYYIK
YGKNKVTFED AFAVEKWPIT LDTDSPVWFN FAWYGSLLSM IIFMCVQCKR MISWNPWTTA
EPSFSIKWEV YNEFGWECIV GWFLHFYIFT MSPHFNLGKK LYFQSFFFSV LCLLESLDCL
AK
