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   27-MAR-2024, entry version 176.
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}.
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; 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; 124.
DR   DIP; DIP-5150N; -.
DR   IntAct; Q06644; 22.
DR   MINT; Q06644; -.
DR   STRING; 4932.YDR307W; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; Q06644; 1 site, No reported glycans.
DR   GlyGen; Q06644; 1 site.
DR   MaxQB; Q06644; -.
DR   PaxDb; 4932-YDR307W; -.
DR   PeptideAtlas; Q06644; -.
DR   EnsemblFungi; YDR307W_mRNA; YDR307W; YDR307W.
DR   GeneID; 851902; -.
DR   KEGG; sce:YDR307W; -.
DR   AGR; SGD:S000002715; -.
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   OrthoDB; 2010953at2759; -.
DR   BioCyc; YEAST:G3O-29866-MONOMER; -.
DR   BRENDA; 2.4.1.109; 984.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 851902; 0 hits in 10 CRISPR screens.
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:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
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   PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF02366; PMT; 1.
DR   SMART; SM00472; MIR; 3.
DR   SUPFAM; SSF82109; MIR domain; 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
//