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P52867

- PMT5_YEAST

UniProt

P52867 - PMT5_YEAST

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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 5

Gene

PMT5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT3 and more rarely with PMT2 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins.1 Publication

Catalytic activityi

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.By similarity

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: SGD

GO - Biological processi

  1. protein O-linked mannosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YDL093W-MONOMER.
BRENDAi2.4.1.109. 984.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 5Curated (EC:2.4.1.109By similarity)
Gene namesi
Name:PMT51 Publication
Ordered Locus Names:YDL093WImported
ORF Names:D23991 Publication
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL093w.
SGDiS000002251. PMT5.

Subcellular locationi

Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence Analysis

GO - Cellular componenti

  1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex Source: SGD
  2. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt3p dimer complex Source: SGD
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 743743Dolichyl-phosphate-mannose--protein mannosyltransferase 5PRO_0000121495Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP52867.
PeptideAtlasiP52867.

Expressioni

Gene expression databases

GenevestigatoriP52867.

Interactioni

Subunit structurei

PMT3 and PMT5 form a functional heterodimer. Forms also a minor complex with PMT2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PMT2P313822EBI-13591,EBI-13573

Protein-protein interaction databases

BioGridi31967. 25 interactions.
DIPiDIP-5025N.
IntActiP52867. 4 interactions.
MINTiMINT-563573.
STRINGi4932.YDL093W.

Structurei

3D structure databases

ProteinModelPortaliP52867.
SMRiP52867. Positions 338-492.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646LumenalSequence AnalysisAdd
BLAST
Topological domaini68 – 12962CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini151 – 1588LumenalSequence Analysis
Topological domaini180 – 1801CytoplasmicSequence Analysis
Topological domaini202 – 23130LumenalSequence AnalysisAdd
BLAST
Topological domaini253 – 26412CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini286 – 583298LumenalSequence AnalysisAdd
BLAST
Topological domaini605 – 62319CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini645 – 6462LumenalSequence Analysis
Topological domaini668 – 68316CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini705 – 74339LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei47 – 6721HelicalSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Transmembranei159 – 17921HelicalSequence AnalysisAdd
BLAST
Transmembranei181 – 20121HelicalSequence AnalysisAdd
BLAST
Transmembranei232 – 25221HelicalSequence AnalysisAdd
BLAST
Transmembranei265 – 28521HelicalSequence AnalysisAdd
BLAST
Transmembranei584 – 60421HelicalSequence AnalysisAdd
BLAST
Transmembranei624 – 64421HelicalSequence AnalysisAdd
BLAST
Transmembranei647 – 66721HelicalSequence AnalysisAdd
BLAST
Transmembranei684 – 70421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini320 – 37455MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini384 – 44461MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini454 – 51057MIR 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 39 family.Curated
Contains 3 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1928.
GeneTreeiENSGT00740000116239.
HOGENOMiHOG000157526.
InParanoidiP52867.
KOiK00728.
OMAiMEFANDI.
OrthoDBiEOG7BP89X.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52867-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKEHLLKVD PIPDVTIKRG PLRSFLITKP CDNLSSLRTV TSSKEKLLVG
60 70 80 90 100
CLLIFTAIVR LHNISLPNSV VFGENEVGTF VSQYVNNIFF TDVHPPLVAM
110 120 130 140 150
LYATVSSVFG YKGLFNYGNI GTEYTANVPY VAMRFFSATL GIVSVLVLYL
160 170 180 190 200
TLRVSGVKIA VAAICAVCFA IENSFVTLSR FTLIEGPFVF FMACAVYFFR
210 220 230 240 250
RSELYLPNSC KANKSLLAAS IALGFAVSSK WAGLFTIAWA GIIVLWRVWF
260 270 280 290 300
MIGDLSRPIG SSIKYMAFQF TCLLAIPAFI YFLIFSVHIK TLNVNGISSS
310 320 330 340 350
FFPAEFRKTL KYNNVIKETV AEVAVGSAVS LNHVGTAGGY LHSHLHNYPA
360 370 380 390 400
GSMQQQVTLY PHIDQNNKWI IELAEHPNEN VTSFQNLTDG TIIKLRQLKN
410 420 430 440 450
GCRLHSHDHK PPVSQNADWQ KEVSCYGYEG FEGDINDDWI IEIDKKRSEP
460 470 480 490 500
GPAQEHIRAI ETKFRLKHYL TGCYLFSHPE KLPEWGFGQQ EVTCAYFARE
510 520 530 540 550
DLTSWYIEEN ENEISLPNPE KVSYKKMSFW QKFVAIHKFM FYLNNYMDTS
560 570 580 590 600
HAYSSEPKTW PLMLRGIDFW NENGREVYFL GNAVLWWSVT AFICTFIIGV
610 620 630 640 650
AVELLAWKLG VNILRDKHII NFHYQVFQYL LGFAAHYFPY FFVGQKLFLY
660 670 680 690 700
DYLPAYYFGI LAFGHALDLI STYISNKRNN TGYIVVAIFM VVCFYFFSEH
710 720 730 740
SPLIYATGWS SNLCKRSKWL GSWDFYCNSL LLSDSHYELN AES
Length:743
Mass (Da):84,776
Last modified:October 1, 1996 - v1
Checksum:iE75625C236AC6A68
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92759 Genomic DNA. Translation: CAA63414.1.
X95644 Genomic DNA. Translation: CAA64918.1.
Z74142 Genomic DNA. Translation: CAA98661.1.
BK006938 Genomic DNA. Translation: DAA11765.1.
PIRiS67635.
RefSeqiNP_010190.1. NM_001180152.1.

Genome annotation databases

EnsemblFungiiYDL093W; YDL093W; YDL093W.
GeneIDi851464.
KEGGisce:YDL093W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92759 Genomic DNA. Translation: CAA63414.1 .
X95644 Genomic DNA. Translation: CAA64918.1 .
Z74142 Genomic DNA. Translation: CAA98661.1 .
BK006938 Genomic DNA. Translation: DAA11765.1 .
PIRi S67635.
RefSeqi NP_010190.1. NM_001180152.1.

3D structure databases

ProteinModelPortali P52867.
SMRi P52867. Positions 338-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31967. 25 interactions.
DIPi DIP-5025N.
IntActi P52867. 4 interactions.
MINTi MINT-563573.
STRINGi 4932.YDL093W.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi P52867.
PeptideAtlasi P52867.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL093W ; YDL093W ; YDL093W .
GeneIDi 851464.
KEGGi sce:YDL093W.

Organism-specific databases

CYGDi YDL093w.
SGDi S000002251. PMT5.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000116239.
HOGENOMi HOG000157526.
InParanoidi P52867.
KOi K00728.
OMAi MEFANDI.
OrthoDBi EOG7BP89X.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci YEAST:YDL093W-MONOMER.
BRENDAi 2.4.1.109. 984.

Miscellaneous databases

NextBioi 968747.

Gene expression databases

Genevestigatori P52867.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
Pfami PF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view ]
SMARTi SM00472. MIR. 3 hits.
[Graphical view ]
SUPFAMi SSF82109. SSF82109. 1 hit.
PROSITEi PS50919. MIR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Dommaschk U.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "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."
    Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
    Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    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.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves."
    Girrbach V., Strahl S.
    J. Biol. Chem. 278:12554-12562(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PMT3 AND PMT2.
  6. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiPMT5_YEAST
AccessioniPrimary (citable) accession number: P52867
Secondary accession number(s): D6VRQ5, Q92181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3