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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: -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 D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: SGD

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, 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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL093W
SGDiS000002251 PMT5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 46LumenalSequence analysisAdd BLAST46
Transmembranei47 – 67HelicalSequence analysisAdd BLAST21
Topological domaini68 – 129CytoplasmicSequence analysisAdd BLAST62
Transmembranei130 – 150HelicalSequence analysisAdd BLAST21
Topological domaini151 – 158LumenalSequence analysis8
Transmembranei159 – 179HelicalSequence analysisAdd BLAST21
Topological domaini180CytoplasmicSequence analysis1
Transmembranei181 – 201HelicalSequence analysisAdd BLAST21
Topological domaini202 – 231LumenalSequence analysisAdd BLAST30
Transmembranei232 – 252HelicalSequence analysisAdd BLAST21
Topological domaini253 – 264CytoplasmicSequence analysisAdd BLAST12
Transmembranei265 – 285HelicalSequence analysisAdd BLAST21
Topological domaini286 – 583LumenalSequence analysisAdd BLAST298
Transmembranei584 – 604HelicalSequence analysisAdd BLAST21
Topological domaini605 – 623CytoplasmicSequence analysisAdd BLAST19
Transmembranei624 – 644HelicalSequence analysisAdd BLAST21
Topological domaini645 – 646LumenalSequence analysis2
Transmembranei647 – 667HelicalSequence analysisAdd BLAST21
Topological domaini668 – 683CytoplasmicSequence analysisAdd BLAST16
Transmembranei684 – 704HelicalSequence analysisAdd BLAST21
Topological domaini705 – 743LumenalSequence analysisAdd BLAST39

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001214951 – 743Dolichyl-phosphate-mannose--protein mannosyltransferase 5Add BLAST743

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi33N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi380N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi386N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP52867
PaxDbiP52867
PRIDEiP52867

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, 102 interactors
DIPiDIP-5025N
IntActiP52867, 7 interactors
MINTiP52867
STRINGi4932.YDL093W

Structurei

3D structure databases

ProteinModelPortaliP52867
SMRiP52867
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini320 – 374MIR 1PROSITE-ProRule annotationAdd BLAST55
Domaini384 – 444MIR 2PROSITE-ProRule annotationAdd BLAST61
Domaini454 – 510MIR 3PROSITE-ProRule annotationAdd BLAST57

Sequence similaritiesi

Belongs to the glycosyltransferase 39 family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00870000137379
HOGENOMiHOG000157526
InParanoidiP52867
KOiK00728
OMAiMEFANDI
OrthoDBiEOG092C0JF4

Family and domain databases

InterProiView protein in InterPro
IPR027005 GlyclTrfase_39-like
IPR003342 Glyco_trans_39/83
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR032421 PMT_4TMC
PANTHERiPTHR10050 PTHR10050, 1 hit
PfamiView protein in Pfam
PF02815 MIR, 1 hit
PF02366 PMT, 1 hit
PF16192 PMT_4TMC, 1 hit
SMARTiView protein in SMART
SM00472 MIR, 3 hits
SUPFAMiSSF82109 SSF82109, 1 hit
PROSITEiView protein in PROSITE
PS50919 MIR, 3 hits

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:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiPMT5_YEAST
AccessioniPrimary (citable) accession number: P52867
Secondary accession number(s): D6VRQ5, Q92181
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 151 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health