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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 3

Gene

PMT3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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 PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to have redundant activity to PMT2.1 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YOR321W-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 3Curated (EC:2.4.1.109By similarity)
Gene namesi
Name:PMT31 Publication
Ordered Locus Names:YOR321WImported
ORF Names:O6148Imported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR321W.
SGDiS000005848. PMT3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 50CytoplasmicSequence analysisAdd BLAST49
Transmembranei51 – 71HelicalSequence analysisAdd BLAST21
Topological domaini72 – 148LumenalSequence analysisAdd BLAST77
Transmembranei149 – 169HelicalSequence analysisAdd BLAST21
Topological domaini170 – 174CytoplasmicSequence analysis5
Transmembranei175 – 195HelicalSequence analysisAdd BLAST21
Topological domaini196 – 235LumenalSequence analysisAdd BLAST40
Transmembranei236 – 256HelicalSequence analysisAdd BLAST21
Topological domaini257 – 282CytoplasmicSequence analysisAdd BLAST26
Transmembranei283 – 303HelicalSequence analysisAdd BLAST21
Topological domaini304 – 602LumenalSequence analysisAdd BLAST299
Transmembranei603 – 623HelicalSequence analysisAdd BLAST21
Topological domaini624 – 639CytoplasmicSequence analysisAdd BLAST16
Transmembranei640 – 660HelicalSequence analysisAdd BLAST21
Topological domaini661 – 665LumenalSequence analysis5
Transmembranei666 – 686HelicalSequence analysisAdd BLAST21
Topological domaini687 – 703CytoplasmicSequence analysisAdd BLAST17
Transmembranei704 – 724HelicalSequence analysisAdd BLAST21
Topological domaini725 – 753LumenalSequence analysisAdd BLAST29

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Affects O-mannosylation activity only when PTM1 and PTM2 are absent.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001214932 – 753Dolichyl-phosphate-mannose--protein mannosyltransferase 3Add BLAST752

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi124N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi398N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP47190.
PRIDEiP47190.

Expressioni

Inductioni

Specifically induced upon tunicamycin, DTT as well as rhodanine-3-acetic acid derivative OGT2468 treatment.1 Publication

Interactioni

Subunit structurei

PMT3 and PMT5 form a functional heterodimer. Forms also a minor complex with PMT1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PMT1P337753EBI-13579,EBI-13567

Protein-protein interaction databases

BioGridi34707. 23 interactors.
DIPiDIP-5158N.
IntActiP47190. 4 interactors.
MINTiMINT-574047.

Structurei

3D structure databases

ProteinModelPortaliP47190.
SMRiP47190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini332 – 387MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini401 – 457MIR 2PROSITE-ProRule annotationAdd BLAST57
Domaini465 – 523MIR 3PROSITE-ProRule annotationAdd BLAST59

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00860000133869.
HOGENOMiHOG000157526.
InParanoidiP47190.
KOiK00728.
OMAiYTISELW.
OrthoDBiEOG092C0JF4.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39-like.
IPR003342. Glyco_trans_39/83.
IPR016093. MIR_motif.
IPR032421. PMT_4TMC.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
PF16192. PMT_4TMC. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47190-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPYRVATGYS EKSTDDDLIW RTPIVKEELE DADNFLKDDA ELYDKVKNES
60 70 80 90 100
AVSHLDTIVM PIIFTVLGMF TRMYKIGRNN HVVWDEAHFG KFGSYYLRHE
110 120 130 140 150
FYHDVHPPLG KMLVGLSGYL AGYNGSWDFP SGEVYPDYID YVKMRLFQAM
160 170 180 190 200
FSSLCVPLAY FTGRAIGFSR LSVWLFTILV IFENSYATLG KFILLDSMLL
210 220 230 240 250
FFTVSSYFCL AKFHTMRKSP FSARWWLWLC LTGLNLGCAI SVKMVGLFII
260 270 280 290 300
SVVGIYTISE LWNLLSDRSV SWKVYVNHWL ARIFGLIIIP VCVFLLCFKI
310 320 330 340 350
HFDLLSNSGP GDSTMPSLFQ ASLNGTKVGK GPRDVALGSS IISIKNQALG
360 370 380 390 400
GALLHSHVQP FPEGSEQQQV TVYGYSDANN EWFFQRIRGV EPWTDAENKT
410 420 430 440 450
IEFVKGGEMY RLMHRLTGKN LHTHEVPAPI SKSEYEVSAY GDVDLGDYKD
460 470 480 490 500
NWIIEIVEQV GEEDPTLLHP LSTSFRIKNS ILGCYLAQSG KHLPEWGFRQ
510 520 530 540 550
GEVVCLKHAS KRDKRTWWNI ETHENERLPQ GEDFVYPKTS FFRNFMQLNS
560 570 580 590 600
AMMATNNALV PNPEKFDGIA SSAWQWPTLN VGVRLCEWSE KSIKYFLLGS
610 620 630 640 650
PASVWPSSIA VCALIIHVIF LTLKWQRQCV ILSDPVERDV FVMAAFYPLL
660 670 680 690 700
AWLLHYMPFV VMSRVVYAHH YLPTLYFALM ILSYYFDMIT KRWATRNTGK
710 720 730 740 750
FLRLGAYIVY GSIVIAGFFY FSPFSFGMDG PVDDYAYLAW LPTWQIVEDI

RNT
Length:753
Mass (Da):86,323
Last modified:October 5, 2010 - v2
Checksum:iF076473B41EB6CBA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti397E → H in CAA58728 (PubMed:8585318).Curated1
Sequence conflicti567D → N in CAA58728 (PubMed:8585318).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83797 Genomic DNA. Translation: CAA58728.1.
X90565 Genomic DNA. Translation: CAA62176.1.
Z75229 Genomic DNA. Translation: CAA99641.1.
BK006948 Genomic DNA. Translation: DAA11085.1.
PIRiS58331.
RefSeqiNP_014966.1. NM_001183741.1.

Genome annotation databases

EnsemblFungiiYOR321W; YOR321W; YOR321W.
GeneIDi854499.
KEGGisce:YOR321W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83797 Genomic DNA. Translation: CAA58728.1.
X90565 Genomic DNA. Translation: CAA62176.1.
Z75229 Genomic DNA. Translation: CAA99641.1.
BK006948 Genomic DNA. Translation: DAA11085.1.
PIRiS58331.
RefSeqiNP_014966.1. NM_001183741.1.

3D structure databases

ProteinModelPortaliP47190.
SMRiP47190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34707. 23 interactors.
DIPiDIP-5158N.
IntActiP47190. 4 interactors.
MINTiMINT-574047.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBiP47190.
PRIDEiP47190.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR321W; YOR321W; YOR321W.
GeneIDi854499.
KEGGisce:YOR321W.

Organism-specific databases

EuPathDBiFungiDB:YOR321W.
SGDiS000005848. PMT3.

Phylogenomic databases

GeneTreeiENSGT00860000133869.
HOGENOMiHOG000157526.
InParanoidiP47190.
KOiK00728.
OMAiYTISELW.
OrthoDBiEOG092C0JF4.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:YOR321W-MONOMER.
BRENDAi2.4.1.109. 984.

Miscellaneous databases

PROiP47190.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39-like.
IPR003342. Glyco_trans_39/83.
IPR016093. MIR_motif.
IPR032421. PMT_4TMC.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
PF16192. PMT_4TMC. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMT3_YEAST
AccessioniPrimary (citable) accession number: P47190
Secondary accession number(s): D6W319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2720 molecules/cell in log phase SD medium.1 Publication

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.