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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene

PMT2

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 PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.4 Publications

Catalytic activityi

Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.1 Publication

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

  • ER-associated misfolded protein catabolic process Source: SGD
  • fungal-type cell wall organization Source: GO_Central
  • protein exit from endoplasmic reticulum Source: SGD
  • protein O-linked glycosylation Source: SGD
  • protein O-linked mannosylation Source: SGD
  • regulation of endoplasmic reticulum unfolded protein response Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YAL023C-MONOMER.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2Curated (EC:2.4.1.1091 Publication)
Gene namesi
Name:PMT21 Publication
Synonyms:FUN251 Publication
Ordered Locus Names:YAL023CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL023C.
SGDiS000000021. PMT2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 64CytoplasmicSequence analysisAdd BLAST63
Transmembranei65 – 85HelicalSequence analysisAdd BLAST21
Topological domaini86 – 167LumenalSequence analysisAdd BLAST82
Transmembranei168 – 188HelicalSequence analysisAdd BLAST21
Topological domaini189 – 198CytoplasmicSequence analysis10
Transmembranei199 – 219HelicalSequence analysisAdd BLAST21
Topological domaini220 – 251LumenalSequence analysisAdd BLAST32
Transmembranei252 – 272HelicalSequence analysisAdd BLAST21
Topological domaini273 – 289CytoplasmicSequence analysisAdd BLAST17
Transmembranei290 – 310HelicalSequence analysisAdd BLAST21
Topological domaini311 – 609LumenalSequence analysisAdd BLAST299
Transmembranei610 – 630HelicalSequence analysisAdd BLAST21
Topological domaini631 – 647CytoplasmicSequence analysisAdd BLAST17
Transmembranei648 – 668HelicalSequence analysisAdd BLAST21
Topological domaini669 – 676LumenalSequence analysis8
Transmembranei677 – 697HelicalSequence analysisAdd BLAST21
Topological domaini698 – 710CytoplasmicSequence analysisAdd BLAST13
Transmembranei711 – 731HelicalSequence analysisAdd BLAST21
Topological domaini732 – 759LumenalSequence analysisAdd BLAST28

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to diminished in vitro and in vivo O-mannosylation activity.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001214922 – 759Dolichyl-phosphate-mannose--protein mannosyltransferase 2Add BLAST758

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei32PhosphoserineCombined sources1
Modified residuei38PhosphoserineCombined sources1
Modified residuei39PhosphoserineCombined sources1
Glycosylationi131N-linked (GlcNAc...)Sequence analysis1
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi403N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP31382.
PRIDEiP31382.

PTM databases

iPTMnetiP31382.

Interactioni

Subunit structurei

PMT1 and PMT2 form a functional heterodimer. The complex interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1. Forms also a minor complex with PMT5.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PMT1P337754EBI-13573,EBI-13567
PMT5P528672EBI-13573,EBI-13591

Protein-protein interaction databases

BioGridi31743. 170 interactors.
DIPiDIP-6720N.
IntActiP31382. 3 interactors.
MINTiMINT-655858.

Structurei

3D structure databases

ProteinModelPortaliP31382.
SMRiP31382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini339 – 394MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini407 – 463MIR 2PROSITE-ProRule annotationAdd BLAST57
Domaini471 – 529MIR 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.
InParanoidiP31382.
KOiK00728.
OMAiTIEDLWE.
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.

P31382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSSSTGYS KNNAAHIKQE NTLRQRESSS ISVSEELSSA DERDAEDFSK
60 70 80 90 100
EKPAAQSSLL RLESVVMPVI FTALALFTRM YKIGINNHVV WDEAHFGKFG
110 120 130 140 150
SYYLRHEFYH DVHPPLGKML VGLSGYLAGY NGSWDFPSGE IYPDYLDYVK
160 170 180 190 200
MRLFNASFSA LCVPLAYFTA KAIGFSLPTV WLMTVLVLFE NSYSTLGRFI
210 220 230 240 250
LLDSMLLFFT VASFFSFVMF HNQRSKPFSR KWWKWLLITG ISLGCTISVK
260 270 280 290 300
MVGLFIITMV GIYTVIDLWT FLADKSMSWK TYINHWLARI FGLIIVPFCI
310 320 330 340 350
FLLCFKIHFD LLSHSGTGDA NMPSLFQARL VGSDVGQGPR DIALGSSVVS
360 370 380 390 400
IKNQALGGSL LHSHIQTYPD GSNQQQVTCY GYKDANNEWF FNRERGLPSW
410 420 430 440 450
SENETDIEYL KPGTSYRLVH KSTGRNLHTH PVAAPVSKTQ WEVSGYGDNV
460 470 480 490 500
VGDNKDNWVI EIMDQRGDED PEKLHTLTTS FRIKNLEMGC YLAQTGNSLP
510 520 530 540 550
EWGFRQQEVV CMKNPFKRDK RTWWNIETHE NERLPPRPED FQYPKTNFLK
560 570 580 590 600
DFIHLNLAMM ATNNALVPDP DKFDYLASSA WQWPTLNVGL RLCGWGDDNP
610 620 630 640 650
KYFLLGTPAS TWASSVAVLA FMATVVILLI RWQRQYVDLR NPSNWNVFLM
660 670 680 690 700
GGFYPLLAWG LHYMPFVIMS RVTYVHHYLP ALYFALIILA YCFDAGLQKW
710 720 730 740 750
SRSKCGRIMR FVLYAGFMAL VIGCFWYFSP ISFGMEGPSS NFRYLNWFST

WDIADKQEA
Length:759
Mass (Da):86,870
Last modified:June 16, 2003 - v2
Checksum:iB1E1480C2E04BE3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA. Translation: AAC04934.2.
BK006935 Genomic DNA. Translation: DAA06965.1.
PIRiS36711.
RefSeqiNP_009379.2. NM_001178168.1.

Genome annotation databases

EnsemblFungiiYAL023C; YAL023C; YAL023C.
GeneIDi851210.
KEGGisce:YAL023C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA. Translation: AAC04934.2.
BK006935 Genomic DNA. Translation: DAA06965.1.
PIRiS36711.
RefSeqiNP_009379.2. NM_001178168.1.

3D structure databases

ProteinModelPortaliP31382.
SMRiP31382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31743. 170 interactors.
DIPiDIP-6720N.
IntActiP31382. 3 interactors.
MINTiMINT-655858.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

PTM databases

iPTMnetiP31382.

Proteomic databases

MaxQBiP31382.
PRIDEiP31382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL023C; YAL023C; YAL023C.
GeneIDi851210.
KEGGisce:YAL023C.

Organism-specific databases

EuPathDBiFungiDB:YAL023C.
SGDiS000000021. PMT2.

Phylogenomic databases

GeneTreeiENSGT00860000133869.
HOGENOMiHOG000157526.
InParanoidiP31382.
KOiK00728.
OMAiTIEDLWE.
OrthoDBiEOG092C0JF4.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:YAL023C-MONOMER.

Miscellaneous databases

PROiP31382.

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 nameiPMT2_YEAST
AccessioniPrimary (citable) accession number: P31382
Secondary accession number(s): D6VPJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 16, 2003
Last modified: November 30, 2016
This is version 163 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 6510 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 I
    Yeast (Saccharomyces cerevisiae) chromosome I: 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.