Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P31382

- PMT2_YEAST

UniProt

P31382 - PMT2_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene

PMT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 to 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

GO - Molecular functioni

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

GO - Biological processi

  1. ER-associated misfolded protein catabolic process Source: SGD
  2. protein exit from endoplasmic reticulum Source: SGD
  3. protein O-linked glycosylation Source: SGD
  4. protein O-linked mannosylation Source: SGD
  5. regulation of endoplasmic reticulum unfolded protein response Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YAL023C-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 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
ProteomesiUP000002311: Chromosome I

Organism-specific databases

CYGDiYAL023c.
SGDiS000000021. PMT2.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 6463CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei65 – 8521HelicalSequence AnalysisAdd
BLAST
Topological domaini86 – 16782LumenalSequence AnalysisAdd
BLAST
Transmembranei168 – 18821HelicalSequence AnalysisAdd
BLAST
Topological domaini189 – 19810CytoplasmicSequence Analysis
Transmembranei199 – 21921HelicalSequence AnalysisAdd
BLAST
Topological domaini220 – 25132LumenalSequence AnalysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence AnalysisAdd
BLAST
Topological domaini273 – 28917CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST
Topological domaini311 – 609299LumenalSequence AnalysisAdd
BLAST
Transmembranei610 – 63021HelicalSequence AnalysisAdd
BLAST
Topological domaini631 – 64717CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei648 – 66821HelicalSequence AnalysisAdd
BLAST
Topological domaini669 – 6768LumenalSequence Analysis
Transmembranei677 – 69721HelicalSequence AnalysisAdd
BLAST
Topological domaini698 – 71013CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei711 – 73121HelicalSequence AnalysisAdd
BLAST
Topological domaini732 – 75928LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex Source: SGD
  2. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex Source: SGD
  3. integral component of membrane Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 759758Dolichyl-phosphate-mannose--protein mannosyltransferase 2PRO_0000121492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei39 – 391Phosphoserine1 Publication
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP31382.
PaxDbiP31382.
PeptideAtlasiP31382.

Expressioni

Gene expression databases

GenevestigatoriP31382.

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 interactions.
DIPiDIP-6720N.
IntActiP31382. 3 interactions.
MINTiMINT-655858.
STRINGi4932.YAL023C.

Structurei

3D structure databases

ProteinModelPortaliP31382.
SMRiP31382. Positions 358-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini339 – 39456MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini407 – 46357MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini471 – 52959MIR 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.
GeneTreeiENSGT00740000115531.
HOGENOMiHOG000157526.
InParanoidiP31382.
KOiK00728.
OMAiWLCISRF.
OrthoDBiEOG7BP89X.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 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.

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 .
PIRi S36711.
RefSeqi NP_009379.2. NM_001178168.1.

3D structure databases

ProteinModelPortali P31382.
SMRi P31382. Positions 358-510.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31743. 170 interactions.
DIPi DIP-6720N.
IntActi P31382. 3 interactions.
MINTi MINT-655858.
STRINGi 4932.YAL023C.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi P31382.
PaxDbi P31382.
PeptideAtlasi P31382.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YAL023C ; YAL023C ; YAL023C .
GeneIDi 851210.
KEGGi sce:YAL023C.

Organism-specific databases

CYGDi YAL023c.
SGDi S000000021. PMT2.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000115531.
HOGENOMi HOG000157526.
InParanoidi P31382.
KOi K00728.
OMAi WLCISRF.
OrthoDBi EOG7BP89X.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci YEAST:YAL023C-MONOMER.
BRENDAi 2.4.1.109. 984.

Miscellaneous databases

NextBioi 968085.

Gene expression databases

Genevestigatori P31382.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 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. "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
    Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
    Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Dolinski K.J., Cherry J.M.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 137-139.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer."
    Gentzsch M., Immervoll T., Tanner W.
    FEBS Lett. 377:128-130(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INTERACTION WITH PMT1.
  6. "Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity."
    Lussier M., Gentzsch M., Sdicu A.-M., Bussey H., Tanner W.
    J. Biol. Chem. 270:2770-2775(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, DISRUPTION PHENOTYPE.
  7. "The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital."
    Gaentzsch M., Tanner W.
    EMBO J. 15:5752-5759(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "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 PMT1 AND PMT5.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast."
    Nakatsukasa K., Okada S., Umebayashi K., Fukuda R., Nishikawa S., Endo T.
    J. Biol. Chem. 279:49762-49772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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.
  12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae."
    Hirayama H., Fujita M., Yoko-o T., Jigami Y.
    J. Biochem. 143:555-567(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-38 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Protein O-mannosyltransferases participate in ER protein quality control."
    Goder V., Melero A.
    J. Cell Sci. 124:144-153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE PMT1-PMT2 COMPLEX, INTERACTION WITH PMT2; EMP24; ERV25; ERP1; ERP2; CDC48; HRD1; USA1; YOS9; ERO1; PDI1; UBR1; CUE4; DFM1 AND TED1.
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

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 26, 2014
This is version 144 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

External Data

Dasty 3