Dolichyl-phosphate-mannose--protein mannosyltransferase 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P31382 (PMT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2
EC=2.4.1.109

Gene names

Name:	PMT2
Ordered Locus Names:	YAL023C
ORF Names:	FUN25

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	759 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to be active on chitinase.
Catalytic activity	Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Miscellaneous	Present with 6510 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glycosyltransferase 39 family. Contains 3 MIR domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated misfolded protein catabolic process Inferred from mutant phenotype PubMed 18182384. Source: SGD protein O-linked mannosylation Inferred from mutant phenotype PubMed 18182384 Ref.5 PubMed 8543034. Source: SGD protein exit from endoplasmic reticulum Inferred from genetic interaction PubMed 21147851. Source: SGD regulation of endoplasmic reticulum unfolded protein response Inferred from genetic interaction PubMed 21231968. Source: SGD
Cellular_component	dolichyl-phosphate-mannose-protein mannosyltransferase complex Inferred from physical interaction PubMed 12551906 PubMed 21956107 PubMed 8543034. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from direct assay PubMed 21956107. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PMT1	P33775	2	EBI-13573,EBI-13567

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 759

759

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

PRO_0000121492

Regions

Topological domain

1 – 64

Cytoplasmic Potential

Transmembrane

65 – 85

Helical; Potential

Topological domain

86 – 167

Lumenal Potential

Transmembrane

168 – 188

Helical; Potential

Topological domain

189 – 198

Cytoplasmic Potential

Transmembrane

199 – 219

Helical; Potential

Topological domain

220 – 251

Lumenal Potential

Transmembrane

252 – 272

Helical; Potential

Topological domain

273 – 289

Cytoplasmic Potential

Transmembrane

290 – 310

Helical; Potential

Topological domain

311 – 609

299

Lumenal Potential

Transmembrane

610 – 630

Helical; Potential

Topological domain

631 – 647

Cytoplasmic Potential

Transmembrane

648 – 668

Helical; Potential

Topological domain

669 – 676

Lumenal Potential

Transmembrane

677 – 697

Helical; Potential

Topological domain

698 – 710

Cytoplasmic Potential

Transmembrane

711 – 731

Helical; Potential

Topological domain

732 – 759

Lumenal Potential

Domain

339 – 394

MIR 1

Domain

407 – 463

MIR 2

Domain

471 – 529

MIR 3

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphoserine Ref.9

Glycosylation

131

N-linked (GlcNAc...) Potential

Glycosylation

155

N-linked (GlcNAc...) Potential

Glycosylation

403

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P31382 [UniParc].

Last modified June 16, 2003. Version 2.
Checksum: B1E1480C2E04BE3D
Show »

FASTA

759

86,870

        10         20         30         40         50         60 
MSSSSSTGYS KNNAAHIKQE NTLRQRESSS ISVSEELSSA DERDAEDFSK EKPAAQSSLL 

        70         80         90        100        110        120 
RLESVVMPVI FTALALFTRM YKIGINNHVV WDEAHFGKFG SYYLRHEFYH DVHPPLGKML 

       130        140        150        160        170        180 
VGLSGYLAGY NGSWDFPSGE IYPDYLDYVK MRLFNASFSA LCVPLAYFTA KAIGFSLPTV 

       190        200        210        220        230        240 
WLMTVLVLFE NSYSTLGRFI LLDSMLLFFT VASFFSFVMF HNQRSKPFSR KWWKWLLITG 

       250        260        270        280        290        300 
ISLGCTISVK MVGLFIITMV GIYTVIDLWT FLADKSMSWK TYINHWLARI FGLIIVPFCI 

       310        320        330        340        350        360 
FLLCFKIHFD LLSHSGTGDA NMPSLFQARL VGSDVGQGPR DIALGSSVVS IKNQALGGSL 

       370        380        390        400        410        420 
LHSHIQTYPD GSNQQQVTCY GYKDANNEWF FNRERGLPSW SENETDIEYL KPGTSYRLVH 

       430        440        450        460        470        480 
KSTGRNLHTH PVAAPVSKTQ WEVSGYGDNV VGDNKDNWVI EIMDQRGDED PEKLHTLTTS 

       490        500        510        520        530        540 
FRIKNLEMGC YLAQTGNSLP EWGFRQQEVV CMKNPFKRDK RTWWNIETHE NERLPPRPED 

       550        560        570        580        590        600 
FQYPKTNFLK DFIHLNLAMM ATNNALVPDP DKFDYLASSA WQWPTLNVGL RLCGWGDDNP 

       610        620        630        640        650        660 
KYFLLGTPAS TWASSVAVLA FMATVVILLI RWQRQYVDLR NPSNWNVFLM GGFYPLLAWG 

       670        680        690        700        710        720 
LHYMPFVIMS RVTYVHHYLP ALYFALIILA YCFDAGLQKW SRSKCGRIMR FVLYAGFMAL 

       730        740        750 
VIGCFWYFSP ISFGMEGPSS NFRYLNWFST WDIADKQEA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Dolinski K.J., Cherry J.M. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 137-139.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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: CHARACTERIZATION.
[6]	"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: CHARACTERIZATION.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-39, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L05146 Genomic DNA. Translation: AAC04934.2. BK006935 Genomic DNA. Translation: DAA06965.1.
PIR	S36711.
RefSeq	NP_009379.2. NM_001178168.1.
3D structure databases
ProteinModelPortal	P31382.
SMR	P31382. Positions 358-510.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6720N.
IntAct	P31382. 2 interactions.
MINT	MINT-655858.
STRING	4932.YAL023C.
Protein family/group databases
CAZy	GT39. Glycosyltransferase Family 39.
Proteomic databases
PaxDb	P31382.
PeptideAtlas	P31382.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAL023C; YAL023C; YAL023C.
GeneID	851210.
KEGG	sce:YAL023C.
Organism-specific databases
CYGD	YAL023c.
SGD	S000000021. PMT2.
Phylogenomic databases
eggNOG	COG1928.
GeneTree	ENSGT00700000104570.
HOGENOM	HOG000157526.
KO	K00728.
OMA	WPINYRG.
OrthoDB	EOG44BF9C.
Enzyme and pathway databases
BioCyc	YEAST:YAL023C-MONOMER.
BRENDA	2.4.1.109. 984.
UniPathway	UPA00378.
Gene expression databases
Genevestigator	P31382.
GermOnline	YAL023C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR027005. GlyclTrfase_39_like. IPR003342. Glyco_trans_39. IPR016093. MIR_motif. [Graphical view]
PANTHER	PTHR10050. PTHR10050. 1 hit.
Pfam	PF02815. MIR. 1 hit. PF02366. PMT. 1 hit. [Graphical view]
SMART	SM00472. MIR. 3 hits. [Graphical view]
SUPFAM	SSF82109. MIR. 1 hit.
PROSITE	PS50919. MIR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	968085.

Entry information

Entry name

PMT2_YEAST

Accession

Primary (citable) accession number: P31382
Secondary accession number(s): D6VPJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	June 16, 2003
Last modified:	May 29, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome I

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents