Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P47190 (PMT3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 3

EC=2.4.1.109
Gene names
Name:PMT3
Ordered Locus Names:YOR321W
ORF Names:O6148
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins By similarity.

Catalytic activity

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753Dolichyl-phosphate-mannose--protein mannosyltransferase 3
PRO_0000121493

Regions

Topological domain1 – 5050Cytoplasmic Potential
Transmembrane51 – 7121Helical; Potential
Topological domain72 – 14877Lumenal Potential
Transmembrane149 – 16921Helical; Potential
Topological domain170 – 1745Cytoplasmic Potential
Transmembrane175 – 19521Helical; Potential
Topological domain196 – 23540Lumenal Potential
Transmembrane236 – 25621Helical; Potential
Topological domain257 – 28226Cytoplasmic Potential
Transmembrane283 – 30321Helical; Potential
Topological domain304 – 602299Lumenal Potential
Transmembrane603 – 62321Helical; Potential
Topological domain624 – 63916Cytoplasmic Potential
Transmembrane640 – 66021Helical; Potential
Topological domain661 – 6655Lumenal Potential
Transmembrane666 – 68621Helical; Potential
Topological domain687 – 70317Cytoplasmic Potential
Transmembrane704 – 72421Helical; Potential
Topological domain725 – 75329Lumenal Potential
Domain332 – 38756MIR 1
Domain401 – 45757MIR 2
Domain465 – 52359MIR 3

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3971E → H in CAA58728. Ref.1
Sequence conflict5671D → N in CAA58728. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47190 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: F076473B41EB6CBA

FASTA75386,323
        10         20         30         40         50         60 
MPYRVATGYS EKSTDDDLIW RTPIVKEELE DADNFLKDDA ELYDKVKNES AVSHLDTIVM 

        70         80         90        100        110        120 
PIIFTVLGMF TRMYKIGRNN HVVWDEAHFG KFGSYYLRHE FYHDVHPPLG KMLVGLSGYL 

       130        140        150        160        170        180 
AGYNGSWDFP SGEVYPDYID YVKMRLFQAM FSSLCVPLAY FTGRAIGFSR LSVWLFTILV 

       190        200        210        220        230        240 
IFENSYATLG KFILLDSMLL FFTVSSYFCL AKFHTMRKSP FSARWWLWLC LTGLNLGCAI 

       250        260        270        280        290        300 
SVKMVGLFII SVVGIYTISE LWNLLSDRSV SWKVYVNHWL ARIFGLIIIP VCVFLLCFKI 

       310        320        330        340        350        360 
HFDLLSNSGP GDSTMPSLFQ ASLNGTKVGK GPRDVALGSS IISIKNQALG GALLHSHVQP 

       370        380        390        400        410        420 
FPEGSEQQQV TVYGYSDANN EWFFQRIRGV EPWTDAENKT IEFVKGGEMY RLMHRLTGKN 

       430        440        450        460        470        480 
LHTHEVPAPI SKSEYEVSAY GDVDLGDYKD NWIIEIVEQV GEEDPTLLHP LSTSFRIKNS 

       490        500        510        520        530        540 
ILGCYLAQSG KHLPEWGFRQ GEVVCLKHAS KRDKRTWWNI ETHENERLPQ GEDFVYPKTS 

       550        560        570        580        590        600 
FFRNFMQLNS AMMATNNALV PNPEKFDGIA SSAWQWPTLN VGVRLCEWSE KSIKYFLLGS 

       610        620        630        640        650        660 
PASVWPSSIA VCALIIHVIF LTLKWQRQCV ILSDPVERDV FVMAAFYPLL AWLLHYMPFV 

       670        680        690        700        710        720 
VMSRVVYAHH YLPTLYFALM ILSYYFDMIT KRWATRNTGK FLRLGAYIVY GSIVIAGFFY 

       730        740        750 
FSPFSFGMDG PVDDYAYLAW LPTWQIVEDI RNT 

« Hide

References

« Hide 'large scale' references
[1]"PMT3 and PMT4, two new members of the protein-O-mannosyltransferase gene family of Saccharomyces cerevisiae."
Immervoll T., Gentzsch M., Tanner W.
Yeast 11:1345-1351(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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].
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83797 Genomic DNA. Translation: CAA58728.1.
X90565 Genomic DNA. Translation: CAA62176.1.
Z75229 Genomic DNA. Translation: CAA99641.1.
BK006948 Genomic DNA. Translation: DAA11085.1.
PIRS58331.
RefSeqNP_014966.1. NM_001183741.1.

3D structure databases

ProteinModelPortalP47190.
SMRP47190. Positions 351-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34707. 24 interactions.
DIPDIP-5158N.
IntActP47190. 4 interactions.
MINTMINT-574047.
STRING4932.YOR321W.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Proteomic databases

PaxDbP47190.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR321W; YOR321W; YOR321W.
GeneID854499.
KEGGsce:YOR321W.

Organism-specific databases

SGDS000005848. PMT3.

Phylogenomic databases

eggNOGCOG1928.
GeneTreeENSGT00740000115531.
HOGENOMHOG000157526.
KOK00728.
OMAFAAHFHI.
OrthoDBEOG7BP89X.

Enzyme and pathway databases

BioCycYEAST:YOR321W-MONOMER.
BRENDA2.4.1.109. 984.

Gene expression databases

GenevestigatorP47190.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio976837.

Entry information

Entry namePMT3_YEAST
AccessionPrimary (citable) accession number: P47190
Secondary accession number(s): D6W319
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families