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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

Pathway:iprotein 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

  • protein O-linked glycosylation Source: SGD
  • protein O-linked mannosylation Source: SGD
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
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR321W.
SGDiS000005848. PMT3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 5049CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei51 – 7121HelicalSequence AnalysisAdd
BLAST
Topological domaini72 – 14877LumenalSequence AnalysisAdd
BLAST
Transmembranei149 – 16921HelicalSequence AnalysisAdd
BLAST
Topological domaini170 – 1745CytoplasmicSequence Analysis
Transmembranei175 – 19521HelicalSequence AnalysisAdd
BLAST
Topological domaini196 – 23540LumenalSequence AnalysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence AnalysisAdd
BLAST
Topological domaini257 – 28226CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei283 – 30321HelicalSequence AnalysisAdd
BLAST
Topological domaini304 – 602299LumenalSequence AnalysisAdd
BLAST
Transmembranei603 – 62321HelicalSequence AnalysisAdd
BLAST
Topological domaini624 – 63916CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei640 – 66021HelicalSequence AnalysisAdd
BLAST
Topological domaini661 – 6655LumenalSequence Analysis
Transmembranei666 – 68621HelicalSequence AnalysisAdd
BLAST
Topological domaini687 – 70317CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei704 – 72421HelicalSequence AnalysisAdd
BLAST
Topological domaini725 – 75329LumenalSequence AnalysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 753752Dolichyl-phosphate-mannose--protein mannosyltransferase 3PRO_0000121493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP47190.
PaxDbiP47190.

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 interactions.
DIPiDIP-5158N.
IntActiP47190. 4 interactions.
MINTiMINT-574047.

Structurei

3D structure databases

ProteinModelPortaliP47190.
SMRiP47190. Positions 351-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini332 – 38756MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini401 – 45757MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini465 – 52359MIR 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.
InParanoidiP47190.
KOiK00728.
OMAiGNPVIFW.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971E → H in CAA58728 (PubMed:8585318).Curated
Sequence conflicti567 – 5671D → N in CAA58728 (PubMed:8585318).Curated

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. Positions 351-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBiP47190.
PaxDbiP47190.

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

eggNOGiCOG1928.
GeneTreeiENSGT00740000115531.
HOGENOMiHOG000157526.
InParanoidiP47190.
KOiK00728.
OMAiGNPVIFW.
OrthoDBiEOG7BP89X.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi976837.
PROiP47190.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Protein-O-glycosylation in yeast: protein-specific mannosyltransferases."
    Gentzsch M., Tanner W.
    Glycobiology 7:481-486(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. "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 PMT5 AND PMT1.
  7. 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. "Functional and genomic analyses of blocked protein O-mannosylation in baker's yeast."
    Arroyo J., Hutzler J., Bermejo C., Ragni E., Garcia-Cantalejo J., Botias P., Piberger H., Schott A., Sanz A.B., Strahl S.
    Mol. Microbiol. 79:1529-1546(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

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: July 22, 2015
This is version 131 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

External Data

Dasty 3

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 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.