Skip Header

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

P47190

- PMT3_YEAST

UniProt

P47190 - PMT3_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 3

Gene

PMT3

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 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 phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.By similarity

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. protein O-linked glycosylation Source: SGD
  2. 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: Chromosome XV

Organism-specific databases

SGDiS000005848. PMT3.

Subcellular locationi

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

GO - Cellular componenti

  1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex Source: SGD
  2. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt3p 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

Affects O-mannosylation activity only when PTM1 and PTM2 are absent.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 753753Dolichyl-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

Gene expression databases

GenevestigatoriP47190.

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. 24 interactions.
DIPiDIP-5158N.
IntActiP47190. 4 interactions.
MINTiMINT-574047.
STRINGi4932.YOR321W.

Structurei

3D structure databases

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

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5050CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini72 – 14877LumenalSequence AnalysisAdd
BLAST
Topological domaini170 – 1745CytoplasmicSequence Analysis
Topological domaini196 – 23540LumenalSequence AnalysisAdd
BLAST
Topological domaini257 – 28226CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini304 – 602299LumenalSequence AnalysisAdd
BLAST
Topological domaini624 – 63916CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini661 – 6655LumenalSequence Analysis
Topological domaini687 – 70317CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini725 – 75329LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei51 – 7121HelicalSequence AnalysisAdd
BLAST
Transmembranei149 – 16921HelicalSequence AnalysisAdd
BLAST
Transmembranei175 – 19521HelicalSequence AnalysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence AnalysisAdd
BLAST
Transmembranei283 – 30321HelicalSequence AnalysisAdd
BLAST
Transmembranei603 – 62321HelicalSequence AnalysisAdd
BLAST
Transmembranei640 – 66021HelicalSequence AnalysisAdd
BLAST
Transmembranei666 – 68621HelicalSequence AnalysisAdd
BLAST
Transmembranei704 – 72421HelicalSequence AnalysisAdd
BLAST

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.
OMAiFAAHFHI.
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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S58331.
RefSeqi NP_014966.1. NM_001183741.1.

3D structure databases

ProteinModelPortali P47190.
SMRi P47190. Positions 351-504.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34707. 24 interactions.
DIPi DIP-5158N.
IntActi P47190. 4 interactions.
MINTi MINT-574047.
STRINGi 4932.YOR321W.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi P47190.
PaxDbi P47190.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR321W ; YOR321W ; YOR321W .
GeneIDi 854499.
KEGGi sce:YOR321W.

Organism-specific databases

SGDi S000005848. PMT3.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000115531.
HOGENOMi HOG000157526.
InParanoidi P47190.
KOi K00728.
OMAi FAAHFHI.
OrthoDBi EOG7BP89X.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci YEAST:YOR321W-MONOMER.
BRENDAi 2.4.1.109. 984.

Miscellaneous databases

NextBioi 976837.

Gene expression databases

Genevestigatori P47190.

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. "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: October 29, 2014
This is version 125 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