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P46971

- PMT4_YEAST

UniProt

P46971 - PMT4_YEAST

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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 4

Gene

PMT4

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 homodimeric complex to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Specifically acts on secretory proteins with an ER-luminally oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1, AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176.4 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
  2. identical protein binding Source: IntAct

GO - Biological processi

  1. protein O-linked glycosylation Source: SGD
  2. protein O-linked mannosylation Source: SGD
  3. regulation of endoplasmic reticulum unfolded protein response Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YJR143C-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 4 (EC:2.4.1.1091 Publication)
Gene namesi
Name:PMT41 Publication
Ordered Locus Names:YJR143CImported
ORF Names:J2176
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR143c.
SGDiS000003904. PMT4.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5353LumenalSequence AnalysisAdd
BLAST
Transmembranei54 – 7421HelicalSequence AnalysisAdd
BLAST
Topological domaini75 – 13662CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Topological domaini158 – 1669LumenalSequence Analysis
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST
Topological domaini188 – 1892CytoplasmicSequence Analysis
Transmembranei190 – 21021HelicalSequence AnalysisAdd
BLAST
Topological domaini211 – 2177LumenalSequence Analysis
Transmembranei218 – 23821HelicalSequence AnalysisAdd
BLAST
Topological domaini239 – 2424CytoplasmicSequence Analysis
Transmembranei243 – 26321HelicalSequence AnalysisAdd
BLAST
Topological domaini264 – 28320LumenalSequence AnalysisAdd
BLAST
Transmembranei284 – 30421HelicalSequence AnalysisAdd
BLAST
Topological domaini305 – 593289CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei594 – 61421HelicalSequence AnalysisAdd
BLAST
Topological domaini615 – 63521LumenalSequence AnalysisAdd
BLAST
Transmembranei636 – 65621HelicalSequence AnalysisAdd
BLAST
Topological domaini657 – 71660CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei717 – 73721HelicalSequence AnalysisAdd
BLAST
Topological domaini738 – 76225LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to diminished MID2 O-mannosylation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 762762Dolichyl-phosphate-mannose--protein mannosyltransferase 4PRO_0000121494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP46971.
PaxDbiP46971.
PeptideAtlasiP46971.

Expressioni

Gene expression databases

GenevestigatoriP46971.

Interactioni

Subunit structurei

Forms a functional homodimer and may form a heterodimer with PMT6. Interacts with RCR1.2 Publications1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-13585,EBI-13585

Protein-protein interaction databases

BioGridi33899. 70 interactions.
DIPiDIP-2549N.
IntActiP46971. 5 interactions.
MINTiMINT-425890.
STRINGi4932.YJR143C.

Structurei

3D structure databases

ProteinModelPortaliP46971.
SMRiP46971. Positions 330-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini331 – 39161MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 45860MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini464 – 52158MIR 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.
GeneTreeiENSGT00740000116239.
HOGENOMiHOG000157526.
InParanoidiP46971.
KOiK00728.
OMAiYLERSYF.
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.

P46971-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVPKKRNHG KLPPSTKDVD DPSLKYTKAA PKCEQVAEHW LLQPLPEPES
60 70 80 90 100
RYSFWVTIVT LLAFAARFYK IWYPKEVVFD EVHFGKFASY YLERSYFFDV
110 120 130 140 150
HPPFAKMMIA FIGWLCGYDG SFKFDEIGYS YETHPAPYIA YRSFNAILGT
160 170 180 190 200
LTVPIMFNTL KELNFRAITC AFASLLVAID TAHVTETRLI LLDAILIISI
210 220 230 240 250
AATMYCYVRF YKCQLRQPFT WSWYIWLHAT GLSLSFVIST KYVGVMTYSA
260 270 280 290 300
IGFAAVVNLW QLLDIKAGLS LRQFMRHFSK RLNGLVLIPF VIYLFWFWVH
310 320 330 340 350
FTVLNTSGPG DAFMSAEFQE TLKDSPLSVD SKTVNYFDII TIKHQDTDAF
360 370 380 390 400
LHSHLARYPQ RYEDGRISSA GQQVTGYTHP DFNNQWEVLP PHGSDVGKGQ
410 420 430 440 450
AVLLNQHIRL RHVATDTYLL AHDVASPFYP TNEEITTVTL EEGDGELYPE
460 470 480 490 500
TLFAFQPLKK SDEGHVLKSK TVSFRLFHVD TSVALWTHND ELLPDWGFQQ
510 520 530 540 550
QEINGNKKVI DPSNNWVVDE IVNLDEVRKV YIPKVVKPLP FLKKWIETQK
560 570 580 590 600
SMFEHNNKLS SEHPFASEPY SWPGSLSGVS FWTNGDEKKQ IYFIGNIIGW
610 620 630 640 650
WFQVISLAVF VGIIVADLIT RHRGYYALNK MTREKLYGPL MFFFVSWCCH
660 670 680 690 700
YFPFFLMARQ KFLHHYLPAH LIACLFSGAL WEVIFSDCKS LDLEKDEDIS
710 720 730 740 750
GASYERNPKV YVKPYTVFLV CVSCAVAWFF VYFSPLVYGD VSLSPSEVVS
760
REWFDIELNF SK
Length:762
Mass (Da):87,966
Last modified:November 1, 1995 - v1
Checksum:i0FBBEB283BBC0CBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83798 Genomic DNA. Translation: CAA58729.1.
Z49643 Genomic DNA. Translation: CAA89676.1.
BK006943 Genomic DNA. Translation: DAA08928.1.
PIRiS60415.
RefSeqiNP_012677.1. NM_001181801.1.

Genome annotation databases

EnsemblFungiiYJR143C; YJR143C; YJR143C.
GeneIDi853608.
KEGGisce:YJR143C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83798 Genomic DNA. Translation: CAA58729.1 .
Z49643 Genomic DNA. Translation: CAA89676.1 .
BK006943 Genomic DNA. Translation: DAA08928.1 .
PIRi S60415.
RefSeqi NP_012677.1. NM_001181801.1.

3D structure databases

ProteinModelPortali P46971.
SMRi P46971. Positions 330-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33899. 70 interactions.
DIPi DIP-2549N.
IntActi P46971. 5 interactions.
MINTi MINT-425890.
STRINGi 4932.YJR143C.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi P46971.
PaxDbi P46971.
PeptideAtlasi P46971.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR143C ; YJR143C ; YJR143C .
GeneIDi 853608.
KEGGi sce:YJR143C.

Organism-specific databases

CYGDi YJR143c.
SGDi S000003904. PMT4.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000116239.
HOGENOMi HOG000157526.
InParanoidi P46971.
KOi K00728.
OMAi YLERSYF.
OrthoDBi EOG7BP89X.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci YEAST:YJR143C-MONOMER.
BRENDAi 2.4.1.109. 984.

Miscellaneous databases

NextBioi 974448.

Gene expression databases

Genevestigatori P46971.

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. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  5. "Protein-O-glycosylation in yeast: protein-specific mannosyltransferases."
    Gentzsch M., Tanner W.
    Glycobiology 7:481-486(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. "O-glycosylation of Axl2/Bud10p by Pmt4p is required for its stability, localization, and function in daughter cells."
    Sanders S.L., Gentzsch M., Tanner W., Herskowitz I.
    J. Cell Biol. 145:1177-1188(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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: SUBUNIT.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "O-glycosylation as a sorting determinant for cell surface delivery in yeast."
    Proszynski T.J., Simons K., Bagnat M.
    Mol. Biol. Cell 15:1533-1543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Aberrant processing of the WSC family and Mid2p cell surface sensors results in cell death of Saccharomyces cerevisiae O-mannosylation mutants."
    Lommel M., Bagnat M., Strahl S.
    Mol. Cell. Biol. 24:46-57(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  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. "Membrane association is a determinant for substrate recognition by PMT4 protein O-mannosyltransferases."
    Hutzler J., Schmid M., Bernard T., Henrissat B., Strahl S.
    Proc. Natl. Acad. Sci. U.S.A. 104:7827-7832(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  13. "Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5."
    Imai K., Noda Y., Adachi H., Yoda K.
    Biosci. Biotechnol. Biochem. 71:249-252(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RCR1.

Entry informationi

Entry nameiPMT4_YEAST
AccessioniPrimary (citable) accession number: P46971
Secondary accession number(s): D6VWW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1270 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3