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Q06644

- PMT7_YEAST

UniProt

Q06644 - PMT7_YEAST

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Protein

Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7

Gene

PMT7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Probable protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.By similarity

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-29866-MONOMER.
BRENDAi2.4.1.109. 984.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7Curated (EC:2.4.1.109By similarity)
Gene namesi
Name:PMT7Imported
Ordered Locus Names:YDR307WImported
ORF Names:D9740.4Imported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR307w.
SGDiS000002715. PMT7.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2626LumenalSequence AnalysisAdd
BLAST
Transmembranei27 – 4721HelicalSequence AnalysisAdd
BLAST
Topological domaini48 – 159112CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence AnalysisAdd
BLAST
Topological domaini181 – 19515LumenalSequence AnalysisAdd
BLAST
Transmembranei196 – 21621HelicalSequence AnalysisAdd
BLAST
Topological domaini217 – 23519CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence AnalysisAdd
BLAST
Topological domaini257 – 482226LumenalSequence AnalysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence AnalysisAdd
BLAST
Topological domaini504 – 56562CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei566 – 58621HelicalSequence AnalysisAdd
BLAST
Topological domaini587 – 61731LumenalSequence AnalysisAdd
BLAST
Transmembranei618 – 63821HelicalSequence AnalysisAdd
BLAST
Topological domaini639 – 66224CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 662662Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7PRO_0000121497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ06644.
PaxDbiQ06644.
PeptideAtlasiQ06644.

Expressioni

Gene expression databases

GenevestigatoriQ06644.

Interactioni

Protein-protein interaction databases

BioGridi32360. 42 interactions.
DIPiDIP-5150N.
IntActiQ06644. 19 interactions.
MINTiMINT-521790.
STRINGi4932.YDR307W.

Structurei

3D structure databases

ProteinModelPortaliQ06644.
SMRiQ06644. Positions 289-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini289 – 34456MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini359 – 41860MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini432 – 48857MIR 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.
InParanoidiQ06644.
KOiK00728.
OMAiITRRINC.
OrthoDBiEOG7KDFKG.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PfamiPF02815. MIR. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06644-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKDLRLQGPY RKYIPYNIFQ QCGIGHLKTL DYIFAFLIVI TNFTLIWKSH
60 70 80 90 100
SSSFWNRPWD NNSEQELSQL IQFYLDKAFY IHELPPFTIQ FYSIIRRLKI
110 120 130 140 150
AENLRYVSLF LNSSTLGFLF LITRRINCSR LISATGLLIL SNWETFRNEG
160 170 180 190 200
TIISFDSLEW CLFSVVIYSF ISISIAKLGT TNWFANVITL SISLGLAISS
210 220 230 240 250
KFIGIVTWAF VILSFVRQFD RLISDVKVTT IQIIKFVILC LLFVLIIPGS
260 270 280 290 300
IFIISYSNLL SNFKTDTPQF SKYMSTYFKS YLRGPQVQPS RLYYGSTITL
310 320 330 340 350
RHLDSMVGYL ASHDISYPSD VDEQLVALSF EEFAADNEWL IEHPTLNLSF
360 370 380 390 400
SEVYHADQLI PVEFGQSIKL RHKSTGKLLR ASTAKPPISE QDYDFQISCT
410 420 430 440 450
KDSNYEGGMD ERWDVLLIKD EINNDKKDNA DDKYIKPLQS EIRFYNNGQR
460 470 480 490 500
CGLLGHDLRL PEWGRFEQEV LCMEYPVIPR TTFLIDSVQL PVDFQVPMIE
510 520 530 540 550
YYIGKISSSA EFNHTLSWSQ FLYLFKEYIF KQYKYNYYIK YGKNKVTFED
560 570 580 590 600
AFAVEKWPIT LDTDSPVWFN FAWYGSLLSM IIFMCVQCKR MISWNPWTTA
610 620 630 640 650
EPSFSIKWEV YNEFGWECIV GWFLHFYIFT MSPHFNLGKK LYFQSFFFSV
660
LCLLESLDCL AK
Length:662
Mass (Da):77,570
Last modified:November 1, 1997 - v1
Checksum:i9083D1DF765A3AE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64743.1.
BK006938 Genomic DNA. Translation: DAA12146.1.
PIRiS61193.
RefSeqiNP_010593.3. NM_001180615.3.

Genome annotation databases

EnsemblFungiiYDR307W; YDR307W; YDR307W.
GeneIDi851902.
KEGGisce:YDR307W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64743.1 .
BK006938 Genomic DNA. Translation: DAA12146.1 .
PIRi S61193.
RefSeqi NP_010593.3. NM_001180615.3.

3D structure databases

ProteinModelPortali Q06644.
SMRi Q06644. Positions 289-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32360. 42 interactions.
DIPi DIP-5150N.
IntActi Q06644. 19 interactions.
MINTi MINT-521790.
STRINGi 4932.YDR307W.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi Q06644.
PaxDbi Q06644.
PeptideAtlasi Q06644.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR307W ; YDR307W ; YDR307W .
GeneIDi 851902.
KEGGi sce:YDR307W.

Organism-specific databases

CYGDi YDR307w.
SGDi S000002715. PMT7.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000116239.
InParanoidi Q06644.
KOi K00728.
OMAi ITRRINC.
OrthoDBi EOG7KDFKG.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci YEAST:G3O-29866-MONOMER.
BRENDAi 2.4.1.109. 984.

Miscellaneous databases

NextBioi 969909.

Gene expression databases

Genevestigatori Q06644.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR016093. MIR_motif.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 1 hit.
Pfami PF02815. MIR. 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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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.

Entry informationi

Entry nameiPMT7_YEAST
AccessioniPrimary (citable) accession number: Q06644
Secondary accession number(s): D6VST6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3