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Protein

Cell wall protein PIR5

Gene

PIR5

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

Functioni

Component of the outer cell wall layer (By similarity). May be involved in meiosis and sporulation.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei62 – 632Cleavage; by KEX2Sequence Analysis
Sitei72 – 721Covalent attachment to cell wall glycanBy similarity
Sitei91 – 911Covalent attachment to cell wall glycanBy similarity
Sitei114 – 1141Covalent attachment to cell wall glycanBy similarity
Sitei154 – 1541Covalent attachment to cell wall glycanBy similarity

GO - Molecular functioni

  1. structural constituent of cell wall Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-31600-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell wall protein PIR5
Alternative name(s):
Protein with internal repeats 5
Gene namesi
Name:PIR5
Ordered Locus Names:YJL160C
ORF Names:J0555
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJL160c.
SGDiS000003696. YJL160C.

Subcellular locationi

Secretedcell wall By similarity
Note: Covalently attached to the cell wall.By similarity

GO - Cellular componenti

  1. cell wall Source: UniProtKB-SubCell
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 6241By similarityPRO_0000377623Add
BLAST
Chaini63 – 287225Cell wall protein PIR5PRO_0000014333Add
BLAST

Post-translational modificationi

Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from specific glutamines within the PIR1/2/3 repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.By similarity

Keywords - PTMi

Cleavage on pair of basic residues

Proteomic databases

PaxDbiP46999.

Miscellaneous databases

PMAP-CutDBP46999.

Expressioni

Inductioni

Cell cycle-regulated. Expression peaks during mitosis.1 Publication

Gene expression databases

GenevestigatoriP46999.

Interactioni

Protein-protein interaction databases

BioGridi33600. 106 interactions.
DIPiDIP-1909N.
IntActiP46999. 2 interactions.
MINTiMINT-395257.
STRINGi4932.YJL160C.

Structurei

3D structure databases

ProteinModelPortaliP46999.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati62 – 8019PIR1/2/3 1Add
BLAST
Repeati81 – 9919PIR1/2/3 2Add
BLAST
Repeati104 – 12219PIR1/2/3 3Add
BLAST
Repeati144 – 16219PIR1/2/3 4Add
BLAST

Domaini

The PIR1/2/3 repeats are required for the covalent linkage to the cell wall (By similarity). Their number varies among different strains of S.cerevisiae.By similarity

Sequence similaritiesi

Belongs to the PIR protein family.Curated
Contains 4 PIR1/2/3 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG38801.
GeneTreeiENSGT00390000008137.
HOGENOMiHOG000248193.
InParanoidiP46999.
OrthoDBiEOG7FNCJZ.

Family and domain databases

InterProiIPR000420. Yeast_PIR.
[Graphical view]
PfamiPF00399. PIR. 4 hits.
[Graphical view]
PROSITEiPS00929. PIR_REPEAT_1. 4 hits.
PS50256. PIR_REPEAT_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHYKKAFLAS LLSSIALTAY APPEPWATLT PSSKMDGGTT EYRTSFGLAV
60 70 80 90 100
IPFTVTESKV KRNVISQIND GQVQVTTQKL PHPVSQIGDG QIQVTTQKVP
110 120 130 140 150
PVVSHIVSQI GDGQLQITTA KNVVTKSTIA VPSKTVTATA TSTATAVSQI
160 170 180 190 200
HDGQVQVTIS SASSSSVLSK SKLEPTKKPN NEKVIKVQAC KSSGTLAITL
210 220 230 240 250
QGGVLIDSSG RIGSIVANRQ FQFDGPPPQA GAIYAGGWSI TKHGTLAIGD
260 270 280
NDVFYQCLSG TFYNLYDQSI GGQCNPVHLQ TVGLVDC
Length:287
Mass (Da):30,215
Last modified:May 16, 2006 - v2
Checksum:i3E02845EA0DD7F33
GO

Sequence cautioni

The sequence CAA89455.1 differs from that shown. Reason: Frameshift at position 174. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49435 Genomic DNA. Translation: CAA89455.1. Frameshift.
AY260893 Genomic DNA. Translation: AAP21761.1.
BK006943 Genomic DNA. Translation: DAA08643.1.
PIRiS56943.
RefSeqiNP_012375.2. NM_001181593.1.

Genome annotation databases

EnsemblFungiiYJL160C; YJL160C; YJL160C.
GeneIDi853280.
KEGGisce:YJL160C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49435 Genomic DNA. Translation: CAA89455.1. Frameshift.
AY260893 Genomic DNA. Translation: AAP21761.1.
BK006943 Genomic DNA. Translation: DAA08643.1.
PIRiS56943.
RefSeqiNP_012375.2. NM_001181593.1.

3D structure databases

ProteinModelPortaliP46999.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33600. 106 interactions.
DIPiDIP-1909N.
IntActiP46999. 2 interactions.
MINTiMINT-395257.
STRINGi4932.YJL160C.

Proteomic databases

PaxDbiP46999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL160C; YJL160C; YJL160C.
GeneIDi853280.
KEGGisce:YJL160C.

Organism-specific databases

CYGDiYJL160c.
SGDiS000003696. YJL160C.

Phylogenomic databases

eggNOGiNOG38801.
GeneTreeiENSGT00390000008137.
HOGENOMiHOG000248193.
InParanoidiP46999.
OrthoDBiEOG7FNCJZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31600-MONOMER.

Miscellaneous databases

NextBioi973570.
PMAP-CutDBP46999.

Gene expression databases

GenevestigatoriP46999.

Family and domain databases

InterProiIPR000420. Yeast_PIR.
[Graphical view]
PfamiPF00399. PIR. 4 hits.
[Graphical view]
PROSITEiPS00929. PIR_REPEAT_1. 4 hits.
PS50256. PIR_REPEAT_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
    Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
    Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-223.
    Strain: ATCC 204511 / S288c / AB972.
  4. "Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae."
    Enyenihi A.H., Saunders W.S.
    Genetics 163:47-54(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FRAMESHIFT.
  6. Cited for: INDUCTION.

Entry informationi

Entry nameiPIR5_YEAST
AccessioniPrimary (citable) accession number: P46999
Secondary accession number(s): D6VW27, Q86ZS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 16, 2006
Last modified: January 7, 2015
This is version 90 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.