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P53301 (CRH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable glycosidase CRH1

EC=3.2.-.-
Alternative name(s):
Congo red hypersensitive protein 1
Gene names
Name:CRH1
Ordered Locus Names:YGR189C
ORF Names:G7553
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable glycosidase that plays a role in cell wall architecture. Required for the transfer of chitin to 1,6-beta-glucan in the cell wall. Ref.6 Ref.10

Subcellular location

Secretedcell wall. Membrane; Lipid-anchorGPI-anchor. Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP), localized particularly in chitin-rich areas. Found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Redistributes uniformly over the cell cortex upon heat stress. Ref.4 Ref.6 Ref.7 Ref.8 Ref.10

Induction

Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. Induced by heat stress. Ref.5 Ref.7 Ref.10

Post-translational modification

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.

Miscellaneous

Present with 44000 wall-bound molecules/cell in log phase YPD medium. Ref.9

Sequence similarities

Belongs to the glycosyl hydrolase 16 family. CRH1 subfamily.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 482460Probable glycosidase CRH1
PRO_0000045430
Propeptide483 – 50725Removed in mature form Potential
PRO_0000045431

Regions

Compositional bias63 – 664Poly-Ser
Compositional bias301 – 481181Ser-rich
Compositional bias301 – 31010Poly-Ser
Compositional bias345 – 35713Poly-Ser
Compositional bias387 – 3915Poly-Ser
Compositional bias467 – 4704Poly-Ser

Sites

Active site1341Nucleophile By similarity
Active site1381Proton donor By similarity

Amino acid modifications

Lipidation4821GPI-anchor amidated asparagine Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P53301 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 7D7B61F57AEA942C

FASTA50752,758
        10         20         30         40         50         60 
MKVLDLLTVL SASSLLSTFA AAESTATADS TTAASSTASC NPLKTTGCTP DTALATSFSE 

        70         80         90        100        110        120 
DFSSSSKWFT DLKHAGEIKY GSDGLSMTLA KRYDNPSLKS NFYIMYGKLE VILKAANGTG 

       130        140        150        160        170        180 
IVSSFYLQSD DLDEIDIEWV GGDNTQFQSN FFSKGDTTTY DRGEFHGVDT PTDKFHNYTL 

       190        200        210        220        230        240 
DWAMDKTTWY LDGESVRVLS NTSSEGYPQS PMYLMMGIWA GGDPDNAAGT IEWAGGETNY 

       250        260        270        280        290        300 
NDAPFTMYIE KVIVTDYSTG KKYTYGDQSG SWESIEADGG SIYGRYDQAQ EDFAVLANGG 

       310        320        330        340        350        360 
SISSSSTSSS TVSSSASSTV SSSVSSTVSS SASSTVSSSV SSTVSSSSSV SSSSSTSPSS 

       370        380        390        400        410        420 
STATSSKTLA SSSVTTSSSI SSFEKQSSSS SKKTVASSST SESIISSTKT PATVSSTTRS 

       430        440        450        460        470        480 
TVAPTTQQSS VSSDSPVQDK GGVATSSNDV TSSTTQISSK YTSTIQSSSS EASSTNSVQI 

       490        500 
SNGADLAQSL PREGKLFSVL VALLALL 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII."
Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M., Nombela C.
Yeast 13:357-363(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae."
Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.
Mol. Gen. Genet. 258:53-59(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Genome-wide analysis of gene expression regulated by the yeast cell wall integrity signalling pathway."
Jung U.S., Levin D.E.
Mol. Microbiol. 34:1049-1057(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"A novel family of cell wall-related proteins regulated differently during the yeast life cycle."
Rodriguez-Pena J.M., Cid V.J., Arroyo J., Nombela C.
Mol. Cell. Biol. 20:3245-3255(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-attached proteins in response to cell wall damage caused by disruption of FKS1 in Saccharomyces cerevisiae."
Terashima H., Yabuki N., Arisawa M., Hamada K., Kitada K.
Mol. Gen. Genet. 264:64-74(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION.
[8]"Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages."
Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M., de Koster C.G.
J. Biol. Chem. 280:20894-20901(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GPI-ANCHOR.
[9]"Mass spectrometric quantitation of covalently bound cell wall proteins in Saccharomyces cerevisiae."
Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.
FEMS Yeast Res. 7:887-896(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Crh1p and Crh2p are required for the cross-linking of chitin to beta(1-6)glucan in the Saccharomyces cerevisiae cell wall."
Cabib E., Blanco N., Grau C., Rodriguez-Pena J.M., Arroyo J.
Mol. Microbiol. 63:921-935(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z72974 Genomic DNA. Translation: CAA97215.1.
X99074 Genomic DNA. Translation: CAA67525.1.
BK006941 Genomic DNA. Translation: DAA08283.1.
PIRS64507.
RefSeqNP_011705.1. NM_001181318.1.

3D structure databases

ProteinModelPortalP53301.
SMRP53301. Positions 57-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33442. 12 interactions.
DIPDIP-4360N.
IntActP53301. 1 interaction.
MINTMINT-475521.
STRING4932.YGR189C.

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Proteomic databases

MaxQBP53301.
PaxDbP53301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR189C; YGR189C; YGR189C.
GeneID853102.
KEGGsce:YGR189C.

Organism-specific databases

CYGDYGR189c.
SGDS000003421. CRH1.

Phylogenomic databases

eggNOGCOG2273.
GeneTreeENSGT00610000086657.
HOGENOMHOG000196187.
OMALENFHTY.
OrthoDBEOG7RNK9W.

Enzyme and pathway databases

BioCycYEAST:G3O-30879-MONOMER.

Gene expression databases

GenevestigatorP53301.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR017168. Glyco_hydro_16_CRH1_prd.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PIRSFPIRSF037299. Glycosidase_CRH1_prd. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Other

NextBio973104.

Entry information

Entry nameCRH1_YEAST
AccessionPrimary (citable) accession number: P53301
Secondary accession number(s): D6VUX2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries