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P32623 (CRH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. 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 CRH2

EC=3.2.-.-
Alternative name(s):
Congo red hypersensitive protein 2
Unknown transcript 2 protein
Gene names
Name:UTR2
Synonyms:CRH2
Ordered Locus Names:YEL040W
ORF Names:SYGP-ORF18
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length467 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.9

Subcellular location

Secretedcell wall. Membrane; Lipid-anchorGPI-anchor. Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP), localized particularly in chitin-rich areas. Localizes to sites of polarized growth. Found at the incipient bud site, as a ring at the bud neck as the bud grows, and in the septum at the time of cytokinesis. Redistributes uniformly over the cell cortex upon heat stress. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

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.

Sequence similarities

Belongs to the glycosyl hydrolase 16 family.

Sequence caution

The sequence AAB28444.1 differs from that shown. Reason: Frameshift at position 120.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGP1P253761EBI-2098544,EBI-2357

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 445422Probable glycosidase CRH2
PRO_0000065745
Propeptide446 – 46722Removed in mature form Potential
PRO_0000232722

Regions

Compositional bias354 – 44289Ser-rich

Sites

Active site1661Nucleophile By similarity
Active site1701Proton donor By similarity

Amino acid modifications

Lipidation4451GPI-anchor amidated asparagine Potential
Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2371N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1301L → V in AAA34941. Ref.4
Sequence conflict1301L → V in AAD13975. Ref.4
Sequence conflict1301L → V in AAB28444. Ref.4
Sequence conflict2911A → R in AAA34941. Ref.4
Sequence conflict2911A → R in AAD13975. Ref.4
Sequence conflict2911A → R in AAB28444. Ref.4
Sequence conflict3541S → C in AAA34941. Ref.4
Sequence conflict3541S → C in AAD13975. Ref.4
Sequence conflict3541S → C in AAB28444. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P32623 [UniParc].

Last modified April 18, 2006. Version 3.
Checksum: B6AE762B5489AA3A

FASTA46749,906
        10         20         30         40         50         60 
MAIVNSWLIC LVSIFSFVVR VEAATFCNAT QACPEDKPCC SQYGECGTGQ YCLNNCDVRY 

        70         80         90        100        110        120 
SFSHDSCMPV PICKSSSTKF KDYSSKLGNA NTFLGNVSEA DWLYTGDVLD YDDEESLILA 

       130        140        150        160        170        180 
MPKNSGGTVL SSTRAVWYGK VSARIKTSHL AGVVTGFILY SGAGDELDYE FVGADLETAQ 

       190        200        210        220        230        240 
TNFYWESVLN YTNSANISTT DTFENYHTYE LDWHEDYVTW SIDGVVGRTL YKNETYNATT 

       250        260        270        280        290        300 
QKYQYPQTPS KVDISIWPGG NSTNAPGTIA WSGGEINWDA SDISNPGYYY AIVNEVNITC 

       310        320        330        340        350        360 
YDPPSDTKKN GTSAYVYTSS SEFLAKDIAI TDDEVMMDSD EGSGLDPHKG ATTSSTQKSS 

       370        380        390        400        410        420 
SSTATSSSKT SSDHSSSTKK SSKTSSTASS SSSSSSSSSS SSSTATKNGD KVVSSVSSSV 

       430        440        450        460 
TSQTQTTSSV SGSASSSTSS MSGNNAGANV AANWRLTVLC VILGYVL 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"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.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry."
Melnick L., Sherman F.
J. Mol. Biol. 233:372-388(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 76-467.
Strain: B-6441.
[5]"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.
[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]"Mechanisms for targeting of the Saccharomyces cerevisiae GPI-anchored cell wall protein Crh2p to polarised growth sites."
Rodriguez-Pena J.M., Rodriguez C., Alvarez A., Nombela C., Arroyo J.
J. Cell Sci. 115:2549-2558(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[9]"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
U18779 Genomic DNA. Translation: AAB65002.1.
AY693014 Genomic DNA. Translation: AAT93033.1.
L22173 Genomic DNA. Translation: AAA34941.1. Frameshift.
S65964 Genomic DNA. Translation: AAD13975.1. Frameshift.
S66130 mRNA. Translation: AAB28444.1. Frameshift.
BK006939 Genomic DNA. Translation: DAA07613.1.
PIRS30839.
RefSeqNP_010874.3. NM_001178855.3.

3D structure databases

ProteinModelPortalP32623.
SMRP32623. Positions 132-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36689. 76 interactions.
MINTMINT-2785828.
STRING4932.YEL040W.

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.
GH16. Glycoside Hydrolase Family 16.

Proteomic databases

MaxQBP32623.
PaxDbP32623.
PeptideAtlasP32623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL040W; YEL040W; YEL040W.
GeneID856671.
KEGGsce:YEL040W.

Organism-specific databases

CYGDYEL040w.
SGDS000000766. UTR2.

Phylogenomic databases

eggNOGCOG2273.
GeneTreeENSGT00610000086657.
HOGENOMHOG000184016.
OMALGGCDIR.
OrthoDBEOG7TN02H.

Enzyme and pathway databases

BioCycYEAST:G3O-30161-MONOMER.

Gene expression databases

GenevestigatorP32623.

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

NextBio982684.

Entry information

Entry nameCRH2_YEAST
AccessionPrimary (citable) accession number: P32623
Secondary accession number(s): D3DLK9, Q6B1R6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 18, 2006
Last modified: June 11, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: 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