Reviewed, UniProtKB/Swiss-Prot P32623 (CRH2_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.5 Ref.8
Subcellular location	Secreted › cell wall. Membrane; Lipid-anchor › GPI-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.8 Ref.4 Ref.6 Ref.7
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 of 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Membrane Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall chitin metabolic process Inferred from genetic interaction. Source: SGD fungal-type cell wall organization Inferred from genetic interaction. Source: SGD
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cellular bud neck septin ring Ref.6 Inferred from direct assay. Source: SGD extracellular region Inferred from electronic annotation. Source: UniProtKB-KW fungal-type cell wall Ref.7 Inferred from direct assay. Source: SGD membrane fraction Inferred from direct assay. Source: SGD
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct transferase activity, transferring glycosyl groups Inferred from genetic interaction. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGP1	P25376	1	EBI-2098544,EBI-2357

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 445	422	Probable glycosidase CRH2		PRO_0000065745
	Propeptide	446 – 467	22	Removed in mature form Potential		PRO_0000232722
Regions
	Compositional bias	354 – 442	89	Ser-rich
Sites
	Active site	166	1	Nucleophile By similarity
	Active site	170	1	Proton donor By similarity
Amino acid modifications
	Lipidation	445	1	GPI-anchor amidated asparagine Potential
	Glycosylation	28	1	N-linked (GlcNAc...) Potential
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Glycosylation	196	1	N-linked (GlcNAc...) Potential
	Glycosylation	233	1	N-linked (GlcNAc...) Potential
	Glycosylation	237	1	N-linked (GlcNAc...) Potential
	Glycosylation	261	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	130	1	L → V in AAA34941. Ref.3
	Sequence conflict	130	1	L → V in AAD13975. Ref.3
	Sequence conflict	130	1	L → V in AAB28444. Ref.3
	Sequence conflict	291	1	A → R in AAA34941. Ref.3
	Sequence conflict	291	1	A → R in AAD13975. Ref.3
	Sequence conflict	291	1	A → R in AAB28444. Ref.3
	Sequence conflict	354	1	S → C in AAA34941. Ref.3
	Sequence conflict	354	1	S → C in AAD13975. Ref.3
	Sequence conflict	354	1	S → C in AAB28444. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P32623-1 [UniParc]. Last modified April 18, 2006. Version 3. Checksum: B6AE762B5489AA3A	FASTA	467	49,906
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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: 8411151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 76-467. Strain: B-6441.
[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: 9613572] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"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: 10757808] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"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: 12045225] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"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: 15781460] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"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: 17302808] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	S30839.
RefSeq	NP_010874.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P32623. 1 interaction.
STRING	P32623.
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH16. Glycoside Hydrolase Family 16.
Proteomic databases
PeptideAtlas	P32623.
Genome annotation databases
Ensembl	YEL040W; YEL040W; YEL040W; Saccharomyces cerevisiae. [Genome view]
GeneID	856671.
KEGG	sce:YEL040W.
NMPDR	fig|4932.3.peg.1925.
Organism-specific databases
CYGD	YEL040w.
SGD	S000000766. UTR2.
Phylogenomic databases
HOGENOM	P32623.
OMA	VVTAFIL
OrthoDB	EOG94TQR6
Gene expression databases
ArrayExpress	P32623.
Genevestigator	P32623.
GermOnline	YEL040W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. IPR000757. Glyco_hydro_16. IPR017168. Glyco_hydro_16_CRH1_prd. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
Pfam	PF00722. Glyco_hydro_16. 1 hit. [Graphical view]
PIRSF	PIRSF037299. Glycosidase_CRH1_prd. 1 hit.
PROSITE	PS01034. GLYCOSYL_HYDROL_F16. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982684.

Entry information

Entry name

CRH2_YEAST

Accession

Primary (citable) accession number: P32623
Secondary accession number(s): Q6B1R6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	April 18, 2006
Last modified:	November 24, 2009
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)