P53301 (CRH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	507 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.6 Ref.10
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. 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Membrane Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell wall chitin metabolic process Inferred from mutant phenotype. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype. Source: SGD
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-KW fungal-type cell wall Inferred from direct assay Ref.6Ref.8. Source: SGD incipient cellular bud site Inferred from direct assay Ref.6. Source: SGD
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro transferase activity, transferring glycosyl groups Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GET3	Q12154	1	EBI-23440,EBI-2989
PEX29	Q03370	1	EBI-23440,EBI-36170
YHR080C	P38800	1	EBI-23440,EBI-24597

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 482	460	Probable glycosidase CRH1		PRO_0000045430
	Propeptide	483 – 507	25	Removed in mature form Potential		PRO_0000045431
Regions
	Compositional bias	63 – 66	4	Poly-Ser
	Compositional bias	301 – 481	181	Ser-rich
	Compositional bias	301 – 310	10	Poly-Ser
	Compositional bias	345 – 357	13	Poly-Ser
	Compositional bias	387 – 391	5	Poly-Ser
	Compositional bias	467 – 470	4	Poly-Ser
Sites
	Active site	134	1	Nucleophile By similarity
	Active site	138	1	Proton donor By similarity
Amino acid modifications
	Lipidation	482	1	GPI-anchor amidated asparagine Potential
	Glycosylation	117	1	N-linked (GlcNAc...) Potential
	Glycosylation	177	1	N-linked (GlcNAc...) Potential
	Glycosylation	201	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P53301 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 7D7B61F57AEA942C	FASTA	507	52,758
	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

References

	« Hide 'large scale' referencesShow '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: 9133739] [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. , 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: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 9613572] [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: 10594829] [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: 10757808] [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: 11016834] [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: 15781460] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PROBABLE 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: 17617218] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION, 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: 17302808] [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.
PIR	S64507.
RefSeq	NP_011705.1. NM_001181318.1.
3D structure databases
ProteinModelPortal	P53301.
SMR	P53301. Positions 48-258.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4360N.
IntAct	P53301. 3 interactions.
MINT	MINT-475521.
STRING	P53301.
Protein family/group databases
CAZy	GH16. Glycoside Hydrolase Family 16.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR189C; YGR189C; YGR189C.
GeneID	853102.
KEGG	sce:YGR189C.
NMPDR	fig|4932.3.peg.2832.
Organism-specific databases
CYGD	YGR189c.
SGD	S000003421. CRH1.
Phylogenomic databases
eggNOG	fuNOG04197.
GeneTree	EFGT00050000000137.
OMA	AGTIEWA.
OrthoDB	EOG4VT962.
Gene expression databases
ArrayExpress	P53301.
Genevestigator	P53301.
GermOnline	YGR189C. 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.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS01034. GLYCOSYL_HYDROL_F16. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	973104.

Entry information

Entry name

CRH1_YEAST

Accession

Primary (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:	December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program