CRH1 (Congo Red Hypersensitive protein 1) encodes a GPI-anchored cell wall transglycosylase of the GH16 family that cross-links chitin to both beta(1-3)- and beta(1-6)-glucan in the S. cerevisiae cell wall. The enzyme uses a retaining double-displacement mechanism: it cleaves a chitin donor chain and transfers it to glucan acceptors, thereby integrating chitin into the glucan network. CRH1 has a secondary weak endochitinase activity (EC 3.2.1.14) but its primary biological role is as a chitin transglycosylase (EC 2.4.-.-). The protein is GPI-anchored at the cell surface and concentrated at chitin-rich areas including the incipient bud site, septum, and bud scars. CRH1 acts redundantly with its paralog CRH2/UTR2; the double mutant completely lacks chitin-glucan cross-links and shows strong sensitivity to Congo Red and Calcofluor White. CRH1 expression is cell-cycle regulated, induced during sporulation, and upregulated by the cell wall integrity pathway (MPK1/RLM1) in response to heat stress and cell wall damage. Present at approximately 44,000 wall-bound copies per cell in log phase.
Definition: Catalysis of the retaining transfer of a chitin oligosaccharide from a chitin donor to a beta-1,3-glucan, beta-1,6-glucan, or chitin oligosaccharide acceptor, producing a chitin-glucan or chitin-chitin cell wall cross-link.
Justification: CRH1's defining molecular function is chitin-to-glucan transglycosylation. The nearest live GO molecular-function term in the review, GO:0016757 glycosyltransferase activity, is too broad, and the weak secondary GO:0008843 endochitinase side activity does not describe the conserved wall cross-linking reaction.
Parent term: hexosyltransferase activity
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005576 extracellular region | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA annotation from phylogenetic inference. CRH1 is a GPI-anchored cell wall protein that is secreted and covalently attached to the outer cell wall. While "extracellular region" is not wrong for a secreted protein, the more specific and accurate term is "fungal-type cell wall" (GO:0009277), which is already annotated with direct experimental evidence (IDA). This IBA adds little information beyond the existing IDA annotations. Reason: Technically correct but too broad. CRH1 is a GPI-CWP covalently incorporated into the cell wall, not a freely secreted extracellular protein. The IDA annotation to fungal-type cell wall is more informative. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000103261 Β· PTHR10963 broad secreted GH16/Crh ancestor SUPPORTS TRANSFER Current PAINT places extracellular-region localization at this broad node. The inference is broad but still valid for the secreted, GPI-anchored yeast cell-wall Crh1 protein. |
| GO:0006030 chitin metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA annotation from phylogenetic inference. CRH1 is directly involved in chitin metabolic process as a chitin transglycosylase that transfers chitin chains to glucan acceptors. This is consistent with IMP and IGI evidence from PMID:18694928. Falcon deep research corroborates that loss of CRH1/CRH2 reduces chitin-glucan linkage and the double mutant abolishes it, while overexpression increases it. Reason: Correct and supported by direct experimental evidence. CRH1 transfers chitin to glucan, which is a chitin metabolic process. GO:0006037 cell wall chitin metabolic process was obsoleted in 2024 and replaced by GO:0006030; CRH1's cell-wall context is captured by fungal-type cell wall organization and localization annotations. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001276384 Β· PTHR10963 fungal Crh cell-wall transglycosylase ancestor SUPPORTS TRANSFER Current PAINT places chitin metabolism at the fungal Crh node with both yeast CRH1 and UTR2/CRH2 as experimental seeds; CRH1 is inside the inherited fungal transglycosylase clade and has direct yeast IMP/IGI evidence for chitin transfer to glucan. SGD:S000003421 Β· yeast CRH1 SUPPORTS TRANSFER Direct yeast CRH1 IMP and IGI evidence grounds the PAINT assertion and makes CRH1's self-donor status expected rather than circular. SGD:S000000766 Β· yeast UTR2/CRH2 SUPPORTS TRANSFER UTR2/CRH2 provides paralogous yeast experimental support for conserved fungal Crh chitin-to-glucan transfer. Supporting Evidence: file:yeast/CRH1/CRH1-deep-research-falcon.md loss of **CRH1** or **CRH2** reduces chitin linked to **Ξ²(1β6)-glucan**, while the **crh1Ξ crh2Ξ** double mutant abolishes detectable chitinβΞ²(1β6)-glucan linkage; overexpression of **CRH1** increases the chitinβΞ²(1β6)-glucan complex |
| GO:0031505 fungal-type cell wall organization | IBA GO_REF:0000033 | ACCEPT | Summary: IBA annotation from phylogenetic inference. CRH1 is a key enzyme in fungal cell wall organization, cross-linking chitin to the glucan network. This is consistent with IMP and IGI evidence from PMID:18694928. Falcon deep research frames the primary role of Crh1 as strengthening and organizing the wall by creating covalent chitin-beta-glucan cross-links at sites of growth and division. Reason: Correct. CRH1 cross-links chitin to glucan, which is an essential step in cell wall organization. Well-supported by multiple lines of evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001276384 Β· PTHR10963 fungal Crh cell-wall transglycosylase ancestor SUPPORTS TRANSFER Current PAINT places fungal-type cell-wall organization at the same fungal Crh node as chitin metabolism, seeded by Saccharomyces and Candida Crh proteins. This matches yeast CRH1's direct role in organizing the wall through covalent chitin-to-glucan cross-links. Supporting Evidence: file:yeast/CRH1/CRH1-deep-research-falcon.md Crh1βs primary role is best described as **strengthening and organizing the wall** by creating **covalent chitinβΞ²-glucan cross-links** at sites of growth and division |
| GO:0009277 fungal-type cell wall | IBA GO_REF:0000033 | ACCEPT | Summary: IBA annotation from phylogenetic inference for cell wall localization. CRH1 is a GPI-CWP covalently attached to the cell wall, confirmed by mass spectrometry (PMID:15781460) and GFP localization (PMID:10757808). Consistent with IDA evidence. Reason: Correct. CRH1 is covalently linked to the cell wall via its GPI anchor remnant. Multiple IDA annotations confirm this. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001276384 Β· PTHR10963 fungal Crh cell-wall transglycosylase ancestor SUPPORTS TRANSFER Current PAINT places fungal-type cell-wall localization at the fungal Crh node supported by yeast and Candida cell-wall Crh proteins, including direct CRH1 evidence; CRH1 is a GPI-anchored cell-wall protein in that inherited clade. |
| GO:0016757 glycosyltransferase activity | IBA GO_REF:0000033 | MODIFY | Summary: IBA annotation from phylogenetic inference. CRH1 is a chitin transglycosylase that transfers chitin chains to glucan acceptors, which is a glycosyltransferase activity. Supported by IDA evidence from PMID:23919454 and IMP/IGI from PMID:18694928. Falcon deep research confirms the family is defined by a GH16-like catalytic motif whose residues are required for in vivo function, and that the enzymes favor transfer (transglycosylation) over net hydrolysis. Reason: Correct but too broad. Crh1 catalyzes chitin-to-beta-glucan transglycosylation, and GO has no specific chitin transglycosylase molecular function term to distinguish this activity from other glycosyltransferases. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN001276384 Β· PTHR10963 fungal Crh cell-wall transglycosylase ancestor SUPPORTS TRANSFER Current PAINT places glycosyltransferase activity at the fungal Crh node with yeast CRH1/UTR2 experimental seeds. The term is broad because GO lacks a chitin transglycosylase child, but the inherited assertion fits CRH1's conserved chitin-to-glucan transfer activity. SGD:S000003421 Β· yeast CRH1 SUPPORTS TRANSFER Direct yeast CRH1 IDA, IMP, and IGI evidence supports the same glycosyltransferase parent term and explains why CRH1 legitimately appears in its own PAINT WITH/FROM evidence. SGD:S000000766 Β· yeast UTR2/CRH2 SUPPORTS TRANSFER UTR2/CRH2 is the redundant yeast Crh paralog and supports transfer of the same chitin-to-glucan activity. Proposed replacements: chitin:glucan chitinotransferase activity Supporting Evidence: file:yeast/CRH1/CRH1-deep-research-falcon.md A catalytic-site mutant allele (Crh1 with substitutions at key acidic residues) fails to complement Congo red sensitivity, implying that the predicted catalytic residues are essential for function in vivo file:yeast/CRH1/CRH1-deep-research-falcon.md The enzyme can join the **reducing end of a chitin donor** to the **non-reducing end of an acceptor** oligosaccharide |
| GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: IEA from InterPro mapping (IPR000757 Beta-glucanase-like domain). CRH1 does have weak endochitinase activity (EC 3.2.1.14) as demonstrated by Mazan et al. (2013), so the annotation is not incorrect. However, the primary function is transglycosylase activity, not hydrolase activity. The hydrolytic activity is secondary and weak. Reason: Technically correct -- CRH1 has documented weak endochitinase activity (PMID:23919454) -- but the primary evolved function is transglycosylation, not hydrolysis. This InterPro-based annotation reflects the ancestral GH16 hydrolase function rather than the derived transglycosylase specialization. Supporting Evidence: PMID:23919454 Both proteins exhibited a weak chitinolytic activity in different assays whereby the ratio of endo- compared with exo-chitinase activity was approximately 4-fold higher in Crh1 than in Crh2 |
| GO:0005975 carbohydrate metabolic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: IEA from InterPro mapping. CRH1 is indeed involved in carbohydrate metabolism (chitin and glucan processing). This is correct but very broad -- the more specific term "chitin metabolic process" (GO:0006030) is already annotated. Reason: Correct but very broad. Subsumed by the more specific GO:0006030 (chitin metabolic process) which is already annotated with experimental evidence. |
| GO:0008843 endochitinase activity | IEA GO_REF:0000003 | KEEP AS NON CORE | Summary: IEA from EC number mapping (EC 3.2.1.14). Mazan et al. (2013) demonstrated weak endochitinase activity for heterologously expressed CRH1. The endo:exo chitinase ratio was approximately 4-fold higher in Crh1 than Crh2. However, the chitinase activity is secondary to the primary transglycosylase function. Reason: Correct. CRH1 has documented endochitinase activity (PMID:23919454), but this weak in vitro activity with a pH optimum of 3.5 is secondary to the primary chitin transglycosylase activity. Supporting Evidence: PMID:23919454 Both proteins exhibited a weak chitinolytic activity in different assays whereby the ratio of endo- compared with exo-chitinase activity was approximately 4-fold higher in Crh1 than in Crh2 |
| GO:0009277 fungal-type cell wall | IEA GO_REF:0000117 | ACCEPT | Summary: IEA from ARBA machine learning model. Correct -- CRH1 is covalently linked to the fungal-type cell wall. Redundant with IDA annotations from PMID:10757808 and PMID:15781460. Reason: Correct and consistent with multiple lines of direct experimental evidence. |
| GO:0016020 membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: IEA from UniProtKB subcellular location mapping. CRH1 is GPI-anchored to the outer leaflet of the plasma membrane before being transferred to the cell wall. The annotation is technically correct but imprecise. CRH1 is primarily a cell wall protein, not a membrane protein in the traditional sense. The GPI anchor transiently associates it with the membrane during transport. Reason: Technically correct (GPI-anchored to membrane) but misleading for CRH1, which is primarily a covalently-linked cell wall protein. The GPI anchor is processed during transfer to the cell wall. |
| GO:0016798 hydrolase activity, acting on glycosyl bonds | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: IEA from InterPro mapping (IPR017168 CRH-like family). CRH1 has weak endochitinase activity, so hydrolysis of glycosyl bonds is technically correct. However, this is a parent term of endochitinase activity (GO:0008843) which is already annotated, and the primary function is transglycosylation rather than hydrolysis. Reason: Correct but broad and redundant. The more specific endochitinase activity (GO:0008843) is already annotated. The primary function is transglycosylase, not hydrolase. |
| GO:0031505 fungal-type cell wall organization | IEA GO_REF:0000117 | ACCEPT | Summary: IEA from ARBA machine learning model. Correct -- CRH1 is essential for cell wall organization through chitin-glucan cross-linking. Consistent with IMP/IGI evidence. Reason: Correct and consistent with experimental evidence from PMID:18694928. |
| GO:0071555 cell wall organization | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: IEA from InterPro mapping. Correct but broad -- the more specific term "fungal-type cell wall organization" (GO:0031505) is already annotated with experimental evidence. Reason: Correct but subsumed by the more specific GO:0031505 (fungal-type cell wall organization) which is already annotated. |
| GO:0071944 cell periphery | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | KEEP AS NON CORE | Summary: HDA annotation from the SWAp-Tag high-throughput localization study (Yofe et al. 2016). CRH1 is a GPI-anchored cell wall protein at the cell surface, so cell periphery is correct. However, more specific terms (fungal-type cell wall, incipient cellular bud site) are already annotated with direct experimental evidence. Reason: Correct but broad. The high-throughput dataset correctly places CRH1 at the cell periphery, but more specific localization terms are already available from focused studies. Supporting Evidence: PMID:26928762 we constructed and investigated a library of βΌ1,800 strains carrying SWAT-GFP modules at the amino termini of endomembrane proteins |
| GO:0016757 glycosyltransferase activity | IDA PMID:23919454 A novel fluorescence assay and catalytic properties of Crh1 ... | MODIFY | Summary: IDA annotation based on Mazan et al. (2013). Heterologously expressed CRH1 was shown to transfer chitin chains to glucan oligosaccharide acceptors in a direct in vitro assay using fluorescently-labeled substrates. This is the most direct demonstration of CRH1's transglycosylase activity. Reason: Core molecular function of CRH1 demonstrated by direct biochemical assay, but GO:0016757 is broader than the chitin transglycosylase activity assayed. CRH1 uses soluble chitin derivatives as donors and glucan-derived oligosaccharides as acceptors to catalyze transglycosylation. Proposed replacements: chitin:glucan chitinotransferase activity Supporting Evidence: PMID:23919454 Both proteins act as chitin transglycosylases; they use soluble chitin derivatives, such as carboxymethyl chitin, glycol-chitin and/or N-acetyl chito-oligosaccharides of DP (degree of polymerization)β₯5 as the oligoglycosyl donors, and oligosaccharides derived from chitin, Ξ²-(1,3)-glucan (laminarin) and Ξ²-(1,6)-glucan (pustulan), fluorescently labelled with sulforhodamine or FITC as acceptors |
| GO:0000131 incipient cellular bud site | IDA PMID:10757808 A novel family of cell wall-related proteins regulated diffe... | ACCEPT | Summary: IDA annotation based on Rodriguez-Pena et al. (2000). Crh1-GFP was observed at the incipient bud site by confocal fluorescence microscopy. CRH1 localizes to chitin-rich areas where cell wall remodeling occurs during polarized growth. Reason: Correct and specific. CRH1-GFP localization to the incipient bud site is consistent with its function in chitin-glucan cross-linking during bud emergence. Supporting Evidence: PMID:10757808 Crh1-green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes file:yeast/CRH1/CRH1-deep-research-falcon.md Crh1-GFP localization studies show enrichment at **polarized growth sites**βbud emergence, the **motherβdaughter neck**, and bud scarsβwhere chitin is enriched; Crh1 also appears at mating-related structures and marks **spore envelopes** during sporulation |
| GO:0006030 chitin metabolic process | IMP PMID:18694928 Assembly of the yeast cell wall. Crh1p and Crh2p act as tran... | ACCEPT | Summary: IMP annotation based on Cabib et al. (2008). Mutant phenotype analysis showed that CRH genes are required for chitin transfer to glucan. Fluorescent chitin acceptor labeling in vivo was dependent on CRH genes. This directly demonstrates CRH1 involvement in chitin metabolism. Reason: Core biological process. CRH1 transfers chitin chains to glucan acceptors, directly participating in chitin metabolism. The crh1/crh2 double mutant completely lacks chitin-glucan cross-links. GO:0006030 is the current replacement for the obsolete cell wall chitin metabolic process term, and fungal-type cell wall annotations capture the cell-wall context. Supporting Evidence: PMID:18694928 the Crh proteins act by transferring chitin chains to beta(1-6)glucan, with a newly observed high activity in the bud scar |
| GO:0006030 chitin metabolic process | IGI PMID:18694928 Assembly of the yeast cell wall. Crh1p and Crh2p act as tran... | ACCEPT | Summary: IGI annotation based on genetic interaction between CRH1 and CRH2 (SGD:S000000766). Cabib et al. (2008) showed that CRH1 and CRH2 are redundantly required for chitin transfer to glucan; the double mutant shows complete loss of chitin-glucan cross-links while single mutants show partial loss. Reason: Correct. The genetic interaction between CRH1 and CRH2 demonstrates redundant function in chitin metabolism. GO:0006030 is the current replacement for the obsolete cell wall chitin metabolic process term, and fungal-type cell wall annotations capture the cell-wall context. Supporting Evidence: PMID:18694928 In vivo, fluorescence was detected in bud scars and at a lower level in the cell contour, both being dependent on the CRH genes |
| GO:0009277 fungal-type cell wall | IDA PMID:10757808 A novel family of cell wall-related proteins regulated diffe... | ACCEPT | Summary: IDA annotation based on Rodriguez-Pena et al. (2000). Crh1-GFP localized to the cell surface, particularly in chitin-rich areas. The protein is a GPI-CWP covalently attached to the cell wall. Reason: Core localization. CRH1 is a GPI-anchored cell wall protein, demonstrated by GFP localization at the cell surface in chitin-rich regions. Supporting Evidence: PMID:10757808 Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas file:yeast/CRH1/CRH1-deep-research-falcon.md it is reported to be covalently incorporated into the wall and releasable by glucanase (laminarinase), consistent with a GPI-anchored wall protein that becomes wall-integrated |
| GO:0009277 fungal-type cell wall | IDA PMID:15781460 Comprehensive proteomic analysis of Saccharomyces cerevisiae... | ACCEPT | Summary: IDA annotation based on Yin et al. (2005). CRH1 was identified as a covalently-bound cell wall protein by mass spectrometry of isolated cell walls. Specifically identified as a GPI-modified CWP. Reason: Direct proteomic identification of CRH1 in isolated cell walls confirms cell wall localization. Supporting Evidence: PMID:15781460 The identified proteins include 12 predicted glycosylphosphatidylinositol-modified CWPs ...seven of the identified proteins (Gas1p, Gas3p, Gas5p, Crh1p, Utr2p, Scw4p, and Scw10p) are classified as glycoside hydrolases |
| GO:0016757 glycosyltransferase activity | IMP PMID:18694928 Assembly of the yeast cell wall. Crh1p and Crh2p act as tran... | MODIFY | Summary: IMP annotation based on Cabib et al. (2008). Mutant phenotype analysis showed CRH-dependent transfer of chitin to glucan both in vivo (fluorescent acceptor labeling) and in digitonin-permeabilized cells. The linking reaction required CRH genes. Reason: The mutant phenotype supports the core chitin-to-glucan transfer activity, but GO:0016757 is broader than the needed chitin transglycosylase molecular function. Proposed replacements: chitin:glucan chitinotransferase activity Supporting Evidence: PMID:18694928 The linking reaction was also shown in digitonin-permeabilized cells, with UDP-N-acetylglucosamine as the substrate for nascent chitin production. Both the nucleotide and the Crh proteins were required here |
| GO:0016757 glycosyltransferase activity | IGI PMID:18694928 Assembly of the yeast cell wall. Crh1p and Crh2p act as tran... | MODIFY | Summary: IGI annotation based on genetic interaction between CRH1 and CRH2. The redundant requirement of both genes for full transglycosylase activity was demonstrated by comparing single and double mutants. Reason: Correct but too broad. The CRH1/CRH2 genetic interaction supports the specific chitin transglycosylase activity that cross-links chitin to glucan. Proposed replacements: chitin:glucan chitinotransferase activity Supporting Evidence: PMID:18694928 In vivo, fluorescence was detected in bud scars and at a lower level in the cell contour, both being dependent on the CRH genes |
| GO:0031505 fungal-type cell wall organization | IMP PMID:18694928 Assembly of the yeast cell wall. Crh1p and Crh2p act as tran... | ACCEPT | Summary: IMP annotation based on Cabib et al. (2008). crh1/crh2 double mutants show altered cell wall architecture with loss of chitin-glucan cross-links and increased alkali-soluble glucan. Deletion aggravated defects of fks1 and gas1 mutants. Reason: Core biological process. CRH1 is essential for proper cell wall organization through chitin-glucan cross-linking. Falcon deep research additionally connects this wall-organizing role to the cell wall integrity (CWI) pathway, with CRH1 induced at 38C in a Slt2-dependent manner. Supporting Evidence: PMID:18694928 The importance of transglycosylation for cell wall assembly is thus firmly established file:yeast/CRH1/CRH1-deep-research-falcon.md shifting cells to **38Β°C** increases CRH1 expression via the **cell integrity pathway**, and this induction is abolished in an **slt2Ξ** mutant, directly linking CRH1 to the CWI MAPK pathway |
| GO:0031505 fungal-type cell wall organization | IGI PMID:18694928 Assembly of the yeast cell wall. Crh1p and Crh2p act as tran... | ACCEPT | Summary: IGI annotation based on genetic interaction between CRH1 and CRH2. Single and double mutant analysis demonstrates their redundant contribution to cell wall organization. Reason: Correct. The genetic interaction confirms both CRH1 and CRH2 contribute to cell wall organization. Supporting Evidence: PMID:18694928 The importance of transglycosylation for cell wall assembly is thus firmly established |
| GO:0008843 endochitinase activity | EXP PMID:23919454 A novel fluorescence assay and catalytic properties of Crh1 ... | KEEP AS NON CORE | Summary: UniProt EXP annotation for the same Mazan et al. biochemical study that supports the EC-derived IEA row. Heterologously expressed Crh1 has weak chitinolytic activity in addition to its primary transglycosylase activity. Reason: The direct biochemical evidence supports endochitinase activity, but it is a weak in vitro activity with a pH optimum of 3.5 and is secondary to the conserved cell-wall chitin transglycosylase reaction that cross-links chitin to beta-glucans. Supporting Evidence: PMID:23919454 Both proteins exhibited a weak chitinolytic activity in different assays whereby the ratio of endo- compared with exo-chitinase activity was approximately 4-fold higher in Crh1 than in Crh2. The pH optimum of both enzymes was 3.5 and the optimum temperature was 37Β°C |
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Download this section (compressed HTML)Q: Is there a more specific GO term for chitin transglycosylase activity that could distinguish the primary transglycosylation function from the secondary endochitinase activity? Currently both activities are annotated under different parent terms (glycosyltransferase vs endochitinase), but there is no specific "chitin transglycosylase activity" term in GO.
Q: What is the relative in vivo contribution of the endochitinase activity versus the transglycosylase activity of CRH1? Is the chitinase activity biologically relevant or simply a side reaction of the GH16 catalytic mechanism?
Experiment: Use compartment-specific fluorescent chitin acceptors with conditional CRH1 expression to determine whether transglycosylation rates differ at different cell surface locations. Compare with CRH2 localization and activity patterns.
Hypothesis: CRH1 chitin transglycosylase activity may have distinct substrate preferences in different cell wall compartments (bud scar vs lateral wall vs septum).
Type: fluorescence microscopy with functional assay
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Download this section (compressed HTML)Chitin transglycosylase; functions in the transfer of chitin to beta(1-6) and beta(1-3) glucans in the cell wall; similar and functionally redundant to Utr2; localizes to sites of polarized growth; expression induced by cell wall stress
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