ID CH3L1_MOUSE Reviewed; 389 AA. AC Q61362; B0FEU7; D3Z2P2; Q3U291; Q4FJW9; Q8BKL8; Q99J84; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 14-MAY-2014, sequence version 3. DT 27-MAR-2024, entry version 181. DE RecName: Full=Chitinase-3-like protein 1; DE AltName: Full=BRP39 protein; DE AltName: Full=Breast regression protein 39; DE AltName: Full=Cartilage glycoprotein 39; DE Short=CGP-39; DE Short=GP-39; DE Flags: Precursor; GN Name=Chi3l1; Synonyms=Brp39, Chil1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=7970700; RA Morrison B.W., Leder P.; RT "neu and ras initiate murine mammary tumors that share genetic markers RT generally absent in c-myc and int-2-initiated tumors."; RL Oncogene 9:3417-3426(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF LEU-136, RP AND CRYSTALLIZATION. RC TISSUE=Mammary gland; RX PubMed=19041398; DOI=10.1016/j.pep.2008.11.001; RA Mohanty A.K., Fisher A.J., Yu Z., Pradeep M.A., Janjanam J., Kaushik J.K.; RT "Cloning, expression, characterization and crystallization of BRP39, a RT signalling glycoprotein expressed during mammary gland apoptosis."; RL Protein Expr. Purif. 64:213-218(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., RA Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=16472595; DOI=10.1053/j.gastro.2005.12.007; RA Mizoguchi E.; RT "Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing RT bacterial adhesion and invasion in colonic epithelial cells."; RL Gastroenterology 130:398-411(2006). RN [8] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19414556; DOI=10.1084/jem.20081271; RA Lee C.G., Hartl D., Lee G.R., Koller B., Matsuura H., Da Silva C.A., RA Sohn M.H., Cohn L., Homer R.J., Kozhich A.A., Humbles A., Kearley J., RA Coyle A., Chupp G., Reed J., Flavell R.A., Elias J.A.; RT "Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in Th2 RT and IL-13-induced tissue responses and apoptosis."; RL J. Exp. Med. 206:1149-1166(2009). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND RP DISRUPTION PHENOTYPE. RX PubMed=20558631; DOI=10.1164/rccm.200912-1793oc; RA Sohn M.H., Kang M.J., Matsuura H., Bhandari V., Chen N.Y., Lee C.G., RA Elias J.A.; RT "The chitinase-like proteins breast regression protein-39 and YKL-40 RT regulate hyperoxia-induced acute lung injury."; RL Am. J. Respir. Crit. Care Med. 182:918-928(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION. RX PubMed=21546314; DOI=10.1016/j.clim.2011.04.007; RA Chen C.C., Llado V., Eurich K., Tran H.T., Mizoguchi E.; RT "Carbohydrate-binding motif in chitinase 3-like 1 (CHI3L1/YKL-40) RT specifically activates Akt signaling pathway in colonic epithelial cells."; RL Clin. Immunol. 140:268-275(2011). RN [12] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22817986; DOI=10.1016/j.chom.2012.05.017; RA Dela Cruz C.S., Liu W., He C.H., Jacoby A., Gornitzky A., Ma B., RA Flavell R., Lee C.G., Elias J.A.; RT "Chitinase 3-like-1 promotes Streptococcus pneumoniae killing and augments RT host tolerance to lung antibacterial responses."; RL Cell Host Microbe 12:34-46(2012). RN [13] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=21866546; DOI=10.1002/ijc.26379; RA Libreros S., Garcia-Areas R., Shibata Y., Carrio R., Torroella-Kouri M., RA Iragavarapu-Charyulu V.; RT "Induction of proinflammatory mediators by CHI3L1 is reduced by chitin RT treatment: decreased tumor metastasis in a breast cancer model."; RL Int. J. Cancer 131:377-386(2012). CC -!- FUNCTION: Carbohydrate-binding lectin with a preference for chitin. Has CC no chitinase activity. May play a role in tissue remodeling and in the CC capacity of cells to respond to and cope with changes in their CC environment. Plays a role in T-helper cell type 2 (Th2) inflammatory CC response and IL-13-induced inflammation, regulating allergen CC sensitization, inflammatory cell apoptosis, dendritic cell accumulation CC and M2 macrophage differentiation. Facilitates invasion of pathogenic CC enteric bacteria into colonic mucosa and lymphoid organs. Mediates CC activation of AKT1 signaling pathway and subsequent IL8 production in CC colonic epithelial cells. Regulates antibacterial responses in lung by CC contributing to macrophage bacterial killing, controlling bacterial CC dissemination and augmenting host tolerance. Also regulates hyperoxia- CC induced injury, inflammation and epithelial apoptosis in lung. CC {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19041398, CC ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, CC ECO:0000269|PubMed:21546314, ECO:0000269|PubMed:22817986}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- INTERACTION: CC Q61362; O88786: Il13ra2; NbExp=12; IntAct=EBI-8392424, EBI-20260800; CC Q61362; P16110: Lgals3; NbExp=4; IntAct=EBI-8392424, EBI-3508325; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm. CC Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage (BAL) CC fluids. Localizes mainly to endoplasmic reticulum when overexpressed in CC cells, with some protein also detected throughout the cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=1; CC IsoId=Q61362-1; Sequence=Displayed; CC Name=2; CC IsoId=Q61362-2; Sequence=VSP_054524; CC Name=3; CC IsoId=Q61362-3; Sequence=VSP_054523; CC -!- TISSUE SPECIFICITY: Detected in lung in pulmonary macrophages and CC alveolar type 2 cells and in bronchoalveolar lavage (BAL) fluids. CC Expressed in mammary tumor cells (at protein level). Expressed in lung. CC Not detected in non-inflammatory colon. {ECO:0000269|PubMed:16472595, CC ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, CC ECO:0000269|PubMed:21866546}. CC -!- INDUCTION: Up-regulated in colon under several inflammatory conditions. CC Up-regulated upon pulmonary inflammation elicited by sensitization and CC challenge with the chitin-free aeroallergen ovalbumin or with chitin- CC containing antigen house dust mite (HDM) extract. Up-regulated in lungs CC after S.pneumoniae infection. Up-regulated in splenic cells of mammary CC tumor-bearing animals. Down-regulated by hyperoxia in lung. CC {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556, CC ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21866546, CC ECO:0000269|PubMed:22817986}. CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and appear normal, but CC have defective antigen-induced Th2 inflammatory responses and defective CC IL-13-induced responses, displaying accelerated cell death responses CC and diminished M2 macrophage differentiation. Mutant mice are more CC sensitive to S.pneumoniae infection, displaying enhanced mortality, CC exacerbated lung injury and decreased bacterial clearance compared to CC wild-type mice. Mutant mice also have an exacerbated response to CC hyperoxia, displaying enhanced protein leak, tissue inflammation and CC chemokine production and premature death. {ECO:0000269|PubMed:19414556, CC ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:22817986}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-9 CC of isoform 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced by alternative splicing of CC isoform 1. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}. CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family, Leu- CC 149 is present instead of the conserved Glu which is an active site CC residue. Therefore this protein lacks chitinase activity. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH03780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH04734.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH05611.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA63603.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X93035; CAA63603.1; ALT_INIT; mRNA. DR EMBL; EU313768; ABY53363.1; -; mRNA. DR EMBL; AK051475; BAC34654.1; -; mRNA. DR EMBL; AK155412; BAE33251.1; -; mRNA. DR EMBL; CT010283; CAJ18491.1; -; mRNA. DR EMBL; AC137104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003780; AAH03780.1; ALT_INIT; mRNA. DR EMBL; BC004734; AAH04734.1; ALT_INIT; mRNA. DR EMBL; BC005611; AAH05611.1; ALT_INIT; mRNA. DR CCDS; CCDS48368.1; -. [Q61362-1] DR CCDS; CCDS87878.1; -. [Q61362-3] DR PIR; S61551; S61551. DR RefSeq; NP_031721.2; NM_007695.3. [Q61362-1] DR RefSeq; XP_006529174.1; XM_006529111.3. DR PDB; 5XEP; X-ray; 2.60 A; A/B/C/D/E/F=9-389. DR PDBsum; 5XEP; -. DR AlphaFoldDB; Q61362; -. DR SMR; Q61362; -. DR BioGRID; 198698; 1. DR IntAct; Q61362; 3. DR STRING; 10090.ENSMUSP00000080717; -. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR GlyCosmos; Q61362; 1 site, No reported glycans. DR GlyGen; Q61362; 1 site. DR PhosphoSitePlus; Q61362; -. DR jPOST; Q61362; -. DR MaxQB; Q61362; -. DR PaxDb; 10090-ENSMUSP00000080717; -. DR PeptideAtlas; Q61362; -. DR ProteomicsDB; 281204; -. [Q61362-1] DR ProteomicsDB; 281205; -. [Q61362-2] DR ProteomicsDB; 281206; -. [Q61362-3] DR ABCD; Q61362; 3 sequenced antibodies. DR Antibodypedia; 34542; 517 antibodies from 37 providers. DR DNASU; 12654; -. DR Ensembl; ENSMUST00000082060.10; ENSMUSP00000080717.4; ENSMUSG00000064246.11. [Q61362-1] DR Ensembl; ENSMUST00000153856.8; ENSMUSP00000117117.2; ENSMUSG00000064246.11. [Q61362-2] DR Ensembl; ENSMUST00000156873.8; ENSMUSP00000119205.2; ENSMUSG00000064246.11. [Q61362-3] DR GeneID; 12654; -. DR KEGG; mmu:12654; -. DR UCSC; uc007crg.2; mouse. [Q61362-1] DR AGR; MGI:1340899; -. DR CTD; 1116; -. DR MGI; MGI:1340899; Chi3l1. DR VEuPathDB; HostDB:ENSMUSG00000064246; -. DR eggNOG; KOG2806; Eukaryota. DR GeneTree; ENSGT00940000161815; -. DR HOGENOM; CLU_002833_3_1_1; -. DR InParanoid; Q61362; -. DR OMA; KSCQRGV; -. DR OrthoDB; 1752999at2759; -. DR PhylomeDB; Q61362; -. DR TreeFam; TF315610; -. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 12654; 2 hits in 79 CRISPR screens. DR ChiTaRS; Chil1; mouse. DR PRO; PR:Q61362; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q61362; Protein. DR Bgee; ENSMUSG00000064246; Expressed in granulocyte and 117 other cell types or tissues. DR ExpressionAtlas; Q61362; baseline and differential. DR Genevisible; Q61362; MM. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0008061; F:chitin binding; ISS:UniProtKB. DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB. DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0030324; P:lung development; ISS:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProtKB. DR GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB. DR GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB. DR GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB. DR GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB. DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 1. DR Gene3D; 3.10.50.10; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR011583; Chitinase_II. DR InterPro; IPR029070; Chitinase_insertion_sf. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR11177; CHITINASE; 1. DR PANTHER; PTHR11177:SF202; CHITINASE-3-LIKE PROTEIN 1; 1. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SMART; SM00636; Glyco_18; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF54556; Chitinase insertion domain; 1. DR PROSITE; PS51910; GH18_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Alternative splicing; Antimicrobial; KW Apoptosis; Cytoplasm; Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Inflammatory response; Reference proteome; Secreted; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000250" FT CHAIN 30..389 FT /note="Chitinase-3-like protein 1" FT /id="PRO_0000011966" FT DOMAIN 30..389 FT /note="GH18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT REGION 333..347 FT /note="Important for AKT1 activation and IL8 production" FT BINDING 79..80 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT BINDING 106..109 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT BINDING 150 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT BINDING 213..216 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT BINDING 361 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT CARBOHYD 68 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" FT DISULFID 34..59 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT DISULFID 309..372 FT /evidence="ECO:0000250" FT VAR_SEQ 1..16 FT /note="MHTSTEARMGMRAALT -> MTLQLA (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_054523" FT VAR_SEQ 1..8 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:19041398, ECO:0000303|Ref.4" FT /id="VSP_054524" FT MUTAGEN 136 FT /note="L->E: No effect on chiting-binding. No restoration FT of chitinase activity." FT /evidence="ECO:0000269|PubMed:19041398" FT CONFLICT 112 FT /note="E -> G (in Ref. 4; ABY53363)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="A -> V (in Ref. 3; BAE33251)" FT /evidence="ECO:0000305" FT CONFLICT 339 FT /note="D -> H (in Ref. 1; CAA63603)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="G -> R (in Ref. 4; ABY53363)" FT /evidence="ECO:0000305" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 60..69 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 82..90 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:5XEP" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 112..119 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 122..139 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 143..147 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 156..173 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 191..197 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 200..204 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 246..255 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 263..279 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 286..290 FT /evidence="ECO:0007829|PDB:5XEP" FT TURN 295..297 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 305..312 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:5XEP" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 326..330 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 340..352 FT /evidence="ECO:0007829|PDB:5XEP" FT STRAND 356..361 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:5XEP" FT HELIX 379..388 FT /evidence="ECO:0007829|PDB:5XEP" SQ SEQUENCE 389 AA; 43893 MW; 9E7D66069B233834 CRC64; MHTSTEARMG MRAALTGFAV LMLLQSCSAY KLVCYFTSWS QYREGVGSFL PDAIQPFLCT HIIYSFANIS SDNMLSTWEW NDESNYDKLN KLKTRNTNLK TLLSVGGWKF GEKRFSEIAS NTERRTAFVR SVAPFLRSYG FDGLDLAWLY PRLRDKQYFS TLIKELNAEF TKEVQPGREK LLLSAALSAG KVAIDTGYDI AQIAQHLDFI NLMTYDFHGV WRQITGHHSP LFQGQKDTRF DRYSNVNYAV QYMIRLGAQA SKLLMGIPTF GKSFTLASSE NQLGAPISGE GLPGRFTKEA GTLAYYEICD FLKGAEVHRL SNEKVPFATK GNQWVGYEDK ESVKNKVGFL KEKKLAGAMV WALDLDDFQG TCQPKEFFPL TNAIKDALA //