CH3L1_MOUSE
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 03-AUG-2022, entry version 172.
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};
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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 IntAct; Q61362; 3.
DR STRING; 10090.ENSMUSP00000080717; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q61362; 1 site.
DR PhosphoSitePlus; Q61362; -.
DR jPOST; Q61362; -.
DR MaxQB; Q61362; -.
DR PaxDb; Q61362; -.
DR PeptideAtlas; Q61362; -.
DR PRIDE; 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; 455 antibodies from 36 providers.
DR DNASU; 12654; -.
DR Ensembl; ENSMUST00000082060; ENSMUSP00000080717; ENSMUSG00000064246. [Q61362-1]
DR Ensembl; ENSMUST00000153856; ENSMUSP00000117117; ENSMUSG00000064246. [Q61362-2]
DR Ensembl; ENSMUST00000156873; ENSMUSP00000119205; ENSMUSG00000064246. [Q61362-3]
DR GeneID; 12654; -.
DR KEGG; mmu:12654; -.
DR UCSC; uc007crg.2; mouse. [Q61362-1]
DR CTD; 12654; -.
DR MGI; MGI:1340899; Chil1.
DR VEuPathDB; HostDB:ENSMUSG00000064246; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000161815; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q61362; -.
DR OMA; HRLLGQQ; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; Q61362; -.
DR TreeFam; TF315610; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12654; 2 hits in 74 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 114 other 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 protein kinase B signaling; 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 Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR028538; CHI3L1.
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:SF202; PTHR11177:SF202; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 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
