CH3L1_HUMAN
ID CH3L1_HUMAN Reviewed; 383 AA.
AC P36222; B2R7B0; P30923; Q8IVA4; Q96HI7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=39 kDa synovial protein;
DE AltName: Full=Cartilage glycoprotein 39;
DE Short=CGP-39;
DE Short=GP-39;
DE Short=hCGP-39;
DE AltName: Full=YKL-40;
DE Flags: Precursor;
GN Name=CHI3L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT THR-311.
RC TISSUE=Cartilage;
RX PubMed=8245017; DOI=10.1016/s0021-9258(19)74461-5;
RA Hakala B.E., White C., Recklies A.D.;
RT "Human cartilage gp-39, a major secretory product of articular chondrocytes
RT and synovial cells, is a mammalian member of a chitinase protein family.";
RL J. Biol. Chem. 268:25803-25810(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-311.
RC TISSUE=Blood;
RX PubMed=9244440; DOI=10.1006/geno.1997.4778;
RA Rehli M., Krause S.W., Andressen R.;
RT "Molecular characterization of the gene for human cartilage gp-39 (CHI3L1),
RT a member of the chitinase protein family and marker for late stages of
RT macrophage differentiation.";
RL Genomics 43:221-225(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-145.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-145.
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 22-45.
RX PubMed=2375755; DOI=10.1042/bj2690265;
RA Nyirkos P., Golds E.E.;
RT "Human synovial cells secrete a 39 kDa protein similar to a bovine mammary
RT protein expressed during the non-lactating period.";
RL Biochem. J. 269:265-268(1990).
RN [8]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9492324; DOI=10.1046/j.1432-1327.1998.2510504.x;
RA Renkema G.H., Boot R.G., Au F.L., Donker-Koopman W.E., Strijland A.,
RA Muijsers A.O., Hrebicek M., Aerts J.M.F.G.;
RT "Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein,
RT a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases
RT secreted by human macrophages.";
RL Eur. J. Biochem. 251:504-509(1998).
RN [9]
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 [10]
RP INVOLVEMENT IN SCZD.
RX PubMed=17160890; DOI=10.1086/510438;
RA Zhao X., Tang R., Gao B., Shi Y., Zhou J., Guo S., Zhang J., Wang Y.,
RA Tang W., Meng J., Li S., Wang H., Ma G., Lin C., Xiao Y., Feng G., Lin Z.,
RA Zhu S., Xing Y., Sang H., St Clair D., He L.;
RT "Functional variants in the promoter region of Chitinase 3-like 1 (CHI3L1)
RT and susceptibility to schizophrenia.";
RL Am. J. Hum. Genet. 80:12-18(2007).
RN [11]
RP FUNCTION.
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 [12]
RP FUNCTION, AND INDUCTION.
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 [13]
RP INVOLVEMENT IN SCZD.
RX PubMed=20051317; DOI=10.1016/j.schres.2009.12.002;
RA Ohi K., Hashimoto R., Yasuda Y., Yoshida T., Takahashi H., Iike N.,
RA Iwase M., Kamino K., Ishii R., Kazui H., Fukumoto M., Takamura H.,
RA Yamamori H., Azechi M., Ikezawa K., Tanimukai H., Tagami S., Morihara T.,
RA Okochi M., Yamada K., Numata S., Ikeda M., Tanaka T., Kudo T., Ueno S.,
RA Yoshikawa T., Ohmori T., Iwata N., Ozaki N., Takeda M.;
RT "The chitinase 3-like 1 gene and schizophrenia: evidence from a multi-
RT center case-control study and meta-analysis.";
RL Schizophr. Res. 116:126-132(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN
RP OLIGOMERS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-60.
RX PubMed=12775711; DOI=10.1074/jbc.m303371200;
RA Houston D.R., Recklies A.D., Krupa J.C., van Aalten D.M.F.;
RT "Structure and ligand-induced conformational change of the 39-kDa
RT glycoprotein from human articular chondrocytes.";
RL J. Biol. Chem. 278:30206-30212(2003).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN
RP OLIGOMERS, AND DISULFIDE BONDS.
RX PubMed=12851408; DOI=10.1074/jbc.m303137200;
RA Fusetti F., Pijning T., Kalk K.H., Bos E., Dijkstra B.W.;
RT "Crystal structure and carbohydrate-binding properties of the human
RT cartilage glycoprotein-39.";
RL J. Biol. Chem. 278:37753-37760(2003).
RN [16]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASRT7.
RX PubMed=18403759; DOI=10.1056/nejmoa0708801;
RA Ober C., Tan Z., Sun Y., Possick J.D., Pan L., Nicolae R., Radford S.,
RA Parry R.R., Heinzmann A., Deichmann K.A., Lester L.A., Gern J.E.,
RA Lemanske R.F. Jr., Nicolae D.L., Elias J.A., Chupp G.L.;
RT "Effect of variation in CHI3L1 on serum YKL-40 level, risk of asthma, and
RT lung function.";
RL N. Engl. J. Med. 358:1682-1691(2008).
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:19414556,
CC ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:9492324}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12775711,
CC ECO:0000269|PubMed:12851408}.
CC -!- INTERACTION:
CC P36222; Q14627: IL13RA2; NbExp=9; IntAct=EBI-6917454, EBI-4320063;
CC P36222; P17931: LGALS3; NbExp=2; IntAct=EBI-6917454, EBI-1170392;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:9492324}. Cytoplasm {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in activated macrophages, articular
CC chondrocytes, synovial cells as well as in liver. Very low or
CC undetectable expression in non-inflammatory colon. Undetectable in
CC muscle tissues, lung, pancreas, mononuclear cells, or fibroblasts.
CC {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:9492324}.
CC -!- INDUCTION: Up-regulated in colon under several inflammatory conditions.
CC Down-regulated by hyperoxia in bronchial epithelial cells.
CC {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:20558631}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12775711}.
CC -!- DISEASE: Asthma-related traits 7 (ASRT7) [MIM:611960]: Asthma-related
CC traits include clinical symptoms of asthma, such as coughing, wheezing,
CC dyspnea, bronchial hyperresponsiveness as assessed by methacholine
CC challenge test, serum IgE levels, atopy and atopic dermatitis.
CC {ECO:0000269|PubMed:18403759}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial
CC psychotic disorder or group of disorders characterized by disturbances
CC in the form and content of thought (e.g. delusions, hallucinations), in
CC mood (e.g. inappropriate affect), in sense of self and relationship to
CC the external world (e.g. loss of ego boundaries, withdrawal), and in
CC behavior (e.g bizarre or apparently purposeless behavior). Although it
CC affects emotions, it is distinguished from mood disorders in which such
CC disturbances are primary. Similarly, there may be mild impairment of
CC cognitive function, and it is distinguished from the dementias in which
CC disturbed cognitive function is considered primary. Some patients
CC manifest schizophrenic as well as bipolar disorder symptoms and are
CC often given the diagnosis of schizoaffective disorder.
CC {ECO:0000269|PubMed:17160890, ECO:0000269|PubMed:20051317}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family, Leu-
CC 140 is present instead of the conserved Glu which is an active site
CC residue. Therefore this protein lacks chitinase activity.
CC {ECO:0000305}.
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DR EMBL; M80927; AAA16074.1; -; mRNA.
DR EMBL; Y08374; CAA69661.1; -; Genomic_DNA.
DR EMBL; Y08375; CAA69661.1; JOINED; Genomic_DNA.
DR EMBL; Y08376; CAA69661.1; JOINED; Genomic_DNA.
DR EMBL; Y08377; CAA69661.1; JOINED; Genomic_DNA.
DR EMBL; Y08378; CAA69661.1; JOINED; Genomic_DNA.
DR EMBL; BT007223; AAP35887.1; -; mRNA.
DR EMBL; AK312911; BAG35757.1; -; mRNA.
DR EMBL; CH471067; EAW91467.1; -; Genomic_DNA.
DR EMBL; BC008568; AAH08568.1; -; mRNA.
DR EMBL; BC038354; AAH38354.1; -; mRNA.
DR EMBL; BC039132; AAH39132.1; -; mRNA.
DR CCDS; CCDS1435.1; -.
DR PIR; A49562; A49562.
DR RefSeq; NP_001267.2; NM_001276.2.
DR PDB; 1HJV; X-ray; 2.75 A; A/B/C/D=22-383.
DR PDB; 1HJW; X-ray; 2.30 A; A/B=22-383.
DR PDB; 1HJX; X-ray; 1.85 A; A/B/C/D=22-383.
DR PDB; 1NWR; X-ray; 2.70 A; A/B/C/D=22-383.
DR PDB; 1NWS; X-ray; 2.70 A; A/B/C/D=22-383.
DR PDB; 1NWT; X-ray; 2.50 A; A/B/C/D=22-383.
DR PDB; 1NWU; X-ray; 2.20 A; A/B/C/D=22-383.
DR PDB; 7CJ2; X-ray; 2.70 A; A/B=22-383.
DR PDBsum; 1HJV; -.
DR PDBsum; 1HJW; -.
DR PDBsum; 1HJX; -.
DR PDBsum; 1NWR; -.
DR PDBsum; 1NWS; -.
DR PDBsum; 1NWT; -.
DR PDBsum; 1NWU; -.
DR PDBsum; 7CJ2; -.
DR AlphaFoldDB; P36222; -.
DR SMR; P36222; -.
DR BioGRID; 107540; 15.
DR IntAct; P36222; 10.
DR STRING; 9606.ENSP00000255409; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR UniLectin; P36222; -.
DR GlyGen; P36222; 2 sites.
DR iPTMnet; P36222; -.
DR PhosphoSitePlus; P36222; -.
DR BioMuta; CHI3L1; -.
DR DMDM; 84028186; -.
DR EPD; P36222; -.
DR jPOST; P36222; -.
DR MassIVE; P36222; -.
DR PaxDb; P36222; -.
DR PeptideAtlas; P36222; -.
DR PRIDE; P36222; -.
DR ProteomicsDB; 55174; -.
DR ABCD; P36222; 3 sequenced antibodies.
DR Antibodypedia; 34542; 455 antibodies from 36 providers.
DR DNASU; 1116; -.
DR Ensembl; ENST00000255409.8; ENSP00000255409.3; ENSG00000133048.13.
DR GeneID; 1116; -.
DR KEGG; hsa:1116; -.
DR MANE-Select; ENST00000255409.8; ENSP00000255409.3; NM_001276.4; NP_001267.2.
DR UCSC; uc001gzi.3; human.
DR CTD; 1116; -.
DR DisGeNET; 1116; -.
DR GeneCards; CHI3L1; -.
DR HGNC; HGNC:1932; CHI3L1.
DR HPA; ENSG00000133048; Tissue enhanced (brain, liver).
DR MalaCards; CHI3L1; -.
DR MIM; 181500; phenotype.
DR MIM; 601525; gene.
DR MIM; 611960; phenotype.
DR neXtProt; NX_P36222; -.
DR OpenTargets; ENSG00000133048; -.
DR PharmGKB; PA26463; -.
DR VEuPathDB; HostDB:ENSG00000133048; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000161815; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; P36222; -.
DR OMA; HRLLGQQ; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; P36222; -.
DR TreeFam; TF315610; -.
DR PathwayCommons; P36222; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P36222; -.
DR SIGNOR; P36222; -.
DR BioGRID-ORCS; 1116; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; CHI3L1; human.
DR EvolutionaryTrace; P36222; -.
DR GeneWiki; CHI3L1; -.
DR GenomeRNAi; 1116; -.
DR Pharos; P36222; Tbio.
DR PRO; PR:P36222; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P36222; protein.
DR Bgee; ENSG00000133048; Expressed in pericardium and 180 other tissues.
DR ExpressionAtlas; P36222; baseline and differential.
DR Genevisible; P36222; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; NAS:UniProtKB.
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; IEP:UniProtKB.
DR GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0070555; P:response to interleukin-1; IEP:UniProtKB.
DR GO; GO:0070741; P:response to interleukin-6; IEP:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEP: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; Antimicrobial; Apoptosis; Asthma; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Inflammatory response; Lectin; Reference proteome;
KW Schizophrenia; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2375755,
FT ECO:0000269|PubMed:9492324"
FT CHAIN 22..383
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000011965"
FT DOMAIN 22..383
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 324..338
FT /note="Important for AKT1 activation and IL8 production"
FT /evidence="ECO:0000250"
FT BINDING 70..71
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 97..100
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 141
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 204..207
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 263
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT BINDING 352
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12775711"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 300..364
FT VARIANT 145
FT /note="R -> G (in dbSNP:rs880633)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_019838"
FT VARIANT 311
FT /note="I -> T (in dbSNP:rs1049407)"
FT /evidence="ECO:0000269|PubMed:8245017,
FT ECO:0000269|PubMed:9244440"
FT /id="VAR_019839"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1HJX"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1NWU"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1HJX"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1NWU"
FT HELIX 147..165
FT /evidence="ECO:0007829|PDB:1HJX"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1NWU"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1NWU"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 254..270
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1HJX"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1HJX"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1HJX"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1HJX"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1HJX"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:1HJX"
SQ SEQUENCE 383 AA; 42625 MW; 6C9EF133BDC7C2D1 CRC64;
MGVKASQTGF VVLVLLQCCS AYKLVCYYTS WSQYREGDGS CFPDALDRFL CTHIIYSFAN
ISNDHIDTWE WNDVTLYGML NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SNTQSRRTFI
KSVPPFLRTH GFDGLDLAWL YPGRRDKQHF TTLIKEMKAE FIKEAQPGKK QLLLSAALSA
GKVTIDSSYD IAKISQHLDF ISIMTYDFHG AWRGTTGHHS PLFRGQEDAS PDRFSNTDYA
VGYMLRLGAP ASKLVMGIPT FGRSFTLASS ETGVGAPISG PGIPGRFTKE AGTLAYYEIC
DFLRGATVHR ILGQQVPYAT KGNQWVGYDD QESVKSKVQY LKDRQLAGAM VWALDLDDFQ
GSFCGQDLRF PLTNAIKDAL AAT
