CH3L1_RAT
ID CH3L1_RAT Reviewed; 381 AA.
AC Q9WTV1; Q5BJR6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=Cartilage glycoprotein 39;
DE Short=CGP-39;
DE Short=GP-39;
DE Flags: Precursor;
GN Name=Chi3l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-371.
RC STRAIN=Lewis;
RA Wendling U., Boots A.M.H., van Eden W.;
RT "Cloning of the rat homologue of human cartilage glycoprotein-39 a
RT potential autoantigen in arthritis.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family, Leu-
CC 138 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=AAH91365.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC091365; AAH91365.1; ALT_INIT; mRNA.
DR EMBL; AF062038; AAD22610.1; -; mRNA.
DR RefSeq; NP_001296749.1; NM_001309820.1.
DR RefSeq; NP_446012.2; NM_053560.2.
DR AlphaFoldDB; Q9WTV1; -.
DR SMR; Q9WTV1; -.
DR STRING; 10116.ENSRNOP00000065787; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q9WTV1; 3 sites.
DR PaxDb; Q9WTV1; -.
DR PRIDE; Q9WTV1; -.
DR Ensembl; ENSRNOT00000078599; ENSRNOP00000074871; ENSRNOG00000053272.
DR GeneID; 89824; -.
DR KEGG; rno:89824; -.
DR UCSC; RGD:620874; rat.
DR CTD; 1116; -.
DR RGD; 620874; Chi3l1.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000161815; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q9WTV1; -.
DR OMA; HRLLGQQ; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; Q9WTV1; -.
DR TreeFam; TF315610; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9WTV1; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000053272; Expressed in lung and 18 other tissues.
DR Genevisible; Q9WTV1; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; ISS: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:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
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; 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; 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; ISS: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 2: Evidence at transcript level;
KW Antimicrobial; Apoptosis; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Inflammatory response; Lectin; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..381
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000011968"
FT DOMAIN 20..381
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 322..336
FT /note="Important for AKT1 activation and IL8 production"
FT /evidence="ECO:0000250"
FT BINDING 68..69
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 95..98
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 139
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 202..205
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 350
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 24..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 298..362
FT /evidence="ECO:0000250"
FT CONFLICT 277
FT /note="T -> S (in Ref. 2; AAD22610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42392 MW; E40BD71A658A2EBB CRC64;
MTLQLPGFAV LMLLQSCSAY KLVCYYTNWS QYREGNGSCF PDALDHSLCT HIIYSFANIS
NNKLSTSEWN DVTLYGMLNT LKTRNPRLKT LLSVGGWSFG SERFSRIVSN AKSRKTFVQS
VAPFLRTYGF DGLDLAWLYP GPKDKQHFTT LIKELKAEFT KEVQPGTEKL LLSAAVSAGK
VTLDSGYDVA QIAQHLDFIN LMTYDFHGTW RHTTGHHSPL FRGQQDTGPD RFSNVDYGVG
YMLRLGAPTN KLVMGIPTFG KSFTLASSEN QVGAPITGSG LPGRYTKEKG TLAYYEICDF
LRGAEVHRIL GQQVPFATKG NQWVGYDDPE SVKNKVKYLK NKQLAGAMVW AVDLDDFRGS
FCGHNVHFPL TNAIKEALAV A
