CH3L1_PONAB
ID CH3L1_PONAB Reviewed; 410 AA.
AC Q5RBP6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chitinase-3-like protein 1;
DE Flags: Precursor;
GN Name=CHI3L1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 167 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; CR858592; CAH90814.1; -; mRNA.
DR RefSeq; NP_001125463.1; NM_001131991.1.
DR AlphaFoldDB; Q5RBP6; -.
DR SMR; Q5RBP6; -.
DR STRING; 9601.ENSPPYP00000000371; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; Q5RBP6; -.
DR GeneID; 100172371; -.
DR KEGG; pon:100172371; -.
DR CTD; 1116; -.
DR eggNOG; KOG2806; Eukaryota.
DR InParanoid; Q5RBP6; -.
DR OrthoDB; 1289629at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
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; 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..48
FT /evidence="ECO:0000250"
FT CHAIN 49..410
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000042788"
FT DOMAIN 49..410
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 351..365
FT /note="Important for AKT1 activation and IL8 production"
FT /evidence="ECO:0000250"
FT BINDING 97..98
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 124..127
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 168
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 231..234
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 290
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 53..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 327..391
FT /evidence="ECO:0000250"
SQ SEQUENCE 410 AA; 45561 MW; DA951C7769571754 CRC64;
MGVKAAQTGI WASQGQSIRV VGFQAQTAHR AICLLGFVVL VLLQCCSAYK LVCYYTSWSQ
YREGDGSCFP DAIDRFLCTH IIYSFANISN DHIDTWEWND VTLYGMLNTL KNRNPNLKTL
LSVGGWNFGS QRFSNIASNT QSRRTFIKSV PPFLRTHGFD GLDLAWLYPG QRDKQHFTTL
IKEMRAEFIK EAQPGKKQLL LSAAVSAGKV TIDSSYDIAK ISQHLDFISI MTYDFHGAWR
GTTGHHSPLF RGQEDASPDR FSNTDYAVGY MLRLEAPASK LVMGIPTFGR SFTLASSETG
VGAPISGPGI PGRFTKEAGT LAYYEICDFL RGATVHRILG QQVPYATKGN QWVGYDDQES
VKSKVQYLKE RQLAGAMVWA LDLDDFQGSF CGQDLRFPLT NAIKDALAAT
