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Database: UniProt
Entry: Q5RBP6
LinkDB: Q5RBP6
Original site: Q5RBP6 
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   24-JAN-2024, entry version 95.
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   GlyCosmos; Q5RBP6; 1 site, No reported glycans.
DR   GeneID; 100172371; -.
DR   KEGG; pon:100172371; -.
DR   CTD; 1116; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   InParanoid; Q5RBP6; -.
DR   OrthoDB; 1752999at2759; -.
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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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   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   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
//
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