CH3L1_CAPHI
ID CH3L1_CAPHI Reviewed; 383 AA.
AC Q8SPQ0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=BP40;
DE AltName: Full=Mammary gland protein 40;
DE Short=MGP-40;
DE Flags: Precursor;
GN Name=CHI3L1;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND X-RAY
RP CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS.
RC TISSUE=Mammary gland;
RX PubMed=12529329; DOI=10.1074/jbc.m208967200;
RA Mohanty A.K., Singh G., Paramasivam M., Saravanan K., Jabeen T., Sharma S.,
RA Yadav S., Kaur P., Kumar P., Srinivasan A., Singh T.P.;
RT "Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-
RT 40) secreted during involution.";
RL J. Biol. Chem. 278:14451-14460(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 22-381 IN COMPLEXES WITH
RP OLIGOSACCHARIDES, GLYCOSYLATION AT ASN-60, AND DISULFIDE BONDS.
RX PubMed=17372347; DOI=10.1107/s0907444907001631;
RA Kumar J., Ethayathulla A.S., Srivastava D.B., Singh N., Sharma S., Kaur P.,
RA Srinivasan A., Singh T.P.;
RT "Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40)
RT and its functional implications: structures of the native glycoprotein and
RT its four complexes with chitin-like oligosaccharides.";
RL Acta Crystallogr. D 63:437-446(2007).
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:0000269|PubMed:12529329}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic
CC 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 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; AY081150; AAL87007.1; -; mRNA.
DR RefSeq; NP_001272618.1; NM_001285689.1.
DR PDB; 1LJY; X-ray; 2.90 A; A=22-383.
DR PDB; 1SYT; X-ray; 2.60 A; A=22-381.
DR PDB; 1ZBV; X-ray; 3.21 A; A=22-381.
DR PDB; 1ZBW; X-ray; 2.80 A; A=22-381.
DR PDB; 1ZU8; X-ray; 3.05 A; A=22-383.
DR PDB; 2AOS; X-ray; 2.90 A; A=22-381.
DR PDB; 2B31; X-ray; 3.10 A; A=22-381.
DR PDB; 2DSZ; X-ray; 2.35 A; A=22-381.
DR PDB; 2DT0; X-ray; 2.45 A; A=22-381.
DR PDB; 2DT1; X-ray; 2.09 A; A=22-381.
DR PDB; 2DT2; X-ray; 2.90 A; A=22-381.
DR PDB; 2DT3; X-ray; 2.28 A; A=22-381.
DR PDB; 2O92; X-ray; 3.00 A; A=22-381.
DR PDB; 2OLH; X-ray; 2.78 A; A=22-381.
DR PDBsum; 1LJY; -.
DR PDBsum; 1SYT; -.
DR PDBsum; 1ZBV; -.
DR PDBsum; 1ZBW; -.
DR PDBsum; 1ZU8; -.
DR PDBsum; 2AOS; -.
DR PDBsum; 2B31; -.
DR PDBsum; 2DSZ; -.
DR PDBsum; 2DT0; -.
DR PDBsum; 2DT1; -.
DR PDBsum; 2DT2; -.
DR PDBsum; 2DT3; -.
DR PDBsum; 2O92; -.
DR PDBsum; 2OLH; -.
DR AlphaFoldDB; Q8SPQ0; -.
DR SMR; Q8SPQ0; -.
DR STRING; 9925.ENSCHIP00000001773; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q8SPQ0; -.
DR PRIDE; Q8SPQ0; -.
DR GeneID; 100860825; -.
DR KEGG; chx:100860825; -.
DR CTD; 1116; -.
DR OrthoDB; 1289629at2759; -.
DR EvolutionaryTrace; Q8SPQ0; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Apoptosis; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Inflammatory response; Lectin; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:12529329"
FT CHAIN 22..383
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000011964"
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:17372347"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000269|PubMed:17372347"
FT DISULFID 300..364
FT /evidence="ECO:0000269|PubMed:17372347"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2DT1"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2DT3"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2DT1"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2OLH"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1LJY"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 254..270
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2DT1"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:2DT1"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:2DT1"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2DT1"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:2DT1"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:2DT1"
SQ SEQUENCE 383 AA; 42894 MW; 17655ED4BE4E9F5F CRC64;
MGLRASGTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHIIYSFAN
ISNNEIDTWE WNDVTLYDTL NTLKNRNPKL KTLLSVGGWN FGPERFSKIA SKTQSRRTFI
KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL TGLVKEMKAE FAREAQAGTE RLLLSAAVSA
GKIAIDRGYD IAQISRHLDF ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA
VSYMLRLGAP ANKLVMGIPT FGRSFTLASS KTDVGAPISG PGIPGRFTKE KGILAYYEIC
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM VWALDLDDFR
GTFCGQNLTF PLTSAVKDVL AEV
