CH3L1_SHEEP
ID CH3L1_SHEEP Reviewed; 361 AA.
AC Q6TMG6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=Secretory glycoprotein of 40 kDa;
DE AltName: Full=Signal-processing protein;
GN Name=CHI3L1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Das U., Saravanan K., Hariprasad R.G., Singh T.P., Srinivasan A.;
RT "Signal processing protein from sheep mammary gland.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), PROTEIN SEQUENCE OF N-TERMINUS,
RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-39, AND DISULFIDE
RP BONDS.
RX PubMed=16859926; DOI=10.1016/j.jsb.2006.05.008;
RA Srivastava D.B., Ethayathulla A.S., Kumar J., Singh N., Sharma S., Das U.,
RA Srinivasan A., Singh T.P.;
RT "Crystal structure of a secretory signalling glycoprotein from sheep at
RT 2.0A resolution.";
RL J. Struct. Biol. 156:505-516(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH N-ACETYLGLUCOSAMINE
RP OLIGOSACCHARIDES, PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS
RP SPECTROMETRY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-39, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17188513; DOI=10.1016/j.jsb.2006.11.002;
RA Srivastava D.B., Ethayathulla A.S., Kumar J., Somvanshi R.K., Sharma S.,
RA Dey S., Singh T.P.;
RT "Carbohydrate binding properties and carbohydrate induced conformational
RT switch in sheep secretory glycoprotein (SPS-40): crystal structures of four
RT complexes of SPS-40 with chitin-like oligosaccharides.";
RL J. Struct. Biol. 158:255-266(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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:17188513}. Cytoplasm {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in mammary gland.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family, Leu-
CC 119 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; AY392761; AAQ94054.1; -; mRNA.
DR PDB; 1SR0; X-ray; 3.05 A; A=1-361.
DR PDB; 1ZBK; X-ray; 2.90 A; A=1-360.
DR PDB; 1ZL1; X-ray; 3.50 A; A=1-360.
DR PDB; 2DPE; X-ray; 2.07 A; A=1-361.
DR PDB; 2DSU; X-ray; 2.20 A; A=1-361.
DR PDB; 2DSV; X-ray; 2.54 A; A=1-361.
DR PDB; 2DSW; X-ray; 2.80 A; A=1-361.
DR PDB; 2FDM; X-ray; 3.00 A; A=1-360.
DR PDB; 2G41; X-ray; 3.00 A; A=1-361.
DR PDB; 2G8Z; X-ray; 2.50 A; A=1-361.
DR PDB; 2PI6; X-ray; 1.65 A; A=1-361.
DR PDB; 5Z4V; X-ray; 1.65 A; A=1-361.
DR PDBsum; 1SR0; -.
DR PDBsum; 1ZBK; -.
DR PDBsum; 1ZL1; -.
DR PDBsum; 2DPE; -.
DR PDBsum; 2DSU; -.
DR PDBsum; 2DSV; -.
DR PDBsum; 2DSW; -.
DR PDBsum; 2FDM; -.
DR PDBsum; 2G41; -.
DR PDBsum; 2G8Z; -.
DR PDBsum; 2PI6; -.
DR PDBsum; 5Z4V; -.
DR AlphaFoldDB; Q6TMG6; -.
DR SMR; Q6TMG6; -.
DR STRING; 9940.ENSOARP00000001430; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q6TMG6; -.
DR eggNOG; KOG2806; Eukaryota.
DR EvolutionaryTrace; Q6TMG6; -.
DR Proteomes; UP000002356; 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 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.
FT CHAIN 1..361
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000077055"
FT DOMAIN 1..361
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 302..316
FT /note="Important for AKT1 activation and IL8 production"
FT /evidence="ECO:0000250"
FT BINDING 49..50
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 76..79
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 120
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 183..186
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 241
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT BINDING 330
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16859926,
FT ECO:0000269|PubMed:17188513"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 5..30
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 278..342
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2PI6"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 31..41
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2PI6"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:2PI6"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1SR0"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2G8Z"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2FDM"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 232..248
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2PI6"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:2PI6"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2PI6"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2PI6"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2PI6"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:2PI6"
SQ SEQUENCE 361 AA; 40563 MW; 8642AF873DC5EE3A CRC64;
YKLICYYTSW SQYREGDGSC FPDAIDPFLC THVIYSFANI SNNEIDTWEW NDVTLYDTLN
TLKNRNPKLK TLLSVGGWNF GPERFSAIAS KTQSRRTFIK SVPPFLRTHG FDGLDLAWLY
PGRRDKRHLT TLVKEMKAEF IREAQAGTEQ LLLSAAVSAG KIAIDRGYDI AQISRHLDFI
SLLTYDFHGA WRQTVGHHSP LFAGNEDASS RFSNADYAVS YMLRLGAPAN KLVMGIPTFG
RSFTLASSKT DVGAPVSGPG VPGRFTKEKG ILAYYEICDF LHGATTHRFR DQQVPYATKG
NQWVAYDDQE SVKNKARYLK NRQLAGAMVW ALDLDDFRGT FCGQNLTFPL TSAVKDVLAE
V
