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Chitinase-3-like protein 1 (Secretory glycoprotein of 40 kDa) (Signal-processing protein)

 CH3L1_SHEEP             Reviewed;         361 AA.
Q6TMG6;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
28-MAR-2018, entry version 86.
RecName: Full=Chitinase-3-like protein 1;
AltName: Full=Secretory glycoprotein of 40 kDa;
AltName: Full=Signal-processing protein;
Name=CHI3L1;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
Das U., Saravanan K., Hariprasad R.G., Singh T.P., Srinivasan A.;
"Signal processing protein from sheep mammary gland.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), PROTEIN SEQUENCE OF N-TERMINUS,
IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-39, AND
DISULFIDE BONDS.
PubMed=16859926; DOI=10.1016/j.jsb.2006.05.008;
Srivastava D.B., Ethayathulla A.S., Kumar J., Singh N., Sharma S.,
Das U., Srinivasan A., Singh T.P.;
"Crystal structure of a secretory signalling glycoprotein from sheep
at 2.0A resolution.";
J. Struct. Biol. 156:505-516(2006).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH
N-ACETYLGLUCOSAMINE OLIGOSACCHARIDES, PROTEIN SEQUENCE OF N-TERMINUS,
IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-39, AND SUBCELLULAR LOCATION.
PubMed=17188513; DOI=10.1016/j.jsb.2006.11.002;
Srivastava D.B., Ethayathulla A.S., Kumar J., Somvanshi R.K.,
Sharma S., Dey S., Singh T.P.;
"Carbohydrate binding properties and carbohydrate induced
conformational switch in sheep secretory glycoprotein (SPS-40):
crystal structures of four complexes of SPS-40 with chitin-like
oligosaccharides.";
J. Struct. Biol. 158:255-266(2007).
-!- FUNCTION: Carbohydrate-binding lectin with a preference for
chitin. Has no chitinase activity. May play a role in tissue
remodeling and in the capacity of cells to respond to and cope
with changes in their environment. Plays a role in T-helper cell
type 2 (Th2) inflammatory response and IL-13-induced inflammation,
regulating allergen sensitization, inflammatory cell apoptosis,
dendritic cell accumulation and M2 macrophage differentiation.
Facilitates invasion of pathogenic enteric bacteria into colonic
mucosa and lymphoid organs. Mediates activation of AKT1 signaling
pathway and subsequent IL8 production in colonic epithelial cells.
Regulates antibacterial responses in lung by contributing to
macrophage bacterial killing, controlling bacterial dissemination
and augmenting host tolerance. Also regulates hyperoxia-induced
injury, inflammation and epithelial apoptosis in lung (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:17188513}. Cytoplasm {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000250}. Endoplasmic reticulum
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in mammary gland.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
{ECO:0000305}.
-!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family,
Leu-119 is present instead of the conserved Glu which is an active
site residue. Therefore this protein lacks chitinase activity.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY392761; AAQ94054.1; -; mRNA.
UniGene; Oar.1069; -.
PDB; 1SR0; X-ray; 3.05 A; A=1-361.
PDB; 1ZBK; X-ray; 2.90 A; A=1-360.
PDB; 1ZL1; X-ray; 3.50 A; A=1-360.
PDB; 2DPE; X-ray; 2.07 A; A=1-361.
PDB; 2DSU; X-ray; 2.20 A; A=1-361.
PDB; 2DSV; X-ray; 2.54 A; A=1-361.
PDB; 2DSW; X-ray; 2.80 A; A=1-361.
PDB; 2FDM; X-ray; 3.00 A; A=1-360.
PDB; 2G41; X-ray; 3.00 A; A=1-361.
PDB; 2G8Z; X-ray; 2.50 A; A=1-361.
PDB; 2PI6; X-ray; 1.65 A; A=1-361.
PDB; 5Z4V; X-ray; 1.65 A; A=1-361.
PDBsum; 1SR0; -.
PDBsum; 1ZBK; -.
PDBsum; 1ZL1; -.
PDBsum; 2DPE; -.
PDBsum; 2DSU; -.
PDBsum; 2DSV; -.
PDBsum; 2DSW; -.
PDBsum; 2FDM; -.
PDBsum; 2G41; -.
PDBsum; 2G8Z; -.
PDBsum; 2PI6; -.
PDBsum; 5Z4V; -.
ProteinModelPortal; Q6TMG6; -.
SMR; Q6TMG6; -.
CAZy; GH18; Glycoside Hydrolase Family 18.
iPTMnet; Q6TMG6; -.
PRIDE; Q6TMG6; -.
HOVERGEN; HBG011684; -.
EvolutionaryTrace; Q6TMG6; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; ISS:UniProtKB.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB.
GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB.
GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB.
Gene3D; 3.10.50.10; -; 1.
InterPro; IPR028538; CHI3L1.
InterPro; IPR011583; Chitinase_II.
InterPro; IPR029070; Chitinase_insertion_sf.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR11177:SF202; PTHR11177:SF202; 1.
Pfam; PF00704; Glyco_hydro_18; 1.
SMART; SM00636; Glyco_18; 1.
SUPFAM; SSF51445; SSF51445; 2.
SUPFAM; SSF54556; SSF54556; 1.
1: Evidence at protein level;
3D-structure; Antimicrobial; Apoptosis; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Inflammatory response; Lectin; Reference proteome;
Secreted.
CHAIN 1 361 Chitinase-3-like protein 1.
/FTId=PRO_0000077055.
REGION 49 50 Chitooligosaccharide binding.
REGION 76 79 Chitooligosaccharide binding.
REGION 183 186 Chitooligosaccharide binding.
REGION 302 316 Important for AKT1 activation and IL8
production. {ECO:0000250}.
BINDING 120 120 Chitooligosaccharide.
BINDING 241 241 Chitooligosaccharide.
BINDING 330 330 Chitooligosaccharide.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16859926,
ECO:0000269|PubMed:17188513}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 5 30
DISULFID 278 342
STRAND 2 8 {ECO:0000244|PDB:2PI6}.
HELIX 9 13 {ECO:0000244|PDB:2PI6}.
HELIX 16 18 {ECO:0000244|PDB:2PI6}.
HELIX 22 24 {ECO:0000244|PDB:2PI6}.
TURN 27 29 {ECO:0000244|PDB:2PI6}.
STRAND 31 41 {ECO:0000244|PDB:2PI6}.
STRAND 44 46 {ECO:0000244|PDB:2PI6}.
HELIX 52 65 {ECO:0000244|PDB:2PI6}.
STRAND 70 76 {ECO:0000244|PDB:2PI6}.
TURN 77 79 {ECO:0000244|PDB:2PI6}.
HELIX 82 89 {ECO:0000244|PDB:2PI6}.
HELIX 92 109 {ECO:0000244|PDB:2PI6}.
STRAND 112 117 {ECO:0000244|PDB:2PI6}.
HELIX 123 125 {ECO:0000244|PDB:2PI6}.
HELIX 126 144 {ECO:0000244|PDB:2PI6}.
TURN 145 147 {ECO:0000244|PDB:1SR0}.
STRAND 152 157 {ECO:0000244|PDB:2PI6}.
HELIX 161 167 {ECO:0000244|PDB:2PI6}.
HELIX 170 176 {ECO:0000244|PDB:2PI6}.
STRAND 178 182 {ECO:0000244|PDB:2PI6}.
STRAND 192 194 {ECO:0000244|PDB:2G8Z}.
STRAND 205 207 {ECO:0000244|PDB:2PI6}.
STRAND 211 214 {ECO:0000244|PDB:2FDM}.
HELIX 215 224 {ECO:0000244|PDB:2PI6}.
HELIX 229 231 {ECO:0000244|PDB:2PI6}.
STRAND 232 248 {ECO:0000244|PDB:2PI6}.
STRAND 255 259 {ECO:0000244|PDB:2PI6}.
TURN 264 266 {ECO:0000244|PDB:2PI6}.
STRAND 271 273 {ECO:0000244|PDB:2PI6}.
HELIX 274 280 {ECO:0000244|PDB:2PI6}.
TURN 281 283 {ECO:0000244|PDB:2PI6}.
STRAND 285 289 {ECO:0000244|PDB:2PI6}.
TURN 290 293 {ECO:0000244|PDB:2PI6}.
STRAND 294 299 {ECO:0000244|PDB:2PI6}.
STRAND 302 305 {ECO:0000244|PDB:2PI6}.
HELIX 309 321 {ECO:0000244|PDB:2PI6}.
STRAND 325 330 {ECO:0000244|PDB:2PI6}.
HELIX 332 334 {ECO:0000244|PDB:2PI6}.
STRAND 337 339 {ECO:0000244|PDB:2PI6}.
STRAND 341 344 {ECO:0000244|PDB:2PI6}.
HELIX 349 359 {ECO:0000244|PDB:2PI6}.
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


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