CH3L1_BOVIN
ID CH3L1_BOVIN Reviewed; 383 AA.
AC P30922; O18949; Q58CW2; Q7YSE8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=39 kDa whey protein;
DE AltName: Full=Cartilage glycoprotein 39;
DE Short=CGP-39;
DE Short=GP-39;
DE AltName: Full=Chitinase-like protein 1;
DE Short=CLP-1;
DE AltName: Full=SPC-40;
DE AltName: Full=Signal-processing protein;
DE Flags: Precursor;
GN Name=CHI3L1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-383.
RC TISSUE=Mammary gland;
RA Srinivasan A., Kumar J., Singh T.P.;
RT "Signal processing protein from bovine mammary gland.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 22-57.
RX PubMed=3122754; DOI=10.1016/0006-291x(88)90524-4;
RA Rejman J.J., Hurley W.L.;
RT "Isolation and characterization of a novel 39 kilodalton whey protein from
RT bovine mammary secretions collected during the nonlactating period.";
RL Biochem. Biophys. Res. Commun. 150:329-334(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-356.
RA Recklies A.D., White C.;
RT "Expression of chitinase-like protein 1 (CLP-1) in bovine chondrocytes.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-383, FUNCTION, GLYCOSYLATION AT
RP ASN-60, AND DISULFIDE BONDS.
RX PubMed=16929095; DOI=10.1107/s0907444906020427;
RA Kumar J., Ethayathulla A.S., Srivastava D.B., Sharma S., Singh S.B.,
RA Srinivasan A., Yadav M.P., Singh T.P.;
RT "Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1
RT Angstrom resolution.";
RL Acta Crystallogr. D 62:953-963(2006).
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, ECO:0000269|PubMed:16929095}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mammary secretions collected during the non-
CC lactating period.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16929095}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46682.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BT021835; AAX46682.1; ALT_INIT; mRNA.
DR EMBL; AY291312; AAP41220.2; -; mRNA.
DR EMBL; AF011373; AAB64304.1; -; mRNA.
DR PIR; A27682; A27682.
DR RefSeq; NP_001073688.1; NM_001080219.1.
DR PDB; 1OWQ; X-ray; 2.00 A; A=22-383.
DR PDB; 2ESC; X-ray; 2.10 A; A=22-383.
DR PDBsum; 1OWQ; -.
DR PDBsum; 2ESC; -.
DR AlphaFoldDB; P30922; -.
DR SMR; P30922; -.
DR STRING; 9913.ENSBTAP00000024253; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; P30922; -.
DR PaxDb; P30922; -.
DR PeptideAtlas; P30922; -.
DR PRIDE; P30922; -.
DR GeneID; 286869; -.
DR KEGG; bta:286869; -.
DR CTD; 1116; -.
DR eggNOG; KOG2806; Eukaryota.
DR InParanoid; P30922; -.
DR OrthoDB; 1289629at2759; -.
DR EvolutionaryTrace; P30922; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
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:0006032; P:chitin catabolic process; IBA:GO_Central.
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:3122754"
FT CHAIN 22..383
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000042787"
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 /evidence="ECO:0000250"
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:16929095"
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:16929095"
FT DISULFID 300..364
FT /evidence="ECO:0000269|PubMed:16929095"
FT CONFLICT 25
FT /note="I -> V (in Ref. 4; AAB64304)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Q -> E (in Ref. 2; AAP41220)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> G (in Ref. 4; AAB64304)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="P -> T (in Ref. 2; AAP41220)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="A -> G (in Ref. 2; AAP41220)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Q -> G (in Ref. 2; AAP41220)"
FT /evidence="ECO:0000305"
FT CONFLICT 226..232
FT /note="QEDASSD -> NSDGSS (in Ref. 2; AAP41220)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..273
FT /note="KTD -> STR (in Ref. 2; AAP41220)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="T -> I (in Ref. 1; AAX46682)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="T -> A (in Ref. 1; AAX46682)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="R -> E (in Ref. 1; AAX46682)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1OWQ"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1OWQ"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 254..270
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1OWQ"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1OWQ"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1OWQ"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1OWQ"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1OWQ"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:1OWQ"
SQ SEQUENCE 383 AA; 43032 MW; 391561804C371A10 CRC64;
MGLRAAHTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHVIYSFAN
ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SKTQSRRTFI
KSVPPFLRTH GFDGLDLAWL YPGWRDKRHL TTLVKEMKAE FVREAQAGTE QLLLSAAVPA
GKIAIDRGYD IAQISRHLDF ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA
VSYMLRLGAP ANKLVMGIPT FGRSYTLASS KTDVGAPISG PGIPGQFTKE KGILAYYEIC
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM VWALDLDDFR
GTFCGQNLTF PLTSAIKDVL ARV
