CH3L1_PIG
ID CH3L1_PIG Reviewed; 383 AA.
AC Q29411; Q5UC99;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=38 kDa heparin-binding glycoprotein;
DE AltName: Full=Signal-processing protein;
DE AltName: Full=gp38k;
DE Flags: Precursor;
GN Name=CHI3L1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-36; 92-105; 183-201;
RP 272-278; 292-206 AND 343-362, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Smooth muscle;
RX PubMed=7768902; DOI=10.1074/jbc.270.22.13076;
RA Shackelton L.M., Mann D.M., Millis A.J.T.;
RT "Identification of a 38-kDa heparin-binding glycoprotein (gp38k) in
RT differentiating vascular smooth muscle cells as a member of a group of
RT proteins associated with tissue remodeling.";
RL J. Biol. Chem. 270:13076-13083(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-383, AND X-RAY CRYSTALLOGRAPHY (2.1
RP ANGSTROMS) OF 22-383.
RC TISSUE=Mammary gland;
RA Baskar Singh S., Srivastava D.B., Ethayathulla A.S., Sharma S.,
RA Srinivasan A., Singh T.P.;
RT "Crystal structure of a porcine 40 kDa signalling protein at 2.89A
RT resolution.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=3086326; DOI=10.1002/jcp.1041270304;
RA Millis A.J.T., Hoyle M., Kent L.;
RT "In vitro expression of a 38,000 dalton heparin-binding glycoprotein by
RT morphologically differentiated smooth muscle cells.";
RL J. Cell. Physiol. 127:366-372(1986).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12799184; DOI=10.1016/s0014-4827(03)00069-7;
RA Nishikawa K.C., Millis A.J.T.;
RT "gp38k (CHI3L1) is a novel adhesion and migration factor for vascular
RT cells.";
RL Exp. Cell Res. 287:79-87(2003).
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). Stimulates migration and adhesion of cultured vascular
CC smooth muscle cells. {ECO:0000250, ECO:0000269|PubMed:12799184}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:3086326, ECO:0000269|PubMed:7768902}. Cytoplasm
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in smooth muscle cells in atherosclerotic
CC plaques. Detected in regions of vascular occlusion in the aorta.
CC {ECO:0000269|PubMed:12799184, ECO:0000269|PubMed:7768902}.
CC -!- INDUCTION: Up-regulated in cultured aortic smooth muscle cells upon
CC transition to a nodular, multilayered culture.
CC {ECO:0000269|PubMed:7768902}.
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=AAV30548.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; U19900; AAA86482.1; -; mRNA.
DR EMBL; Z47803; CAA87764.1; -; mRNA.
DR EMBL; AY762599; AAV30548.1; ALT_SEQ; mRNA.
DR PIR; S51327; S51327.
DR RefSeq; NP_001001540.1; NM_001001540.1.
DR PDB; 1XHG; X-ray; 2.90 A; A=22-381.
DR PDB; 1XRV; X-ray; 2.10 A; A=22-381.
DR PDB; 1ZB5; X-ray; 2.45 A; A=22-381.
DR PDB; 1ZBC; X-ray; 2.29 A; A=22-381.
DR PDBsum; 1XHG; -.
DR PDBsum; 1XRV; -.
DR PDBsum; 1ZB5; -.
DR PDBsum; 1ZBC; -.
DR AlphaFoldDB; Q29411; -.
DR SMR; Q29411; -.
DR STRING; 9823.ENSSSCP00000016408; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q29411; -.
DR PaxDb; Q29411; -.
DR PRIDE; Q29411; -.
DR GeneID; 396865; -.
DR KEGG; ssc:396865; -.
DR CTD; 1116; -.
DR eggNOG; KOG2806; Eukaryota.
DR InParanoid; Q29411; -.
DR OrthoDB; 1289629at2759; -.
DR EvolutionaryTrace; Q29411; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:7768902"
FT CHAIN 22..383
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000011967"
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:3086326"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 300..364
FT CONFLICT 69
FT /note="W -> L (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="K -> N (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..141
FT /note="LY -> IS (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="I -> V (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 166..167
FT /note="QA -> LP (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="Q -> R (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> G (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="E -> G (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="V -> A (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..313
FT /note="THRFRD -> VRRPLG (in Ref. 1; AAA86482)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="A -> T (in Ref. 1; AAA86482/CAA87764)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1XRV"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1XRV"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1ZB5"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 254..270
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1XRV"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1XRV"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1XRV"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1XRV"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:1XRV"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:1XRV"
SQ SEQUENCE 383 AA; 42800 MW; FC6F637E1FD8886E CRC64;
MGLRVAQTGF VALVLLQSCA AYKLVCYYTS WSQYREGDGS CFPDAIDPFL CTHIIYSFAN
ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SKTQSRRTFI
KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL TTLVKEMKAE FIREAQAGTE QLLLSAAVSA
GKVAIDRGYD IAQISQHLDF ISLLTYDFHG AWRQTTGHHS PLFRGQEDAS SDRFSNADYA
VSYVLRLGAP ANKLVMGIPT FGRSFTLASS KTDVGAPVSG PGIPGRFTKE KGILAYYEIC
DFLQGATTHR FRDQQVPYAT KGNQWVGYDD QESVKNKAKY LKSRQLAGAM VWALDLDDFR
GNFCGQNLRF PLTSAIKDVL AAA
