CH3L1_BUBBU
ID CH3L1_BUBBU Reviewed; 383 AA.
AC Q7YS85; I6YIV5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=Mammary gland protein 40;
DE AltName: Full=SPB-40;
DE Flags: Precursor;
GN Name=CHI3L1; Synonyms=MGP-40;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Bilgrami S., Saravanan K., Yadav S., Kaur P., Srinivasan A., Singh T.P.;
RT "Buffalo mammary gland protein.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Singh S., Anand V., Jena M.K., Jamwal M., Kumar S., Dang A.K., Malakar D.,
RA Mohanty T.K., Kaushik J.K., Mohanty A.K.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-383, GLYCOSYLATION AT ASN-60,
RP AND DISULFIDE BONDS.
RX PubMed=17401190; DOI=10.1107/s1744309107010445;
RA Ethayathulla A.S., Srivastava D.B., Kumar J., Saravanan K., Bilgrami S.,
RA Sharma S., Kaur P., Srinivasan A., Singh T.P.;
RT "Structure of the buffalo secretory signalling glycoprotein at 2.8 A
RT resolution.";
RL Acta Crystallogr. F 63:258-265(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. Cytoplasm
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic
CC 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 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; AY295929; AAP42568.2; -; mRNA.
DR EMBL; JQ796280; AFN52415.1; -; mRNA.
DR RefSeq; NP_001277897.1; NM_001290968.1.
DR PDB; 1TFV; X-ray; 2.90 A; A=22-381.
DR PDB; 2O9O; X-ray; 2.80 A; A=22-381.
DR PDB; 2QF8; X-ray; 2.80 A; A=22-381.
DR PDB; 4MAV; X-ray; 2.79 A; A=22-381.
DR PDB; 4ML4; X-ray; 2.50 A; A=22-381.
DR PDB; 4MPK; X-ray; 2.65 A; A=22-381.
DR PDB; 4MTV; X-ray; 2.80 A; A=22-381.
DR PDB; 4NSB; X-ray; 3.05 A; A=22-381.
DR PDB; 4Q7N; X-ray; 1.79 A; A=22-381.
DR PDB; 5Z05; X-ray; 1.49 A; A=22-383.
DR PDB; 5Z3S; X-ray; 1.65 A; A=22-383.
DR PDB; 5Z4W; X-ray; 1.79 A; A=22-383.
DR PDBsum; 1TFV; -.
DR PDBsum; 2O9O; -.
DR PDBsum; 2QF8; -.
DR PDBsum; 4MAV; -.
DR PDBsum; 4ML4; -.
DR PDBsum; 4MPK; -.
DR PDBsum; 4MTV; -.
DR PDBsum; 4NSB; -.
DR PDBsum; 4Q7N; -.
DR PDBsum; 5Z05; -.
DR PDBsum; 5Z3S; -.
DR PDBsum; 5Z4W; -.
DR AlphaFoldDB; Q7YS85; -.
DR SMR; Q7YS85; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q7YS85; -.
DR GeneID; 102399197; -.
DR KEGG; bbub:102399197; -.
DR CTD; 1116; -.
DR EvolutionaryTrace; Q7YS85; -.
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; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Inflammatory response; Lectin;
KW Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..383
FT /note="Chitinase-3-like protein 1"
FT /id="PRO_0000077054"
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:17401190"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000269|PubMed:17401190"
FT DISULFID 300..364
FT /evidence="ECO:0000269|PubMed:17401190"
FT CONFLICT 89
FT /note="K -> N (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="F -> Y (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="Y -> W (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="P -> T (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="Q -> N (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="Missing (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="K -> R (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="Q -> R (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="E -> W (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="A -> T (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="N -> S (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="G -> R (in Ref. 1; AAP42568)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5Z05"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2O9O"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4Q7N"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 147..165
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5Z05"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:5Z4W"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4MAV"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 254..270
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5Z05"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4MPK"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:5Z05"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:5Z05"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5Z05"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5Z05"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:5Z05"
SQ SEQUENCE 383 AA; 42935 MW; 8FE18A55F586AF4D CRC64;
MGLRVAQTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHVIYSFAN
ISNNEIDTWE WNDVTLYDTL NTLKNRNPKL KTLLSVGGWN FGSQRFSKIA SKTQSRRTFI
KSVPPFLRTH GFDGLDLAWL YPGWRDKRHL TTLVKEMKAE FVREAQAGTE QLLLSAAVPA
GKIAIDRGYD IAQISRHLDF ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA
VSYMLRLGAP ANKLVMGIPT FGKSYTLASS KTDVGAPISG PGIPGQFTKE KGILAYYEIC
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM VWALDLDDFR
GTFCGQNLAF PLTNAIKDVL AGV
