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O35744

- CHIL3_MOUSE

UniProt

O35744 - CHIL3_MOUSE

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Protein

Chitinase-like protein 3

Gene

Chil3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy.3 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Kineticsi

4-methylumbelliferone-N-acetylglucosamine (MU-(GlcNAc)1) is a GlcNAc2 analog.

  1. KM=120.8 µM for 4-methylumbelliferone-N-acetylglucosamine (at pH 4-4.5)1 Publication

Vmax=0.023 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 4.5-5.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401ChitooligosaccharideCurated
Binding sitei213 – 2131ChitooligosaccharideCurated

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: MGI
  2. carbohydrate binding Source: MGI
  3. chitin binding Source: UniProtKB-KW

GO - Biological processi

  1. chitin catabolic process Source: InterPro
  2. inflammatory response Source: MGI
  3. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Inflammatory response, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding, Lectin

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase-like protein 3 (EC:3.2.1.52)
Alternative name(s):
Beta-N-acetylhexosaminidase Ym1
Chitinase-3-like protein 3
ECF-L
Eosinophil chemotactic cytokine
Secreted protein Ym1
Gene namesi
Name:Chil3
Synonyms:Chi3l3, Ym1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1330860. Chil3.

Subcellular locationi

Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule
Note: Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in cytoplasmic granules in peritoneal neutrophils. Detected in needle-shaped crystals present in the cytoplasm of bone marrow macrophages.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic membrane-bounded vesicle Source: MGI
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. extracellular region Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21212 PublicationsAdd
BLAST
Chaini22 – 398377Chitinase-like protein 3PRO_0000011970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 51
Disulfide bondi49 ↔ 394
Disulfide bondi307 ↔ 372

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO35744.
PaxDbiO35744.
PRIDEiO35744.

Expressioni

Tissue specificityi

Expressed in peritoneal cavity macrophages and in peritoneal and bone marrow-derived neutrophils. Abundantly expressed in bone marrow, with moderate levels detected in gastric antrum, spleen and in alveolar macrophages in lung. Not detected in brain, heart, liver, kidney, stomach, intestine, skeletal muscle, ovary, testis, thymus and lymph nodes (at protein level). Detected at low levels in bone marrow, spleen, thymus and lung. Barely detectable in intestine, kidney and coecum.6 Publications

Developmental stagei

In yolk sac, first detected at low levels at E8.5, with significant expression detected at E10.5 in myeloid precursor cells. In liver, expressed from E16.5 to P7.5 with highest levels detected from E18.5 to P0.5. In spleen, first detected at E16.5, with peak levels detected at E18.5 and P0.5 and expression persisting through the spleen maturation to the adult stage. In bone marrow, high expression levels detected from E16.5 until adulthood. In lung, first detected around the time of birth, with levels increasing significantly from P14.5 towards adulthood.1 Publication

Inductioni

Up-regulated in response to IL3 and IL4, during the inflammatory response and upon parasitic infection.4 Publications

Gene expression databases

BgeeiO35744.
CleanExiMM_CHI3L3.
GenevestigatoriO35744.

Interactioni

Protein-protein interaction databases

IntActiO35744. 1 interaction.
MINTiMINT-4090737.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297
Helixi30 – 345
Helixi37 – 393
Helixi43 – 453
Turni48 – 503
Beta strandi52 – 6211
Beta strandi65 – 673
Helixi73 – 8210
Helixi83 – 853
Beta strandi91 – 977
Turni99 – 1013
Helixi104 – 1107
Helixi113 – 12917
Beta strandi134 – 1385
Beta strandi142 – 1443
Helixi150 – 17324
Beta strandi179 – 1846
Helixi188 – 1947
Helixi197 – 2037
Beta strandi205 – 2095
Helixi217 – 2193
Helixi236 – 2405
Helixi243 – 25210
Helixi257 – 2593
Beta strandi260 – 27415
Beta strandi284 – 2885
Turni293 – 2953
Beta strandi300 – 3023
Helixi303 – 3119
Beta strandi315 – 3195
Turni320 – 3234
Beta strandi324 – 3296
Beta strandi332 – 3354
Helixi339 – 35113
Beta strandi356 – 3605
Helixi362 – 3643
Turni370 – 3723
Helixi378 – 3869

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9LX-ray2.50A22-398[»]
1VF8X-ray1.31A22-398[»]
ProteinModelPortaliO35744.
SMRiO35744. Positions 22-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35744.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3325.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiO35744.
KOiK17524.
OMAiIISYWKD.
OrthoDBiEOG7ZGX3G.
PhylomeDBiO35744.
TreeFamiTF315610.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35744-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKLILVTGL AILLNVQLGS SYQLMCYYTS WAKDRPIEGS FKPGNIDPCL
60 70 80 90 100
CTHLIYAFAG MQNNEITYTH EQDLRDYEAL NGLKDKNTEL KTLLAIGGWK
110 120 130 140 150
FGPAPFSAMV STPQNRQIFI QSVIRFLRQY NFDGLNLDWQ YPGSRGSPPK
160 170 180 190 200
DKHLFSVLVK EMRKAFEEES VEKDIPRLLL TSTGAGIIDV IKSGYKIPEL
210 220 230 240 250
SQSLDYIQVM TYDLHDPKDG YTGENSPLYK SPYDIGKSAD LNVDSIISYW
260 270 280 290 300
KDHGAASEKL IVGFPAYGHT FILSDPSKTG IGAPTISTGP PGKYTDESGL
310 320 330 340 350
LAYYEVCTFL NEGATEVWDA PQEVPYAYQG NEWVGYDNVR SFKLKAQWLK
360 370 380 390
DNNLGGAVVW PLDMDDFSGS FCHQRHFPLT STLKGDLNIH SASCKGPY
Length:398
Mass (Da):44,458
Last modified:March 1, 2001 - v2
Checksum:iC11187661B99D1D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051P → S no nucleotide entry (PubMed:9828134)Curated
Sequence conflicti105 – 1051P → S in BAA13458. (PubMed:10625674)Curated
Sequence conflicti257 – 2571S → P in BAE23385. (PubMed:11297523)Curated
Sequence conflicti361 – 3611P → R no nucleotide entry (PubMed:9828134)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D87757 mRNA. Translation: BAA13458.2.
M94584 mRNA. Translation: AAB62394.2.
AK137503 mRNA. Translation: BAE23385.1.
AK154420 mRNA. Translation: BAE32572.1.
BC061154 mRNA. Translation: AAH61154.1.
U56900 mRNA. Translation: AAB01230.1.
CCDSiCCDS17718.1.
PIRiS27879.
RefSeqiNP_034022.2. NM_009892.2.
UniGeneiMm.387173.

Genome annotation databases

EnsembliENSMUST00000063062; ENSMUSP00000053923; ENSMUSG00000040809.
GeneIDi12655.
KEGGimmu:12655.
UCSCiuc008qvw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D87757 mRNA. Translation: BAA13458.2 .
M94584 mRNA. Translation: AAB62394.2 .
AK137503 mRNA. Translation: BAE23385.1 .
AK154420 mRNA. Translation: BAE32572.1 .
BC061154 mRNA. Translation: AAH61154.1 .
U56900 mRNA. Translation: AAB01230.1 .
CCDSi CCDS17718.1.
PIRi S27879.
RefSeqi NP_034022.2. NM_009892.2.
UniGenei Mm.387173.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E9L X-ray 2.50 A 22-398 [» ]
1VF8 X-ray 1.31 A 22-398 [» ]
ProteinModelPortali O35744.
SMRi O35744. Positions 22-394.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O35744. 1 interaction.
MINTi MINT-4090737.

Chemistry

ChEMBLi CHEMBL1795141.

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

Proteomic databases

MaxQBi O35744.
PaxDbi O35744.
PRIDEi O35744.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063062 ; ENSMUSP00000053923 ; ENSMUSG00000040809 .
GeneIDi 12655.
KEGGi mmu:12655.
UCSCi uc008qvw.2. mouse.

Organism-specific databases

CTDi 12655.
MGIi MGI:1330860. Chil3.

Phylogenomic databases

eggNOGi COG3325.
GeneTreei ENSGT00550000074323.
HOGENOMi HOG000111109.
HOVERGENi HBG011684.
InParanoidi O35744.
KOi K17524.
OMAi IISYWKD.
OrthoDBi EOG7ZGX3G.
PhylomeDBi O35744.
TreeFami TF315610.

Miscellaneous databases

EvolutionaryTracei O35744.
NextBioi 281876.
PROi O35744.
SOURCEi Search...

Gene expression databases

Bgeei O35744.
CleanExi MM_CHI3L3.
Genevestigatori O35744.

Family and domain databases

Gene3Di 3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
SMARTi SM00636. Glyco_18. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic characterization of the murine Ym1 gene and identification of a cluster of highly homologous genes."
    Jin H.M., Copeland N.G., Gilbert D.J., Jenkins N.A., Kirkpatrick R.B., Rosenberg M.
    Genomics 54:316-322(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ.
  2. "Identification of a novel eosinophil chemotactic cytokine (ECF-L) as a chitinase family protein."
    Owhashi M., Arita H., Hayai N.
    J. Biol. Chem. 275:1279-1286(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-39, FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Tissue: Bone marrow.
  3. "A macrophage protein, Ym1, transiently expressed during inflammation is a novel mammalian lectin."
    Chang N.-C.A., Hung S.-I., Hwa K.-Y., Kato I., Chen J.-E., Liu C.-H., Chang A.C.
    J. Biol. Chem. 276:17497-17506(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-48; 109-134; 162-192 AND 210-225, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Tissue: Macrophage.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Bone and Dendritic cell.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart and Lung.
  6. "Mouse chitinase-related protein mRNA (MCRP), partial cds."
    Shmelkov S.V., Zinovjeva M.V., Belyavsky A.V.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-398.
    Strain: CBA.
    Tissue: Bone marrow.
  7. "Ym1 is a neutrophil granule protein that crystallizes in p47phox-deficient mice."
    Harbord M., Novelli M., Canas B., Power D., Davis C., Godovac-Zimmermann J., Roes J., Segal A.W.
    J. Biol. Chem. 277:5468-5475(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "TH2 cytokines and allergic challenge induce Ym1 expression in macrophages by a STAT6-dependent mechanism."
    Welch J.S., Escoubet-Lozach L., Sykes D.B., Liddiard K., Greaves D.R., Glass C.K.
    J. Biol. Chem. 277:42821-42829(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IL3 AND IL4.
  9. "Transient expression of Ym1, a heparin-binding lectin, during developmental hematopoiesis and inflammation."
    Hung S.I., Chang A.C., Kato I., Chang N.C.
    J. Leukoc. Biol. 72:72-82(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
  10. "Cellular expression of murine Ym1 and Ym2, chitinase family proteins, as revealed by in situ hybridization and immunohistochemistry."
    Nio J., Fujimoto W., Konno A., Kon Y., Owhashi M., Iwanaga T.
    Histochem. Cell Biol. 121:473-482(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "The crystal structure of a novel mammalian lectin, Ym1, suggests a saccharide binding site."
    Sun Y.-J., Chang N.-C.A., Hung S.-I., Chang A.C., Chou C.-C., Hsiao C.-D.
    J. Biol. Chem. 276:17507-17514(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-398, DISULFIDE BONDS.
  12. "The crystal structure of Ym1 at 1.31 A resolution."
    Tsai M.L., Liaw S.H., Chang N.C.
    J. Struct. Biol. 148:290-296(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 22-398, DISULFIDE BONDS.

Entry informationi

Entry nameiCHIL3_MOUSE
AccessioniPrimary (citable) accession number: O35744
Secondary accession number(s): P70201
, Q3U462, Q3UV87, Q61201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3