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Reviewed, UniProtKB/Swiss-Prot Q61362 (CH3L1_MOUSE)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chitinase-3-like protein 1
Alternative name(s):
    Cartilage glycoprotein 39
      Short name=CGP-39
      Short name=GP-39
    BRP39 protein
Gene names
Name: Chi3l1
Synonyms: Brp39
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secretedextracellular space By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 381360Chitinase-3-like protein 1
PRO_0000011966

Regions

Region71 – 722Chitooligosaccharide binding By similarity
Region98 – 1014Chitooligosaccharide binding By similarity
Region205 – 2084Chitooligosaccharide By similarity

Sites

Binding site1421Chitooligosaccharide By similarity
Binding site3531Chitooligosaccharide By similarity

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) By similarity
Disulfide bond26 ↔ 51 By similarity
Disulfide bond301 ↔ 364 By similarity

Experimental info

Sequence conflict3311D → H in CAA63603. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61362-1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: EF6588C5AE9D4450

FASTA38142,979
        10         20         30         40         50         60 
MGMRAALTGF AVLMLLQSCS AYKLVCYFTS WSQYREGVGS FLPDAIQPFL CTHIIYSFAN 

        70         80         90        100        110        120 
ISSDNMLSTW EWNDESNYDK LNKLKTRNTN LKTLLSVGGW KFGEKRFSEI ASNTERRTAF 

       130        140        150        160        170        180 
VRSVAPFLRS YGFDGLDLAW LYPRLRDKQY FSTLIKELNA EFTKEVQPGR EKLLLSAALS 

       190        200        210        220        230        240 
AGKVAIDTGY DIAQIAQHLD FINLMTYDFH GVWRQITGHH SPLFQGQKDT RFDRYSNVNY 

       250        260        270        280        290        300 
AVQYMIRLGA QASKLLMGIP TFGKSFTLAS SENQLGAPIS GEGLPGRFTK EAGTLAYYEI 

       310        320        330        340        350        360 
CDFLKGAEVH RLSNEKVPFA TKGNQWVGYE DKESVKNKVG FLKEKKLAGA MVWALDLDDF 

       370        380 
QGTCQPKEFF PLTNAIKDAL A 

« Hide

References

« Hide 'large scale' references
[1]"neu and ras initiate murine mammary tumors that share genetic markers generally absent in c-myc and int-2-initiated tumors."
Morrison B.W., Leder P.
Oncogene 9:3417-3426(1994) [PubMed: 7970700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[2]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Spinal ganglion.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

X93035 mRNA. Translation: CAA63603.1.
AK051475 mRNA. Translation: BAC34654.1. Different initiation.
BC003780 mRNA. Translation: AAH03780.1.
BC004734 mRNA. Translation: AAH04734.1.
BC005611 mRNA. Translation: AAH05611.1.
IPIIPI00277478.
PIRS61551.
UniGeneMm.38274

3D structure databases

HSSPHSSP built from PDB template 1HJX based on UniProtKB P36222.
SMRQ61362. Positions 22-381.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSiteQ61362.

Genome annotation databases

EnsemblENSMUSG00000064246. Mus musculus. [Contig view]
KEGGmmu:12654.

Organism-specific databases

MGIMGI:1340899. Chi3l1.

Phylogenomic databases

HOVERGENQ61362.

Gene expression databases

ArrayExpressQ61362.
BgeeQ61362.
CleanExMM_CHI3L1.
GermOnlineENSMUSG00000064246. Mus musculus.

Family and domain databases

InterProIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
ProDomPD000471. Chitinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio281872.
SOURCESearch...

Entry information

Entry nameCH3L1_MOUSE
AccessionPrimary (citable) accession number: Q61362
Secondary accession number(s): Q8BKL8, Q99J84
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents