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Q9D7Q1

- CHIT1_MOUSE

UniProt

Q9D7Q1 - CHIT1_MOUSE

Protein

Chitotriosidase-1

Gene

Chit1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens By similarity.By similarity

    Catalytic activityi

    Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei140 – 1401Proton donorPROSITE-ProRule annotation
    Binding sitei269 – 2691ChitooligosaccharideBy similarity
    Binding sitei356 – 3561ChitooligosaccharideBy similarity

    GO - Molecular functioni

    1. chitin binding Source: UniProtKB-KW
    2. endochitinase activity Source: Ensembl

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding

    Protein family/group databases

    CAZyiCBM14. Carbohydrate-Binding Module Family 14.
    GH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chitotriosidase-1 (EC:3.2.1.14)
    Alternative name(s):
    Chitinase-1
    Gene namesi
    Name:Chit1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1919134. Chit1.

    Subcellular locationi

    Secreted 1 Publication. Lysosome By similarity
    Note: A small proportion is lysosomal.By similarity

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi136 – 1361D → N: Loss of activity; when associated with Q-140. 1 Publication
    Mutagenesisi140 – 1401E → Q: Loss of activity; when associated with N-136. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121By similarityAdd
    BLAST
    Chaini22 – 464443Chitotriosidase-1PRO_0000011942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 51PROSITE-ProRule annotation
    Disulfide bondi307 ↔ 368PROSITE-ProRule annotation
    Disulfide bondi448 ↔ 461PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ9D7Q1.
    PaxDbiQ9D7Q1.
    PRIDEiQ9D7Q1.

    Expressioni

    Tissue specificityi

    Highly expressed in tongue, stomach, kidney, brain, skin, testis, and bone marrow. Low level of expression was found in lung, heart, spleen, small intestine, and liver. Not detectable in pancreas, salivary gland, large intestine, uterus, or peripheral blood mononuclear cells (PBMC).2 Publications

    Gene expression databases

    BgeeiQ9D7Q1.
    CleanExiMM_CHIT1.
    GenevestigatoriQ9D7Q1.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000083666.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D7Q1.
    SMRiQ9D7Q1. Positions 22-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini415 – 46450Chitin-binding type-2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 712Chitooligosaccharide bindingBy similarity
    Regioni97 – 1004Chitooligosaccharide bindingBy similarity
    Regioni210 – 2134Chitooligosaccharide bindingBy similarity

    Sequence similaritiesi

    Contains 1 chitin-binding type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3325.
    GeneTreeiENSGT00550000074323.
    HOGENOMiHOG000111109.
    HOVERGENiHBG011684.
    InParanoidiQ9D7Q1.
    KOiK01183.
    OMAiHRIKDQK.
    OrthoDBiEOG7ZGX3G.
    PhylomeDBiQ9D7Q1.
    TreeFamiTF315610.

    Family and domain databases

    Gene3Di2.170.140.10. 1 hit.
    3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR002557. Chitin-bd_dom.
    IPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01607. CBM_14. 1 hit.
    PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SMARTiSM00494. ChtBD2. 1 hit.
    SM00636. Glyco_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    SSF57625. SSF57625. 1 hit.
    PROSITEiPS50940. CHIT_BIND_II. 1 hit.
    PS01095. CHITINASE_18. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9D7Q1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVQSLAWAGV MTLLMVQWGS AAKLVCYLTN WSQYRTEAVR FFPRDVDPNL    50
    CTHVIFAFAG MDNHQLSTVE HNDELLYQEL NSLKTKNPKL KTLLAVGGWT 100
    FGTQKFTDMV ATASNRQTFV KSALSFLRTQ GFDGLDLDWE FPGGRGSPTV 150
    DKERFTALIQ DLAKAFQEEA QSSGKERLLL TAAVPSDRGL VDAGYEVDKI 200
    AQSLDFINLM AYDFHSSLEK TTGHNSPLYK RQGESGAAAE QNVDAAVTLW 250
    LQKGTPASKL ILGMPTYGRS FTLASSSDNG VGAPATGPGA PGPYTKDKGV 300
    LAYYEACSWK ERHRIEDQKV PYAFQDNQWV SFDDVESFKA KAAYLKQKGL 350
    GGAMVWVLDL DDFKGSFCNQ GPYPLIRTLR QELNLPSETP RSPEQIIPEP 400
    RPSSMPEQGP SPGLDNFCQG KADGVYPNPG DESTYYNCGG GRLFQQSCPP 450
    GLVFRASCKC CTWS 464
    Length:464
    Mass (Da):51,112
    Last modified:September 5, 2006 - v2
    Checksum:i6276B6A414B4E96A
    GO
    Isoform 2 (identifier: Q9D7Q1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         343-396: AYLKQKGLGG...SETPRSPEQI → KLMGSTPTLE...KFLEPHPTPV
         397-464: Missing.

    Show »
    Length:396
    Mass (Da):43,413
    Checksum:i32BB674B61AF7123
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei343 – 39654AYLKQ…SPEQI → KLMGSTPTLETSPLTTTVEE GGCSSRAVLQAWCLEPLANV VPGAKFLEPHPTPV in isoform 2. 1 PublicationVSP_020143Add
    BLAST
    Alternative sequencei397 – 46468Missing in isoform 2. 1 PublicationVSP_020144Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY458654 mRNA. Translation: AAR14312.1.
    AY536287 mRNA. Translation: AAS47832.1.
    AK009012 mRNA. Translation: BAB26025.1.
    CCDSiCCDS15304.1. [Q9D7Q1-1]
    CCDS69943.1. [Q9D7Q1-2]
    RefSeqiNP_001271453.1. NM_001284524.1. [Q9D7Q1-2]
    NP_001271454.1. NM_001284525.1. [Q9D7Q1-1]
    NP_082255.1. NM_027979.2. [Q9D7Q1-1]
    XP_006529942.1. XM_006529879.1. [Q9D7Q1-1]
    XP_006529943.1. XM_006529880.1. [Q9D7Q1-1]
    XP_006529944.1. XM_006529881.1. [Q9D7Q1-2]
    UniGeneiMm.328268.

    Genome annotation databases

    EnsembliENSMUST00000086475; ENSMUSP00000083666; ENSMUSG00000026450. [Q9D7Q1-1]
    ENSMUST00000159963; ENSMUSP00000123979; ENSMUSG00000026450. [Q9D7Q1-1]
    ENSMUST00000160060; ENSMUSP00000124331; ENSMUSG00000026450. [Q9D7Q1-2]
    GeneIDi71884.
    KEGGimmu:71884.
    UCSCiuc007crf.1. mouse. [Q9D7Q1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY458654 mRNA. Translation: AAR14312.1 .
    AY536287 mRNA. Translation: AAS47832.1 .
    AK009012 mRNA. Translation: BAB26025.1 .
    CCDSi CCDS15304.1. [Q9D7Q1-1 ]
    CCDS69943.1. [Q9D7Q1-2 ]
    RefSeqi NP_001271453.1. NM_001284524.1. [Q9D7Q1-2 ]
    NP_001271454.1. NM_001284525.1. [Q9D7Q1-1 ]
    NP_082255.1. NM_027979.2. [Q9D7Q1-1 ]
    XP_006529942.1. XM_006529879.1. [Q9D7Q1-1 ]
    XP_006529943.1. XM_006529880.1. [Q9D7Q1-1 ]
    XP_006529944.1. XM_006529881.1. [Q9D7Q1-2 ]
    UniGenei Mm.328268.

    3D structure databases

    ProteinModelPortali Q9D7Q1.
    SMRi Q9D7Q1. Positions 22-383.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000083666.

    Protein family/group databases

    CAZyi CBM14. Carbohydrate-Binding Module Family 14.
    GH18. Glycoside Hydrolase Family 18.

    Proteomic databases

    MaxQBi Q9D7Q1.
    PaxDbi Q9D7Q1.
    PRIDEi Q9D7Q1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086475 ; ENSMUSP00000083666 ; ENSMUSG00000026450 . [Q9D7Q1-1 ]
    ENSMUST00000159963 ; ENSMUSP00000123979 ; ENSMUSG00000026450 . [Q9D7Q1-1 ]
    ENSMUST00000160060 ; ENSMUSP00000124331 ; ENSMUSG00000026450 . [Q9D7Q1-2 ]
    GeneIDi 71884.
    KEGGi mmu:71884.
    UCSCi uc007crf.1. mouse. [Q9D7Q1-1 ]

    Organism-specific databases

    CTDi 1118.
    MGIi MGI:1919134. Chit1.

    Phylogenomic databases

    eggNOGi COG3325.
    GeneTreei ENSGT00550000074323.
    HOGENOMi HOG000111109.
    HOVERGENi HBG011684.
    InParanoidi Q9D7Q1.
    KOi K01183.
    OMAi HRIKDQK.
    OrthoDBi EOG7ZGX3G.
    PhylomeDBi Q9D7Q1.
    TreeFami TF315610.

    Miscellaneous databases

    NextBioi 334840.
    PROi Q9D7Q1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D7Q1.
    CleanExi MM_CHIT1.
    Genevestigatori Q9D7Q1.

    Family and domain databases

    Gene3Di 2.170.140.10. 1 hit.
    3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR002557. Chitin-bd_dom.
    IPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01607. CBM_14. 1 hit.
    PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view ]
    SMARTi SM00494. ChtBD2. 1 hit.
    SM00636. Glyco_18. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    SSF57625. SSF57625. 1 hit.
    PROSITEi PS50940. CHIT_BIND_II. 1 hit.
    PS01095. CHITINASE_18. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional characterization of mouse chitotriosidase."
      Zheng T., Rabach M., Chen N.Y., Rabach L., Hu X., Elias J.A., Zhu Z.
      Gene 357:37-46(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-136 AND GLU-140.
      Strain: C57BL/6.
      Tissue: Tongue.
    2. "Marked differences in tissue-specific expression of chitinases in mouse and man."
      Boot R.G., Bussink A.P., Verhoek M., de Boer P.A.J., Moorman A.F., Aerts J.M.F.G.
      J. Histochem. Cytochem. 53:1283-1292(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Tongue.
    3. "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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Tongue.

    Entry informationi

    Entry nameiCHIT1_MOUSE
    AccessioniPrimary (citable) accession number: Q9D7Q1
    Secondary accession number(s): Q6QJD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 122 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

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3