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Q8BNJ2

- ATS4_MOUSE

UniProt

Q8BNJ2 - ATS4_MOUSE

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene

Adamts4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
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    Functioni

    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site By similarity.By similarity

    Catalytic activityi

    Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi190 – 1901Zinc; in inhibited formBy similarity
    Metal bindingi357 – 3571Zinc; catalyticBy similarity
    Active sitei358 – 3581PROSITE-ProRule annotation
    Metal bindingi361 – 3611Zinc; catalyticBy similarity
    Metal bindingi367 – 3671Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: MGI
    2. metallopeptidase activity Source: MGI
    3. protein binding Source: MGI
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. defense response to bacterium Source: MGI
    2. proteolysis Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199052. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.221.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
    Short name:
    ADAM-TS 4
    Short name:
    ADAM-TS4
    Short name:
    ADAMTS-4
    Alternative name(s):
    Aggrecanase-1
    Gene namesi
    Name:Adamts4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1339949. Adamts4.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4949Sequence AnalysisAdd
    BLAST
    Propeptidei50 – 208159By similarityPRO_0000029166Add
    BLAST
    Chaini209 – 833625A disintegrin and metalloproteinase with thrombospondin motifs 4PRO_0000029167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi289 ↔ 341By similarity
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi318 ↔ 323By similarity
    Disulfide bondi335 ↔ 419By similarity
    Disulfide bondi373 ↔ 403By similarity
    Disulfide bondi445 ↔ 468By similarity
    Disulfide bondi456 ↔ 478By similarity
    Disulfide bondi463 ↔ 497By similarity
    Disulfide bondi491 ↔ 502By similarity
    Disulfide bondi528 ↔ 565By similarity
    Disulfide bondi532 ↔ 570By similarity
    Disulfide bondi543 ↔ 555By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ8BNJ2.
    PRIDEiQ8BNJ2.

    PTM databases

    PhosphoSiteiQ8BNJ2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BNJ2.
    BgeeiQ8BNJ2.
    GenevestigatoriQ8BNJ2.

    Interactioni

    Subunit structurei

    Interacts with SRPX2.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BNJ2.
    SMRiQ8BNJ2. Positions 211-801.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini214 – 424211Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 51583DisintegrinAdd
    BLAST
    Domaini516 – 57156TSP type-1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni682 – 833152SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi188 – 1958Cysteine switchBy similarity

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.By similarity
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG271890.
    GeneTreeiENSGT00650000092972.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiQ8BNJ2.
    KOiK07764.
    OrthoDBiEOG7WDN1M.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 1 hit.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BNJ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQMGLHPRR GLTGHWLQRF QPCLPLHTVQ WRRLLLLAFL LSLAWPASPL    50
    PREEEIVFPE KLNGSSILPG SGVPARLLYR LPAFGEMLLL ELEQDPGVQV 100
    EGLTVQYLGQ APEMLGGAEP GTYLTGTING DPESVASLHW DGGALLGVLQ 150
    YRGAELHLQP LEGGALNSAG GPGAHILRRK SPASSQGPMC TVKAPSGSPS 200
    PISRRTKRFA SLSRFVETLV VADDKMAAFH GTGLKRYLLT VMAAAAKAFK 250
    HPSIRNPVNL VVTRLVILGS GQEGPQVGPS AAQTLRSFCT WQRGLNTPND 300
    SDPDHFDTAI LFTRQDLCGV STCDTLGMAD VGTVCDPARS CAIVEDDGLQ 350
    SAFTAAHELG HVFNMLHDNS KPCTNLNGQG GSSRHVMAPV MAHVDPEEPW 400
    SPCSARFITD FLDNGYGHCL LDKPEAPLHL PATFPGKDYD ADRQCQLTFG 450
    PDSSHCPQLP PPCAALWCSG HLNGHAMCQT KHSPWADGTP CGSSQACMGG 500
    RCLHVDQLKD FNVPQAGGWG PWGPWGDCSR TCGGGVQFSS RDCTRPVPRN 550
    GGKYCEGRRT RFRSCNTENC PHGSALTFRE EQCAAYNHRT DLFKSFPGPM 600
    DWVPRYTGVA PRDQCKLTCQ ARALGYYYVL EPRVADGTPC SPDTSSVCVQ 650
    GRCIHAGCDR IIGSKKKFDK CMVCGGDGSR CSKQSGSFKK FRYGYSDVVT 700
    IPAGATHILV RQQGGSGLKS IYLALKLSDG SYALNGEYTL MPSPTDVVLP 750
    GAVSLRYSGA TAASETLSGH GPLAQPLTLQ VLVAGNPQNA RLRYSFFVPR 800
    PVPSTPRPPP QDWLQRRAEI LKILRKRPWA GRK 833
    Length:833
    Mass (Da):90,070
    Last modified:May 10, 2005 - v2
    Checksum:i6512B9ED2617F3A4
    GO

    Sequence cautioni

    The sequence BAC38944.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181Q → R in AAH27773. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK083534 mRNA. Translation: BAC38944.1. Different initiation.
    BC027773 mRNA. Translation: AAH27773.1.
    RefSeqiNP_766433.1. NM_172845.2.
    UniGeneiMm.491147.

    Genome annotation databases

    EnsembliENSMUST00000111315; ENSMUSP00000106947; ENSMUSG00000006403.
    GeneIDi240913.
    KEGGimmu:240913.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK083534 mRNA. Translation: BAC38944.1 . Different initiation.
    BC027773 mRNA. Translation: AAH27773.1 .
    RefSeqi NP_766433.1. NM_172845.2.
    UniGenei Mm.491147.

    3D structure databases

    ProteinModelPortali Q8BNJ2.
    SMRi Q8BNJ2. Positions 211-801.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M12.221.

    PTM databases

    PhosphoSitei Q8BNJ2.

    Proteomic databases

    PaxDbi Q8BNJ2.
    PRIDEi Q8BNJ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000111315 ; ENSMUSP00000106947 ; ENSMUSG00000006403 .
    GeneIDi 240913.
    KEGGi mmu:240913.

    Organism-specific databases

    CTDi 9507.
    MGIi MGI:1339949. Adamts4.

    Phylogenomic databases

    eggNOGi NOG271890.
    GeneTreei ENSGT00650000092972.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi Q8BNJ2.
    KOi K07764.
    OrthoDBi EOG7WDN1M.

    Enzyme and pathway databases

    Reactomei REACT_199052. Degradation of the extracellular matrix.

    Miscellaneous databases

    NextBioi 384802.
    PROi Q8BNJ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BNJ2.
    Bgeei Q8BNJ2.
    Genevestigatori Q8BNJ2.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: C57BL/6J.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiATS4_MOUSE
    AccessioniPrimary (citable) accession number: Q8BNJ2
    Secondary accession number(s): Q8K384
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 99 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3