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Q3U435

- MMP25_MOUSE

UniProt

Q3U435 - MMP25_MOUSE

Protein

Matrix metalloproteinase-25

Gene

Mmp25

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    May activate progelatinase A.By similarity

    Cofactori

    Binds 1 zinc ion per subunit.By similarity
    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi145 – 1451Zinc; in inhibited formBy similarity
    Metal bindingi287 – 2871Zinc; catalyticPROSITE-ProRule annotation
    Active sitei288 – 2881PROSITE-ProRule annotation
    Metal bindingi291 – 2911Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi297 – 2971Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. hard palate development Source: MGI
    2. inflammatory response Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.024.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-25 (EC:3.4.24.-)
    Short name:
    MMP-25
    Gene namesi
    Name:Mmp25
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2443938. Mmp25.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular matrix Source: InterPro
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 162162By similarityPRO_0000288635Add
    BLAST
    Chaini163 – 593431Matrix metalloproteinase-25PRO_0000288636Add
    BLAST
    Propeptidei594 – 61522Removed in mature formSequence AnalysisPRO_0000288637Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi371 ↔ 562By similarity
    Lipidationi593 – 5931GPI-anchor amidated alanineSequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

    Proteomic databases

    PRIDEiQ3U435.

    PTM databases

    PhosphoSiteiQ3U435.

    Expressioni

    Gene expression databases

    BgeeiQ3U435.
    CleanExiMM_MMP25.
    GenevestigatoriQ3U435.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000024696.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3U435.
    SMRiQ3U435. Positions 113-564.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei53 – 7321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati368 – 41750Hemopexin 1Add
    BLAST
    Repeati421 – 46646Hemopexin 2Add
    BLAST
    Repeati467 – 51549Hemopexin 3Add
    BLAST
    Repeati516 – 56247Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi143 – 1508Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi158 – 1625Poly-Arg
    Compositional biasi340 – 36829Pro-richAdd
    BLAST

    Domaini

    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

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295915.
    GeneTreeiENSGT00750000117336.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    InParanoidiQ3U435.
    KOiK08003.
    OMAiHYWRFPK.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ3U435.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR024079. MetalloPept_cat_dom.
    IPR028733. MMP25.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF21. PTHR10201:SF21. 1 hit.
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q3U435-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCFPGSQISP ARLYYLVSAP WICTGSLTSS RLPRRRESGP LRVPPRSVQA    50
    ERILRLPAFG LPLLALLLVP LLPVRAQNPD AKVVSMGVEW LTRYGYLPPA 100
    DPVHAQMQSL EKLQDAIKVM QRFAGLPETG QMDPMTIKTM RKPRCSLPDV 150
    LGAAGLVRRR RRYSLSGSVW KKRTLTWSIR SFSQKSQLSP QIVRTLLSYA 200
    LAVWATESGL TFQEVNSQYQ EPDIIIHFAR AYHQDSYPFD GSGGTLAHAF 250
    FPGEHPISGD THFDDEETWT FGSTDDNGID LFAVAVHEFG HALGLGHSSA 300
    PNSIMRPFYQ GPVGDPATYR LPQDDRDGLQ QLYGRVSQNP NARPTRKPLV 350
    PPPQPPAMPP DSPATPVPDR CEGNFDAVAN IRGEIFLFKG PWFWRLQPSG 400
    QLVSPRPAGL HRFWEGLPTH VKVIQAAYAR PLDGRIILFS GPQFWVFQER 450
    QLEGAARPLV EFGLPPGEDV DAVFSWPHNG KTYLIRGQKY WRYDEVAARP 500
    DPGYPRALSL WDGAPFAPDD VTISNTGDTY FFKGTHFWRF AEGSVKAESD 550
    SPQPIGPKWL DCPAPNSDPR VTSPPKTTSK TRSCDCHCEL NQASEQLSPL 600
    LLPLLPLVAG EVFSY 615
    Length:615
    Mass (Da):68,496
    Last modified:October 11, 2005 - v1
    Checksum:i7B0842CACF06382D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK154458 mRNA. Translation: BAE32600.1.
    BC112379 mRNA. Translation: AAI12380.1.
    CCDSiCCDS28452.1.
    RefSeqiNP_001028511.1. NM_001033339.3.
    UniGeneiMm.235343.

    Genome annotation databases

    EnsembliENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
    GeneIDi240047.
    KEGGimmu:240047.
    UCSCiuc008asq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK154458 mRNA. Translation: BAE32600.1 .
    BC112379 mRNA. Translation: AAI12380.1 .
    CCDSi CCDS28452.1.
    RefSeqi NP_001028511.1. NM_001033339.3.
    UniGenei Mm.235343.

    3D structure databases

    ProteinModelPortali Q3U435.
    SMRi Q3U435. Positions 113-564.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000024696.

    Protein family/group databases

    MEROPSi M10.024.

    PTM databases

    PhosphoSitei Q3U435.

    Proteomic databases

    PRIDEi Q3U435.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024696 ; ENSMUSP00000024696 ; ENSMUSG00000023903 .
    GeneIDi 240047.
    KEGGi mmu:240047.
    UCSCi uc008asq.1. mouse.

    Organism-specific databases

    CTDi 64386.
    MGIi MGI:2443938. Mmp25.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00750000117336.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi Q3U435.
    KOi K08003.
    OMAi HYWRFPK.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q3U435.
    TreeFami TF315428.

    Miscellaneous databases

    NextBioi 384387.
    PROi Q3U435.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3U435.
    CleanExi MM_MMP25.
    Genevestigatori Q3U435.

    Family and domain databases

    Gene3Di 1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR024079. MetalloPept_cat_dom.
    IPR028733. MMP25.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF21. PTHR10201:SF21. 1 hit.
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS51642. HEMOPEXIN_2. 4 hits.
    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: NOD.
    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].

    Entry informationi

    Entry nameiMMP25_MOUSE
    AccessioniPrimary (citable) accession number: Q3U435
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    In contrast to the human ortholog it does not have a signal sequence as it has an additional 53 residue sequence at the N-terminus. At the position of the human initiation methionine there is a leucine (Leu-54).Curated

    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