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Q9EPL5

- MMP1A_MOUSE

UniProt

Q9EPL5 - MMP1A_MOUSE

Protein

Interstitial collagenase A

Gene

Mmp1a

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 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X By similarity. Able to degrade synthetic peptides and type I and II fibrillar collagen.By similarity

    Catalytic activityi

    Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

    Cofactori

    Binds 4 calcium ions per subunit.By similarity
    Binds 2 zinc ions per subunit.By similarity

    Enzyme regulationi

    Can be activated without removal of the activation peptide.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi89 – 891Zinc 2; in inhibited formBy similarity
    Metal bindingi155 – 1551Calcium 2By similarity
    Metal bindingi165 – 1651Zinc 1By similarity
    Metal bindingi167 – 1671Zinc 1By similarity
    Metal bindingi172 – 1721Calcium 3By similarity
    Metal bindingi173 – 1731Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi180 – 1801Zinc 1By similarity
    Metal bindingi187 – 1871Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi189 – 1891Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi191 – 1911Calcium 2By similarity
    Metal bindingi193 – 1931Zinc 1By similarity
    Metal bindingi195 – 1951Calcium 3By similarity
    Metal bindingi198 – 1981Calcium 3By similarity
    Metal bindingi215 – 2151Zinc 2; catalyticBy similarity
    Active sitei216 – 2161PROSITE-ProRule annotation
    Metal bindingi219 – 2191Zinc 2; catalyticBy similarity
    Metal bindingi225 – 2251Zinc 2; catalyticBy similarity
    Metal bindingi283 – 2831Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi376 – 3761Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi425 – 4251Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to alkaloid Source: Ensembl
    2. cellular response to drug Source: Ensembl
    3. cellular response to fluid shear stress Source: Ensembl
    4. cellular response to interleukin-1 Source: Ensembl
    5. cellular response to iron(III) ion Source: Ensembl
    6. cellular response to lipopolysaccharide Source: Ensembl
    7. cellular response to peptide hormone stimulus Source: Ensembl
    8. cellular response to tumor necrosis factor Source: Ensembl
    9. cellular response to vitamin D Source: Ensembl
    10. collagen catabolic process Source: UniProtKB-KW
    11. cysteine metabolic process Source: Ensembl
    12. ferulate metabolic process Source: Ensembl
    13. luteinization Source: Ensembl
    14. luteolysis Source: Ensembl
    15. polysaccharide metabolic process Source: Ensembl
    16. positive regulation of endopeptidase activity Source: Ensembl
    17. positive regulation of fibroblast migration Source: Ensembl
    18. positive regulation of smooth muscle cell migration Source: Ensembl
    19. response to inactivity Source: Ensembl
    20. response to indole-3-methanol Source: Ensembl
    21. response to mechanical stimulus Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.
    REACT_211508. Basigin interactions.

    Protein family/group databases

    MEROPSiM10.033.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interstitial collagenase A (EC:3.4.24.7)
    Alternative name(s):
    Matrix metalloproteinase-1a
    Short name:
    MMP-1a
    Mcol-A
    Gene namesi
    Name:Mmp1a
    Synonyms:McolA
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1933846. Mmp1a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular space Source: Ensembl
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 9679Activation peptideBy similarityPRO_0000042645Add
    BLAST
    Chaini97 – 464368Interstitial collagenase APRO_0000042646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi276 ↔ 464By similarity
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiQ9EPL5.

    PTM databases

    PhosphoSiteiQ9EPL5.

    Expressioni

    Gene expression databases

    BgeeiQ9EPL5.
    GenevestigatoriQ9EPL5.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EPL5.
    SMRiQ9EPL5. Positions 29-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati273 – 32250Hemopexin 1Add
    BLAST
    Repeati323 – 36947Hemopexin 2Add
    BLAST
    Repeati372 – 42049Hemopexin 3Add
    BLAST
    Repeati421 – 46444Hemopexin 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni95 – 274180MetalloproteaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi87 – 948Cysteine switchBy similarity

    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, Signal

    Phylogenomic databases

    eggNOGiNOG258253.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ149J4.
    KOiK01388.
    PhylomeDBiQ9EPL5.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PfamiPF00045. Hemopexin. 3 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.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. 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.

    Q9EPL5-1 [UniParc]FASTAAdd to Basket

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    MPSLPLLLLL WAASSYSFPV FHNGDRQNVE TVWKYLENYY NLGKNMQAKN    50
    VNGKEMMAEK LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT 100
    HNNPRWTKTH LTYSILNYTP YLPKAVVEDA IARAFRVWSD VTPLTFQRVF 150
    EEEGDIVLSF HRGDHGDNNP FDGPNYKLAH TFQPGPGLGG DVHYDLDETW 200
    TNSSENFNLF YVTAHELGHS LGLTHSSDIG ALMFPSYTWY TEDFVLNQDD 250
    INRIQDLYGP SPNPIQPTGA TTPHPCNGDL TFDAITTFRG EVFFFKGRFY 300
    IRVNRFMPEP ELNLIGILWP NLPVKLDAAY EASMIDQVRY FKGSKVWAVQ 350
    EQSVLRGFPR DIHSFFGFPS NVTHIDAAVC EEETGKTYFF VDHMYWRYDE 400
    NTQSMDPGYP RLTAEDFPGI DDKVDDVFQK GENFYFFHQS VQHRFNLQIR 450
    RVDDSRDSST WFNC 464
    Length:464
    Mass (Da):53,488
    Last modified:March 1, 2001 - v1
    Checksum:i09FFC0470E5F9948
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ278462 mRNA. Translation: CAC18880.1.
    AK049552 mRNA. Translation: BAC33807.1.
    AY211543 Genomic DNA. Translation: AAO37582.1.
    BC117756 mRNA. Translation: AAI17757.1.
    RefSeqiNP_114395.1. NM_032006.3.
    UniGeneiMm.156952.

    Genome annotation databases

    GeneIDi83995.
    KEGGimmu:83995.
    UCSCiuc009ocp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ278462 mRNA. Translation: CAC18880.1 .
    AK049552 mRNA. Translation: BAC33807.1 .
    AY211543 Genomic DNA. Translation: AAO37582.1 .
    BC117756 mRNA. Translation: AAI17757.1 .
    RefSeqi NP_114395.1. NM_032006.3.
    UniGenei Mm.156952.

    3D structure databases

    ProteinModelPortali Q9EPL5.
    SMRi Q9EPL5. Positions 29-463.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M10.033.

    PTM databases

    PhosphoSitei Q9EPL5.

    Proteomic databases

    PRIDEi Q9EPL5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 83995.
    KEGGi mmu:83995.
    UCSCi uc009ocp.1. mouse.

    Organism-specific databases

    CTDi 83995.
    MGIi MGI:1933846. Mmp1a.

    Phylogenomic databases

    eggNOGi NOG258253.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q149J4.
    KOi K01388.
    PhylomeDBi Q9EPL5.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.
    REACT_211508. Basigin interactions.

    Miscellaneous databases

    NextBioi 350854.
    PROi Q9EPL5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EPL5.
    Genevestigatori Q9EPL5.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    Pfami PF00045. Hemopexin. 3 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 PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation."
      Balbin M., Fueyo A., Knauper V., Lopez J.M., Alvarez J., Sanchez L.M., Quesada V., Bordallo J., Murphy G., Lopez-Otin C.
      J. Biol. Chem. 276:10253-10262(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
      , 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.
    3. "Genomic sequence analysis in the mouse T-complex region."
      Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129/SvJ.
    4. "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 nameiMMP1A_MOUSE
    AccessioniPrimary (citable) accession number: Q9EPL5
    Secondary accession number(s): Q149J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 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