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Q9EPL5

- MMP1A_MOUSE

UniProt

Q9EPL5 - MMP1A_MOUSE

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Protein

Interstitial collagenase A

Gene
Mmp1a, McolA
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.

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 form By similarity
Metal bindingi155 – 1551Calcium 2 By similarity
Metal bindingi165 – 1651Zinc 1 By similarity
Metal bindingi167 – 1671Zinc 1 By similarity
Metal bindingi172 – 1721Calcium 3 By similarity
Metal bindingi173 – 1731Calcium 3; via carbonyl oxygen By similarity
Metal bindingi180 – 1801Zinc 1 By similarity
Metal bindingi187 – 1871Calcium 2; via carbonyl oxygen By similarity
Metal bindingi189 – 1891Calcium 2; via carbonyl oxygen By similarity
Metal bindingi191 – 1911Calcium 2 By similarity
Metal bindingi193 – 1931Zinc 1 By similarity
Metal bindingi195 – 1951Calcium 3 By similarity
Metal bindingi198 – 1981Calcium 3 By similarity
Metal bindingi215 – 2151Zinc 2; catalytic By similarity
Active sitei216 – 2161 By similarity
Metal bindingi219 – 2191Zinc 2; catalytic By similarity
Metal bindingi225 – 2251Zinc 2; catalytic By similarity
Metal bindingi283 – 2831Calcium 4; via carbonyl oxygen By similarity
Metal bindingi376 – 3761Calcium 4; via carbonyl oxygen By similarity
Metal bindingi425 – 4251Calcium 4; via carbonyl oxygen By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
BLAST
Propeptidei18 – 9679Activation peptide By similarityPRO_0000042645Add
BLAST
Chaini97 – 464368Interstitial collagenase APRO_0000042646Add
BLAST

Amino acid modifications

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

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.

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 switch By 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.
Contains 4 hemopexin repeats.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 98 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

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