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Protein

Interstitial collagenase A

Gene

Mmp1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.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

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi89Zinc 2; in inhibited formBy similarity1
Metal bindingi155Calcium 2By similarity1
Metal bindingi165Zinc 1By similarity1
Metal bindingi167Zinc 1By similarity1
Metal bindingi172Calcium 3By similarity1
Metal bindingi173Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi180Zinc 1By similarity1
Metal bindingi187Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi189Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi191Calcium 2By similarity1
Metal bindingi193Zinc 1By similarity1
Metal bindingi195Calcium 3By similarity1
Metal bindingi198Calcium 3By similarity1
Metal bindingi215Zinc 2; catalyticBy similarity1
Active sitei216PROSITE-ProRule annotation1
Metal bindingi219Zinc 2; catalyticBy similarity1
Metal bindingi225Zinc 2; catalyticBy similarity1
Metal bindingi283Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi376Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi425Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1933846. Mmp1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000004264518 – 96Activation peptideBy similarityAdd BLAST79
ChainiPRO_000004264697 – 464Interstitial collagenase AAdd BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi202N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi276 ↔ 464By similarity
Glycosylationi371N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9EPL5.
PRIDEiQ9EPL5.

PTM databases

PhosphoSitePlusiQ9EPL5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000043089.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034492.

Structurei

3D structure databases

ProteinModelPortaliQ9EPL5.
SMRiQ9EPL5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati273 – 322Hemopexin 1Add BLAST50
Repeati323 – 369Hemopexin 2Add BLAST47
Repeati372 – 420Hemopexin 3Add BLAST49
Repeati421 – 464Hemopexin 4Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 274MetalloproteaseAdd BLAST180

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi87 – 94Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9EPL5.
KOiK01388.
PhylomeDBiQ9EPL5.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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

« Hide

        10         20         30         40         50
MPSLPLLLLL WAASSYSFPV FHNGDRQNVE TVWKYLENYY NLGKNMQAKN
60 70 80 90 100
VNGKEMMAEK LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT
110 120 130 140 150
HNNPRWTKTH LTYSILNYTP YLPKAVVEDA IARAFRVWSD VTPLTFQRVF
160 170 180 190 200
EEEGDIVLSF HRGDHGDNNP FDGPNYKLAH TFQPGPGLGG DVHYDLDETW
210 220 230 240 250
TNSSENFNLF YVTAHELGHS LGLTHSSDIG ALMFPSYTWY TEDFVLNQDD
260 270 280 290 300
INRIQDLYGP SPNPIQPTGA TTPHPCNGDL TFDAITTFRG EVFFFKGRFY
310 320 330 340 350
IRVNRFMPEP ELNLIGILWP NLPVKLDAAY EASMIDQVRY FKGSKVWAVQ
360 370 380 390 400
EQSVLRGFPR DIHSFFGFPS NVTHIDAAVC EEETGKTYFF VDHMYWRYDE
410 420 430 440 450
NTQSMDPGYP RLTAEDFPGI DDKVDDVFQK GENFYFFHQS VQHRFNLQIR
460
RVDDSRDSST WFNC
Length:464
Mass (Da):53,488
Last modified:March 1, 2001 - v1
Checksum:i09FFC0470E5F9948
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9EPL5.
SMRiQ9EPL5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034492.

Protein family/group databases

MEROPSiM10.033.

PTM databases

PhosphoSitePlusiQ9EPL5.

Proteomic databases

PaxDbiQ9EPL5.
PRIDEiQ9EPL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi83995.
MGIiMGI:1933846. Mmp1a.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9EPL5.
KOiK01388.
PhylomeDBiQ9EPL5.

Miscellaneous databases

PROiQ9EPL5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000043089.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 114 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.