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Protein

Stromelysin-1

Gene

Mmp3

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

Functioni

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

Catalytic activityi

Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi92Zinc 2; in inhibited formBy similarity1
Metal bindingi124Calcium 1By similarity1
Metal bindingi158Calcium 2By similarity1
Metal bindingi168Zinc 1By similarity1
Metal bindingi170Zinc 1By similarity1
Metal bindingi175Calcium 3By similarity1
Metal bindingi176Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi180Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi183Zinc 1By similarity1
Metal bindingi190Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi192Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi194Calcium 2By similarity1
Metal bindingi196Zinc 1By similarity1
Metal bindingi198Calcium 3By similarity1
Metal bindingi199Calcium 1By similarity1
Metal bindingi201Calcium 1By similarity1
Metal bindingi201Calcium 3By similarity1
Metal bindingi218Zinc 2; catalyticBy similarity1
Active sitei219PROSITE-ProRule annotation1
Metal bindingi222Zinc 2; catalyticBy similarity1
Metal bindingi228Zinc 2; catalyticBy similarity1
Metal bindingi297Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi389Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi438Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular response to amino acid stimulus Source: MGI
  • collagen catabolic process Source: UniProtKB-KW
  • extracellular matrix disassembly Source: Reactome
  • negative regulation of hydrogen peroxide metabolic process Source: MGI
  • negative regulation of protein kinase B signaling Source: ParkinsonsUK-UCL
  • positive regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
  • positive regulation of protein oligomerization Source: MGI
  • protein catabolic process Source: ParkinsonsUK-UCL
  • proteolysis Source: ParkinsonsUK-UCL
  • regulation of cell migration Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-2179392. EGFR Transactivation by Gastrin.

Protein family/group databases

MEROPSiM10.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-1 (EC:3.4.24.17)
Short name:
SL-1
Alternative name(s):
EMS-2
Matrix metalloproteinase-3
Short name:
MMP-3
Transin-1
Gene namesi
Name:Mmp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97010. Mmp3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: ParkinsonsUK-UCL
  • extracellular region Source: Reactome
  • mitochondrion Source: ParkinsonsUK-UCL
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17CuratedAdd BLAST17
PropeptideiPRO_000002873018 – 99Activation peptideAdd BLAST82
ChainiPRO_0000028731100 – 477Stromelysin-1Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi290 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP28862.
PaxDbiP28862.
PeptideAtlasiP28862.
PRIDEiP28862.

PTM databases

iPTMnetiP28862.
PhosphoSitePlusiP28862.

Expressioni

Developmental stagei

Present in unfertilized eggs and at the zygote and cleavage stages. Levels increase at the blastocyst stage and with endoderm differentiation.1 Publication

Gene expression databases

BgeeiENSMUSG00000043613.
CleanExiMM_MMP3.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034497.

Structurei

3D structure databases

ProteinModelPortaliP28862.
SMRiP28862.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati287 – 336Hemopexin 1Add BLAST50
Repeati337 – 383Hemopexin 2Add BLAST47
Repeati385 – 433Hemopexin 3Add BLAST49
Repeati434 – 477Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi90 – 97Cysteine 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.
HOVERGENiHBG052484.
InParanoidiP28862.
KOiK01394.

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. 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.
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.

P28862-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGLPVLLWL CVVVCSSYPL HDSARDDDAG MELLQKYLEN YYGLAKDVKQ
60 70 80 90 100
FIKKKDSSLI VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF
110 120 130 140 150
STFPGSPKWR KSHITYRIVN YTPDLPRQSV DSAIEKALKV WEEVTPLTFS
160 170 180 190 200
RISEGEADIM ISFAVGEHGD FVPFDGPGTV LAHAYAPGPG INGDAHFDDD
210 220 230 240 250
ERWTEDVTGT NLFLVAAHEL GHSLGLYHSA KAEALMYPVY KSSTDLSRFH
260 270 280 290 300
LSQDDVDGIQ SLYGTPTASP DVLVVPTKSN SLEPETSPMC SSTLFFDAVS
310 320 330 340 350
TLRGEVLFFK DRHFWRKSLR TPEPEFYLIS SFWPSLPSNM DAAYEVTNRD
360 370 380 390 400
TVFIFKGNQF WAIRGHEELA GYPKSIHTLG LPATVKKIDA AISNKEKRKT
410 420 430 440 450
YFFVEDKYWR FDEKKQSMEP GFPRKIAEDF PGVDSRVDAV FEAFGFLYFF
460 470
SGSSQLEFDP NAKKVTHILK SNSWFNC
Length:477
Mass (Da):53,845
Last modified:February 1, 1994 - v2
Checksum:i9C15594F45262D37
GO

Sequence cautioni

The sequence CAA44860 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti468I → T (PubMed:2744464).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66402 mRNA. Translation: CAA47029.1.
X63162 mRNA. Translation: CAA44860.1. Different initiation.
PIRiJC1476. KCMSS1.
RefSeqiNP_034939.1. NM_010809.2.
UniGeneiMm.4993.

Genome annotation databases

GeneIDi17392.
KEGGimmu:17392.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66402 mRNA. Translation: CAA47029.1.
X63162 mRNA. Translation: CAA44860.1. Different initiation.
PIRiJC1476. KCMSS1.
RefSeqiNP_034939.1. NM_010809.2.
UniGeneiMm.4993.

3D structure databases

ProteinModelPortaliP28862.
SMRiP28862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034497.

Protein family/group databases

MEROPSiM10.005.

PTM databases

iPTMnetiP28862.
PhosphoSitePlusiP28862.

Proteomic databases

MaxQBiP28862.
PaxDbiP28862.
PeptideAtlasiP28862.
PRIDEiP28862.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi17392.
KEGGimmu:17392.

Organism-specific databases

CTDi4314.
MGIiMGI:97010. Mmp3.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOVERGENiHBG052484.
InParanoidiP28862.
KOiK01394.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-2179392. EGFR Transactivation by Gastrin.

Miscellaneous databases

PROiP28862.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000043613.
CleanExiMM_MMP3.

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. 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.
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 nameiMMP3_MOUSE
AccessioniPrimary (citable) accession number: P28862
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1994
Last modified: November 30, 2016
This is version 154 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

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.