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P28862

- MMP3_MOUSE

UniProt

P28862 - MMP3_MOUSE

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Protein

Stromelysin-1

Gene

Mmp3

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 Ca(2+) ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn(2+) ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
Metal bindingi124 – 1241Calcium 1By similarity
Metal bindingi158 – 1581Calcium 2By similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi170 – 1701Zinc 1By similarity
Metal bindingi175 – 1751Calcium 3By similarity
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi183 – 1831Zinc 1By similarity
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi194 – 1941Calcium 2By similarity
Metal bindingi196 – 1961Zinc 1By similarity
Metal bindingi198 – 1981Calcium 3By similarity
Metal bindingi199 – 1991Calcium 1By similarity
Metal bindingi201 – 2011Calcium 1By similarity
Metal bindingi201 – 2011Calcium 3By similarity
Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
Active sitei219 – 2191PROSITE-ProRule annotation
Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
Metal bindingi228 – 2281Zinc 2; catalyticBy similarity
Metal bindingi297 – 2971Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi389 – 3891Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi438 – 4381Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to amino acid stimulus Source: MGI
  2. collagen catabolic process Source: UniProtKB-KW
  3. negative regulation of protein kinase B signaling Source: ParkinsonsUK-UCL
  4. positive regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
  5. protein catabolic process Source: ParkinsonsUK-UCL
  6. proteolysis Source: ParkinsonsUK-UCL
  7. 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

ReactomeiREACT_198350. EGFR Transactivation by Gastrin.
REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

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
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:97010. Mmp3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: ParkinsonsUK-UCL
  2. extracellular region Source: Reactome
  3. mitochondrion Source: ParkinsonsUK-UCL
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717CuratedAdd
BLAST
Propeptidei18 – 9982Activation peptidePRO_0000028730Add
BLAST
Chaini100 – 477378Stromelysin-1PRO_0000028731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi290 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP28862.

PTM databases

PhosphoSiteiP28862.

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

BgeeiP28862.
CleanExiMM_MMP3.
ExpressionAtlasiP28862. baseline and differential.
GenevestigatoriP28862.

Structurei

3D structure databases

ProteinModelPortaliP28862.
SMRiP28862. Positions 32-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati287 – 33650Hemopexin 1Add
BLAST
Repeati337 – 38347Hemopexin 2Add
BLAST
Repeati385 – 43349Hemopexin 3Add
BLAST
Repeati434 – 47744Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine 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.
HOVERGENiHBG052484.
InParanoidiP28862.
KOiK01394.

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.
IPR028700. Stromelysin_1.
[Graphical view]
PANTHERiPTHR10201:SF38. PTHR10201:SF38. 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.
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 CAA44860.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti468 – 4681I → T(PubMed:2744464)Curated

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_010809.1.
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.
PIRi JC1476. KCMSS1.
RefSeqi NP_034939.1. NM_010809.1.
UniGenei Mm.4993.

3D structure databases

ProteinModelPortali P28862.
SMRi P28862. Positions 32-477.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.005.

PTM databases

PhosphoSitei P28862.

Proteomic databases

PRIDEi P28862.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 17392.
KEGGi mmu:17392.

Organism-specific databases

CTDi 4314.
MGIi MGI:97010. Mmp3.

Phylogenomic databases

eggNOGi NOG258253.
HOVERGENi HBG052484.
InParanoidi P28862.
KOi K01394.

Enzyme and pathway databases

Reactomei REACT_198350. EGFR Transactivation by Gastrin.
REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

NextBioi 292020.
PROi P28862.
SOURCEi Search...

Gene expression databases

Bgeei P28862.
CleanExi MM_MMP3.
ExpressionAtlasi P28862. baseline and differential.
Genevestigatori P28862.

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.
IPR028700. Stromelysin_1.
[Graphical view ]
PANTHERi PTHR10201:SF38. PTHR10201:SF38. 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 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. "Cloning and sequencing of a cDNA encoding mouse stromelysin 1."
    Hammani K., Henriet P., Eeckhout Y.
    Gene 120:321-322(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NMRI.
    Tissue: Calvaria.
  2. Li F., Strange R., Saurer S., Niemann H., Friis R.R.
    Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss.
  3. "Genes for extracellular-matrix-degrading metalloproteinases and their inhibitor, TIMP, are expressed during early mammalian development."
    Brenner C.A., Adler R.R., Rappolee D.A., Pedersen R.A., Werb Z.
    Genes Dev. 3:848-859(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 415-469, DEVELOPMENTAL STAGE.

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 26, 2014
This is version 140 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

External Data

Dasty 3