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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

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to amino acid stimulus Source: MGI
  2. collagen catabolic process Source: UniProtKB-KW
  3. 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_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. extracellular region Source: Reactome
  2. intracellular membrane-bounded organelle 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 Inferred
Add
BLAST
Propeptidei18 – 9982Activation peptide
PRO_0000028730Add
BLAST
Chaini100 – 477378Stromelysin-1
PRO_0000028731Add
BLAST

Amino acid modifications

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

ArrayExpressiP28862.
BgeeiP28862.
CleanExiMM_MMP3.
GenevestigatoriP28862.

Structurei

3D structure databases

ProteinModelPortaliP28862.
SMRiP28862. Positions 32-477.

Family & Domainsi

Domains and Repeats

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

Motif

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

MKGLPVLLWL CVVVCSSYPL HDSARDDDAG MELLQKYLEN YYGLAKDVKQ    50
FIKKKDSSLI VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF 100
STFPGSPKWR KSHITYRIVN YTPDLPRQSV DSAIEKALKV WEEVTPLTFS 150
RISEGEADIM ISFAVGEHGD FVPFDGPGTV LAHAYAPGPG INGDAHFDDD 200
ERWTEDVTGT NLFLVAAHEL GHSLGLYHSA KAEALMYPVY KSSTDLSRFH 250
LSQDDVDGIQ SLYGTPTASP DVLVVPTKSN SLEPETSPMC SSTLFFDAVS 300
TLRGEVLFFK DRHFWRKSLR TPEPEFYLIS SFWPSLPSNM DAAYEVTNRD 350
TVFIFKGNQF WAIRGHEELA GYPKSIHTLG LPATVKKIDA AISNKEKRKT 400
YFFVEDKYWR FDEKKQSMEP GFPRKIAEDF PGVDSRVDAV FEAFGFLYFF 450
SGSSQLEFDP NAKKVTHILK SNSWFNC 477
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti468 – 4681I → T1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

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_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

NextBioi 292020.
PROi P28862.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28862.
Bgeei P28862.
CleanExi MM_MMP3.
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: September 3, 2014
This is version 137 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

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