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P03957

- MMP3_RAT

UniProt

P03957 - MMP3_RAT

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Protein

Stromelysin-1

Gene

Mmp3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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 bindingi90 – 901Zinc 2; in inhibited formBy similarity
Metal bindingi122 – 1221Calcium 1By similarity
Metal bindingi156 – 1561Calcium 2By similarity
Metal bindingi166 – 1661Zinc 1By similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi173 – 1731Calcium 3By similarity
Metal bindingi174 – 1741Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi181 – 1811Zinc 1By similarity
Metal bindingi188 – 1881Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Calcium 2By similarity
Metal bindingi194 – 1941Zinc 1By similarity
Metal bindingi196 – 1961Calcium 3By similarity
Metal bindingi197 – 1971Calcium 1By similarity
Metal bindingi199 – 1991Calcium 1By similarity
Metal bindingi199 – 1991Calcium 3By similarity
Metal bindingi216 – 2161Zinc 2; catalyticBy similarity
Active sitei217 – 2171
Metal bindingi220 – 2201Zinc 2; catalyticBy similarity
Metal bindingi226 – 2261Zinc 2; catalyticBy similarity
Metal bindingi295 – 2951Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi387 – 3871Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi436 – 4361Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. protein complex binding Source: RGD
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to cell-matrix adhesion Source: RGD
  2. cellular response to interleukin-1 Source: RGD
  3. collagen catabolic process Source: UniProtKB-KW
  4. female pregnancy Source: RGD
  5. positive regulation of cell migration Source: RGD
  6. response to amino acid Source: RGD
  7. response to cytokine Source: RGD
  8. response to estradiol Source: RGD
  9. response to hypoxia Source: RGD
  10. response to interleukin-1 Source: RGD
  11. response to lipopolysaccharide Source: RGD
  12. response to tumor necrosis factor Source: RGD
  13. wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-1 (EC:3.4.24.17)
Short name:
SL-1
Alternative name(s):
Matrix metalloproteinase-3
Short name:
MMP-3
PTR1 protein
Transin-1
Gene namesi
Name:Mmp3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621317. Mmp3.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: RGD
  2. dendrite Source: RGD
  3. extracellular space Source: RGD
  4. nucleus Source: RGD
  5. proteinaceous extracellular matrix Source: UniProtKB-KW
  6. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717CuratedAdd
BLAST
Propeptidei18 – 9780Activation peptidePRO_0000028734Add
BLAST
Chaini98 – 475378Stromelysin-1PRO_0000028735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi288 ↔ 475By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP03957.
PRIDEiP03957.

Expressioni

Inductioni

By epidermal growth factor and is increased in FR3T3 and RAT-1 fibroblasts transformed by polyoma virus, Rous sarcoma virus, or the human cellular H-Ras oncogene.

Gene expression databases

GenevestigatoriP03957.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012310.

Structurei

3D structure databases

ProteinModelPortaliP03957.
SMRiP03957. Positions 31-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati285 – 33450Hemopexin 1Add
BLAST
Repeati335 – 38147Hemopexin 2Add
BLAST
Repeati383 – 43149Hemopexin 3Add
BLAST
Repeati432 – 47544Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi88 – 958Cysteine 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.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP03957.
PhylomeDBiP03957.

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.

P03957-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGLPVLLWL CTAVCSSYPL HGSEEDAGME VLQKYLENYY GLEKDVKQFT
60 70 80 90 100
KKKDSSPVVK KIQEMQKFLG LKMTGKLDSN TMELMHKPRC GVPDVGGFST
110 120 130 140 150
FPGSPKWRKN HISYRIVNYT LDLPRESVDS AIERALKVWE EVTPLTFSRI
160 170 180 190 200
SEGEADIMIS FAVEEHGDFI PFDGPGMVLA HAYAPGPGTN GDAHFDDDER
210 220 230 240 250
WTDDVTGTNL FLVAAHELGH SLGLFHSANA EALMYPVYKS STDLARFHLS
260 270 280 290 300
QDDVDGIQSL YGPPTESPDV LVVPTKSNSL DPETLPMCSS ALSFDAVSTL
310 320 330 340 350
RGEVLFFKDR HFWRKSLRTP EPGFYLISSF WPSLPSNMDA AYEVTNRDTV
360 370 380 390 400
FILKGNQIWA IRGHEELAGY PKSIHTLGLP ETVQKIDAAI SLKDQKKTYF
410 420 430 440 450
FVEDKFWRFD EKKQSMDPEF PRKIAENFPG IGTKVDAVFE AFGFLYFFSG
460 470
SSQLEFDPNA GKVTHILKSN SWFNC
Length:475
Mass (Da):53,428
Last modified:October 23, 1986 - v1
Checksum:iD81239DC3E26782E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02601 mRNA. Translation: CAA26448.1.
PIRiA00997. KCRTIH.
UniGeneiRn.32086.

Genome annotation databases

UCSCiRGD:621317. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02601 mRNA. Translation: CAA26448.1 .
PIRi A00997. KCRTIH.
UniGenei Rn.32086.

3D structure databases

ProteinModelPortali P03957.
SMRi P03957. Positions 31-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000012310.

Protein family/group databases

MEROPSi M10.005.

Proteomic databases

PaxDbi P03957.
PRIDEi P03957.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:621317. rat.

Organism-specific databases

RGDi 621317. Mmp3.

Phylogenomic databases

eggNOGi NOG258253.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P03957.
PhylomeDBi P03957.

Miscellaneous databases

NextBioi 13948460.
PROi P03957.

Gene expression databases

Genevestigatori P03957.

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. "Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts."
    Matrisian L.M., Glaichenhaus N., Gesnel M.-C., Breathnach R.
    EMBO J. 4:1435-1440(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts."
    Matrisian L.M., Gleroy P., Ruhlmann C., Gesnel M.-C., Breathnach R.
    Mol. Cell. Biol. 6:1679-1686(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin."
    Umenishi F., Yasumitsu H., Ashida Y., Yamauti J., Umeda M., Miyazaki K.
    J. Biochem. 108:537-543(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-28; 110-119; 309-315 AND 316-325.
  4. "Structure-function relationships in the collagenase family member transin."
    Sanchez-Lopez R., Nicholson R., Gesnel M.-C., Matrisian L.M., Breathnach R.
    J. Biol. Chem. 263:11892-11899(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, CHARACTERIZATION.

Entry informationi

Entry nameiMMP3_RAT
AccessioniPrimary (citable) accession number: P03957
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: November 26, 2014
This is version 141 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3