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Protein

Stromelysin-1

Gene

Mmp3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

Preferential cleavage where P1', P2' and P3' are hydrophobic residues.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • Ca2+1 PublicationNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Inhibited by a synthetic peptide corresponding to the inhibitory cysteine switch motif (PubMed:1988438). Inhibited by ethylenediaminetetraacetic acid (EDTA), 1,10-pheanthroline, 2-mecaptoethanol, dithiothreitol and metalloproteinase inhibitor protein TIMP (PubMed:1963430, PubMed:2841336).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi90Zinc 2; in inhibited formBy similarity1
Metal bindingi122Calcium 1By similarity1
Metal bindingi156Calcium 2By similarity1
Metal bindingi166Zinc 1By similarity1
Metal bindingi168Zinc 1By similarity1
Metal bindingi173Calcium 3By similarity1
Metal bindingi174Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi176Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi181Zinc 1By similarity1
Metal bindingi188Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi190Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi192Calcium 2By similarity1
Metal bindingi194Zinc 1By similarity1
Metal bindingi196Calcium 3By similarity1
Metal bindingi197Calcium 1By similarity1
Metal bindingi199Calcium 1By similarity1
Metal bindingi199Calcium 3By similarity1
Metal bindingi216Zinc 2; catalyticBy similarity1
Active sitei2171 Publication1
Metal bindingi220Zinc 2; catalyticBy similarity1
Metal bindingi226Zinc 2; catalyticBy similarity1
Metal bindingi295Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi387Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi436Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

  • metalloendopeptidase activity Source: InterPro
  • protein complex binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to cell-matrix adhesion Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • collagen catabolic process Source: UniProtKB-KW
  • female pregnancy Source: RGD
  • positive regulation of cell migration Source: RGD
  • response to amino acid Source: RGD
  • response to cytokine Source: RGD
  • response to estradiol Source: RGD
  • response to hypoxia Source: RGD
  • response to interleukin-1 Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to tumor necrosis factor Source: RGD
  • wound healing Source: RGD

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-1 (EC:3.4.24.173 Publications)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621317. Mmp3.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: RGD
  • dendrite Source: RGD
  • extracellular space Source: RGD
  • nucleus Source: RGD
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • protein complex Source: RGD

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi85M → L: Does not induce autoproteolytic activation. 1 Publication1
Mutagenesisi88P → A: Does not induce autoproteolytic activation. 1 Publication1
Mutagenesisi88P → G or L: Induces partial autoproteolytic activation. 2 Publications1
Mutagenesisi89R → K, L or Q: Induces constitutive autoproteolytic activation. 1 Publication1
Mutagenesisi90C → S, H or D: Induces constitutive autoproteolytic activation. 1 Publication1
Mutagenesisi91G → A: Induces constitutive autoproteolytic activation. 1 Publication1
Mutagenesisi92V → G: Induces constitutive autoproteolytic activation. 1 Publication1
Mutagenesisi92V → I or A: Induces partial autoproteolytic activation. 1 Publication1
Mutagenesisi92V → L or D: Does not induce autoproteolytic activation. 1 Publication1
Mutagenesisi93P → V, G or N: Induces partial autoproteolytic activation. 2 Publications1
Mutagenesisi98F → S: Loss of autocleavage without affecting acitvation by APMA. 1 Publication1
Mutagenesisi216H → L: Loss of autoproteolytic activation and catalytic activity. 1 Publication1
Mutagenesisi217E → G: Loss of autoproteolytic activation and catalytic activity. 1 Publication1
Mutagenesisi226H → S: Loss of autoproteolytic activation and catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17CuratedAdd BLAST17
PropeptideiPRO_000002873418 – 97Activation peptide1 PublicationAdd BLAST80
ChainiPRO_000002873598 – 475Stromelysin-1Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi118N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi288 ↔ 475By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP03957.

PTM databases

PhosphoSitePlusiP03957.

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.

Interactioni

GO - Molecular functioni

  • protein complex binding Source: RGD

Structurei

3D structure databases

ProteinModelPortaliP03957.
SMRiP03957.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati285 – 334Hemopexin 1Add BLAST50
Repeati335 – 381Hemopexin 2Add BLAST47
Repeati383 – 431Hemopexin 3Add BLAST49
Repeati432 – 475Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi88 – 95Cysteine switch2 Publications8

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.2 Publications

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP03957.
PhylomeDBiP03957.

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.
InterProiView protein in InterPro
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1.
PANTHERiPTHR10201:SF198. PTHR10201:SF198. 1 hit.
PfamiView protein in Pfam
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiView protein in SMART
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiView protein in PROSITE
PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.

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.

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.

Entry informationi

Entry nameiMMP3_RAT
AccessioniPrimary (citable) accession number: P03957
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: July 5, 2017
This is version 156 of the entry and version 1 of the sequence. See 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