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Protein

Stromelysin-3

Gene

Mmp11

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

Functioni

May play an important role in the progression of epithelial malignancies.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca2+ ion per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi84Zinc 2; in inhibited formBy similarity1
Metal bindingi168Zinc 11
Metal bindingi170Zinc 11
Metal bindingi175Calcium1
Metal bindingi176Calcium; via carbonyl oxygen1
Metal bindingi178Calcium; via carbonyl oxygen1
Metal bindingi180Calcium; via carbonyl oxygen1
Metal bindingi183Zinc 11
Metal bindingi196Zinc 11
Metal bindingi219Zinc 2; catalytic1
Active sitei2201
Metal bindingi223Zinc 2; catalytic1
Metal bindingi229Zinc 2; catalytic1

GO - Molecular functioni

GO - Biological processi

  • basement membrane organization Source: MGI
  • collagen catabolic process Source: MGI
  • collagen fibril organization Source: MGI
  • extracellular matrix organization Source: MGI
  • multicellular organism development Source: InterPro
  • negative regulation of fat cell differentiation 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

BRENDAi3.4.24.B3. 3474.
ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1592389. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiM10.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-3 (EC:3.4.24.-)
Short name:
SL-3
Short name:
ST3
Alternative name(s):
Matrix metalloproteinase-11
Short name:
MMP-11
Gene namesi
Name:Mmp11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:97008. Mmp11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
PropeptideiPRO_000002877236 – 101Activation peptideBy similarityAdd BLAST66
ChainiPRO_0000028773102 – 492Stromelysin-3Add BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi298 ↔ 484By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ02853.
PRIDEiQ02853.

PTM databases

PhosphoSitePlusiQ02853.

Miscellaneous databases

PMAP-CutDBQ02853.

Expressioni

Tissue specificityi

Specifically expressed in the mammary gland during apoptosis.

Gene expression databases

BgeeiENSMUSG00000000901.
CleanExiMM_MMP11.
ExpressionAtlasiQ02853. baseline and differential.
GenevisibleiQ02853. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000924.

Chemistry databases

BindingDBiQ02853.

Structurei

Secondary structure

1492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi102 – 105Combined sources4
Beta strandi108 – 111Combined sources4
Beta strandi113 – 118Combined sources6
Helixi127 – 142Combined sources16
Beta strandi148 – 151Combined sources4
Beta strandi153 – 156Combined sources4
Beta strandi158 – 164Combined sources7
Beta strandi168 – 171Combined sources4
Beta strandi176 – 179Combined sources4
Beta strandi182 – 185Combined sources4
Beta strandi190 – 198Combined sources9
Beta strandi203 – 206Combined sources4
Beta strandi208 – 212Combined sources5
Helixi213 – 224Combined sources12
Helixi251 – 260Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HV5X-ray2.60A/B/C/D/E/F102-265[»]
ProteinModelPortaliQ02853.
SMRiQ02853.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02853.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati295 – 343Hemopexin 1Add BLAST49
Repeati344 – 386Hemopexin 2Add BLAST43
Repeati388 – 436Hemopexin 3Add BLAST49
Repeati437 – 484Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi82 – 89Cysteine 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.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ02853.
KOiK07993.
OMAiFFQGAQY.
OrthoDBiEOG091G03DP.
PhylomeDBiQ02853.
TreeFamiTF315428.

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.
IPR006026. Peptidase_Metallo.
IPR028705. Stromelysin-3.
[Graphical view]
PANTHERiPTHR10201:SF20. PTHR10201:SF20. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 1 hit.
PROSITEiPS00024. 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.

Q02853-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARAACLLRA ISRVLLLPLP LLLLLLLLLP SPLMARARPP ESHRHHPVKK
60 70 80 90 100
GPRLLHAALP NTLTSVPASH WVPSPAGSSR PLRCGVPDLP DVLNARNRQK
110 120 130 140 150
RFVLSGGRWE KTDLTYRILR FPWQLVREQV RQTVAEALQV WSEVTPLTFT
160 170 180 190 200
EVHEGRADIM IDFARYWHGD NLPFDGPGGI LAHAFFPKTH REGDVHFDYD
210 220 230 240 250
ETWTIGDNQG TDLLQVAAHE FGHVLGLQHT TAAKALMSPF YTFRYPLSLS
260 270 280 290 300
PDDRRGIQHL YGRPQMAPTS PAPTLSSQAG TDTNEIALLE PETPPDVCET
310 320 330 340 350
SFDAVSTIRG ELFFFKAGFV WRLRSGRLQP GYPALASRHW QGLPSPVDAA
360 370 380 390 400
FEDAQGQIWF FQGAQYWVYD GEKPVLGPAP LSKLGLQGSP VHAALVWGPE
410 420 430 440 450
KNKIYFFRGG DYWRFHPRTQ RVDNPVPRRS TDWRGVPSEI DAAFQDAEGY
460 470 480 490
AYFLRGHLYW KFDPVKVKVL EGFPRPVGPD FFDCAEPANT FR
Length:492
Mass (Da):55,441
Last modified:February 1, 1996 - v2
Checksum:iB54E260E4AB3D7C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12604 mRNA. Translation: CAA78248.1.
CCDSiCCDS23937.1.
PIRiA44399.
RefSeqiNP_001293113.1. NM_001306184.1.
NP_032632.1. NM_008606.3.
UniGeneiMm.4561.

Genome annotation databases

EnsembliENSMUST00000000924; ENSMUSP00000000924; ENSMUSG00000000901.
ENSMUST00000120281; ENSMUSP00000112940; ENSMUSG00000000901.
GeneIDi17385.
KEGGimmu:17385.
UCSCiuc007fto.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12604 mRNA. Translation: CAA78248.1.
CCDSiCCDS23937.1.
PIRiA44399.
RefSeqiNP_001293113.1. NM_001306184.1.
NP_032632.1. NM_008606.3.
UniGeneiMm.4561.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HV5X-ray2.60A/B/C/D/E/F102-265[»]
ProteinModelPortaliQ02853.
SMRiQ02853.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000924.

Chemistry databases

BindingDBiQ02853.
ChEMBLiCHEMBL3412.

Protein family/group databases

MEROPSiM10.007.

PTM databases

PhosphoSitePlusiQ02853.

Proteomic databases

PaxDbiQ02853.
PRIDEiQ02853.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000924; ENSMUSP00000000924; ENSMUSG00000000901.
ENSMUST00000120281; ENSMUSP00000112940; ENSMUSG00000000901.
GeneIDi17385.
KEGGimmu:17385.
UCSCiuc007fto.1. mouse.

Organism-specific databases

CTDi4320.
MGIiMGI:97008. Mmp11.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ02853.
KOiK07993.
OMAiFFQGAQY.
OrthoDBiEOG091G03DP.
PhylomeDBiQ02853.
TreeFamiTF315428.

Enzyme and pathway databases

BRENDAi3.4.24.B3. 3474.
ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

EvolutionaryTraceiQ02853.
PMAP-CutDBQ02853.
PROiQ02853.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000901.
CleanExiMM_MMP11.
ExpressionAtlasiQ02853. baseline and differential.
GenevisibleiQ02853. MM.

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.
IPR006026. Peptidase_Metallo.
IPR028705. Stromelysin-3.
[Graphical view]
PANTHERiPTHR10201:SF20. PTHR10201:SF20. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 1 hit.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP11_MOUSE
AccessioniPrimary (citable) accession number: Q02853
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 158 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.