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Protein

Stromelysin-3

Gene

Mmp11

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

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 1By similarity1
Metal bindingi170Zinc 1By similarity1
Metal bindingi175CalciumBy similarity1
Metal bindingi176Calcium; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium; via carbonyl oxygenBy similarity1
Metal bindingi180Calcium; via carbonyl oxygenBy similarity1
Metal bindingi183Zinc 1By similarity1
Metal bindingi196Zinc 1By similarity1
Metal bindingi218Zinc 2; catalyticBy similarity1
Active sitei219PROSITE-ProRule annotation1
Metal bindingi222Zinc 2; catalyticBy similarity1
Metal bindingi228Zinc 2; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi3099. Mmp11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
PropeptideiPRO_000004264936 – 101Activation peptideBy similarityAdd BLAST66
ChainiPRO_0000042650102 – 491Stromelysin-3Add BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi297 ↔ 483By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ499S5.
PRIDEiQ499S5.

PTM databases

PhosphoSitePlusiQ499S5.

Expressioni

Tissue specificityi

Highly expressed in ovary and uterus.1 Publication

Inductioni

In skin fibroblasts of superficial dermis upon skin lesion with highest level between days 5-10.1 Publication

Gene expression databases

BgeeiENSRNOG00000028344.
GenevisibleiQ499S5. RN.

Interactioni

Protein-protein interaction databases

BioGridi247514. 2 interactors.
STRINGi10116.ENSRNOP00000035334.

Structurei

3D structure databases

ProteinModelPortaliQ499S5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati298 – 342Hemopexin 1Add BLAST45
Repeati343 – 385Hemopexin 2Add BLAST43
Repeati387 – 435Hemopexin 3Add BLAST49
Repeati436 – 483Hemopexin 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.
InParanoidiQ499S5.
KOiK07993.
OMAiFFQGAQY.
OrthoDBiEOG091G03DP.
PhylomeDBiQ499S5.

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.

Q499S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARAACLLRA ISRALLLPLP LLLLLLLLLP PQLMARARPP ENHRHRPVKR
60 70 80 90 100
VPQLLPAALP NSLPSVPASH WVPGPASSSR PLRCGVPDPP DVLNARNRQK
110 120 130 140 150
RFVLSGGRWE KTDLTYRILR FPWQLVREQV RQTVAEALRV WSEVTPLTFT
160 170 180 190 200
EVHEGRADIM IDFTRYWHGD NLPFDGPGGI LAHAFFPKTH REGDVHFDYD
210 220 230 240 250
ETWTIGDKGT DLLQVAAHEF GHVLGLQHTT AAKALMSPFY TFRYPLSLSP
260 270 280 290 300
DDRRGIQHLY GRPQLTPTSP TPTLSSQAGT DTNEIALQEP EVPPEVCETS
310 320 330 340 350
FDAVSTIRGE LFFFKAGFVW RLRSGQLQPG YPALASRHWQ GLPSPVDAAF
360 370 380 390 400
EDAQGQIWFF QGAQYWVYDG EKPVLGPAPL SKLGLQGSPV HAALVWGPEK
410 420 430 440 450
NKIYFFRGGD YWRFHPRTQR VDNPVPRRTT DWRGVPSEID AAFQDAEGYA
460 470 480 490
YFLRGHLYWK FDPVKVKVLE SFPRPIGPDF FDCAEPANTF R
Length:491
Mass (Da):55,511
Last modified:September 13, 2005 - v1
Checksum:iB0C5B191A623FD41
GO

Sequence cautioni

The sequence AAC53061 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH99781 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46034 mRNA. Translation: AAC53061.1. Different initiation.
BC099781 mRNA. Translation: AAH99781.2. Different initiation.
RefSeqiNP_037112.2. NM_012980.2.
XP_008772050.1. XM_008773828.2.
UniGeneiRn.11123.

Genome annotation databases

EnsembliENSRNOT00000031400; ENSRNOP00000035334; ENSRNOG00000028344.
ENSRNOT00000087725; ENSRNOP00000074176; ENSRNOG00000054959.
GeneIDi103694874.
25481.
KEGGirno:103694874.
rno:25481.
UCSCiRGD:3099. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46034 mRNA. Translation: AAC53061.1. Different initiation.
BC099781 mRNA. Translation: AAH99781.2. Different initiation.
RefSeqiNP_037112.2. NM_012980.2.
XP_008772050.1. XM_008773828.2.
UniGeneiRn.11123.

3D structure databases

ProteinModelPortaliQ499S5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247514. 2 interactors.
STRINGi10116.ENSRNOP00000035334.

Protein family/group databases

MEROPSiM10.007.

PTM databases

PhosphoSitePlusiQ499S5.

Proteomic databases

PaxDbiQ499S5.
PRIDEiQ499S5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000031400; ENSRNOP00000035334; ENSRNOG00000028344.
ENSRNOT00000087725; ENSRNOP00000074176; ENSRNOG00000054959.
GeneIDi103694874.
25481.
KEGGirno:103694874.
rno:25481.
UCSCiRGD:3099. rat.

Organism-specific databases

CTDi4320.
RGDi3099. Mmp11.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ499S5.
KOiK07993.
OMAiFFQGAQY.
OrthoDBiEOG091G03DP.
PhylomeDBiQ499S5.

Enzyme and pathway databases

ReactomeiR-RNO-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

PROiQ499S5.

Gene expression databases

BgeeiENSRNOG00000028344.
GenevisibleiQ499S5. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q499S5
Secondary accession number(s): P97568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: September 13, 2005
Last modified: November 30, 2016
This is version 93 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, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.