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Protein

Matrix metalloproteinase-17

Gene

Mmp17

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

Functioni

Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.1 Publication

Catalytic activityi

Cleaves pro-TNF-alpha at the 74-Ala-|-Gln-75 site.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi109Zinc; in inhibited formBy similarity1
Metal bindingi247Zinc; catalyticPROSITE-ProRule annotation1
Active sitei2481
Metal bindingi251Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi257Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • drinking behavior Source: MGI
  • kidney development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-17 (EC:3.4.24.-)
Short name:
MMP-17
Alternative name(s):
Membrane-type matrix metalloproteinase 4
Short name:
MT-MMP 4
Short name:
MTMMP4
Membrane-type-4 matrix metalloproteinase
Short name:
MT4-MMP
Short name:
MT4MMP
Gene namesi
Name:Mmp17
Synonyms:Mt4mmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1346076. Mmp17.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi248E → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
PropeptideiPRO_000002882140 – 124By similarityAdd BLAST85
ChainiPRO_0000028822125 – 558Matrix metalloproteinase-17Add BLAST434
PropeptideiPRO_0000028823559 – 578Removed in mature formSequence analysisAdd BLAST20

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi136N-linked (GlcNAc...)Sequence analysis1
Glycosylationi322N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi336 ↔ 527By similarity
Lipidationi558GPI-anchor amidated serineSequence analysis1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

Proteomic databases

PaxDbiQ9R0S3.
PeptideAtlasiQ9R0S3.
PRIDEiQ9R0S3.

2D gel databases

REPRODUCTION-2DPAGEQ9R0S3.

PTM databases

PhosphoSitePlusiQ9R0S3.

Expressioni

Tissue specificityi

Expressed by monocytes and macrophages.

Gene expression databases

BgeeiENSMUSG00000029436.
CleanExiMM_MMP17.
GenevisibleiQ9R0S3. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031390.

Structurei

3D structure databases

ProteinModelPortaliQ9R0S3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati333 – 382Hemopexin 1Add BLAST50
Repeati386 – 432Hemopexin 2Add BLAST47
Repeati436 – 479Hemopexin 3Add BLAST44
Repeati480 – 527Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi107 – 114Cysteine 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.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S3.
KOiK07997.
OMAiAHNDRTY.
OrthoDBiEOG091G03DP.
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.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028726. MMP17.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF21. PTHR10201:SF21. 2 hits.
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.
PROSITEiPS51642. 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.

Q9R0S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRPRGPGS PRGPGPPRPG PGLPPLLLVL ALAAHGGCAA PAPRAEDLSL
60 70 80 90 100
GVEWLSRFGY LPPADPASGQ LQTQEELSKA ITAMQQFGGL ETTGILDEAT
110 120 130 140 150
LALMKTPRCS LPDLPPGAQS RRKRQTPPPT KWSKRNLSWR VRTFPRDSPL
160 170 180 190 200
GRDTVRALMY YALKVWSDIT PLNFHEVAGN AADIQIDFSK ADHNDGYPFD
210 220 230 240 250
GPGGTVAHAF FPGDHHTAGD THFDDDEPWT FRSSDAHGMD LFAVAVHEFG
260 270 280 290 300
HAIGLSHVAA PSSIMQPYYQ GPVGDPLRYG LPYEDRVRVW QLYGVRESVS
310 320 330 340 350
PTAQLDTPEP EEPPLLPEPP NNRSSTPPQK DVPHRCTAHF DAVAQIRGEA
360 370 380 390 400
FFFKGKYFWR LTRDRHLVSL QPAQMHRFWR GLPLHLDSVD AVYERTSDHK
410 420 430 440 450
IVFFKGDRYW VFKDNNVEEG YPRPVSDFSL PPGGIDAVFS WAHNDRTYFF
460 470 480 490 500
KDQLYWRYDD HTRRMDPGYP AQGPLWRGVP SMLDDAMRWS DGASYFFRGQ
510 520 530 540 550
EYWKVLDGEL EAAPGYPQST ARDWLVCGEP LADAEDVGPG PQGRSGAQDG
560 570
LAVCSCTSDA HRLALPSLLL LTPLLWGL
Length:578
Mass (Da):64,333
Last modified:July 27, 2011 - v3
Checksum:i168C933B63A1EB7B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45A → G in CAB92315 (PubMed:10799478).Curated1
Sequence conflicti277L → V in BAA82708 (PubMed:10471807).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021224 mRNA. Translation: BAA82708.2.
AJ010731 mRNA. Translation: CAB92315.1.
CH466529 Genomic DNA. Translation: EDL19513.1.
BC051917 mRNA. Translation: AAH51917.1.
CCDSiCCDS19695.1.
RefSeqiNP_035976.3. NM_011846.5.
UniGeneiMm.42047.

Genome annotation databases

EnsembliENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
GeneIDi23948.
KEGGimmu:23948.
UCSCiuc008zsy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021224 mRNA. Translation: BAA82708.2.
AJ010731 mRNA. Translation: CAB92315.1.
CH466529 Genomic DNA. Translation: EDL19513.1.
BC051917 mRNA. Translation: AAH51917.1.
CCDSiCCDS19695.1.
RefSeqiNP_035976.3. NM_011846.5.
UniGeneiMm.42047.

3D structure databases

ProteinModelPortaliQ9R0S3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031390.

Protein family/group databases

MEROPSiM10.017.

PTM databases

PhosphoSitePlusiQ9R0S3.

2D gel databases

REPRODUCTION-2DPAGEQ9R0S3.

Proteomic databases

PaxDbiQ9R0S3.
PeptideAtlasiQ9R0S3.
PRIDEiQ9R0S3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
GeneIDi23948.
KEGGimmu:23948.
UCSCiuc008zsy.1. mouse.

Organism-specific databases

CTDi4326.
MGIiMGI:1346076. Mmp17.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S3.
KOiK07997.
OMAiAHNDRTY.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

Miscellaneous databases

PROiQ9R0S3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029436.
CleanExiMM_MMP17.
GenevisibleiQ9R0S3. 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.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028726. MMP17.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF21. PTHR10201:SF21. 2 hits.
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.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP17_MOUSE
AccessioniPrimary (citable) accession number: Q9R0S3
Secondary accession number(s): Q80UM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 144 of the entry and version 3 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

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.