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Protein

Matrix metalloproteinase-17

Gene

MMP17

Organism
Homo sapiens (Human)
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.

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 bindingi110Zinc; in inhibited formBy similarity1
Metal bindingi248Zinc; catalyticPROSITE-ProRule annotation1
Active sitei249PROSITE-ProRule annotation1
Metal bindingi252Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi258Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • enzyme activator activity Source: ProtInc
  • metalloaminopeptidase activity Source: ParkinsonsUK-UCL
  • metalloendopeptidase activity Source: ProtInc
  • zinc ion binding Source: ProtInc

GO - Biological processi

  • drinking behavior Source: Ensembl
  • kidney development Source: Ensembl
  • proteolysis Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1592389. Activation of Matrix Metalloproteinases.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7163. MMP17.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi4326.
OpenTargetsiENSG00000198598.
PharmGKBiPA30875.

Chemistry databases

ChEMBLiCHEMBL2937.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1641.

Polymorphism and mutation databases

BioMutaiMMP17.
DMDMi296439485.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
PropeptideiPRO_000002881836 – 125By similarityAdd BLAST90
ChainiPRO_0000028819126 – 565Matrix metalloproteinase-17Add BLAST440
PropeptideiPRO_0000028820566 – 603Removed in mature formSequence analysisAdd BLAST38

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi137N-linked (GlcNAc...)Sequence analysis1
Glycosylationi318N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi332 ↔ 523By similarity
Lipidationi565GPI-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

PaxDbiQ9ULZ9.
PeptideAtlasiQ9ULZ9.
PRIDEiQ9ULZ9.

PTM databases

iPTMnetiQ9ULZ9.
PhosphoSitePlusiQ9ULZ9.

Expressioni

Tissue specificityi

Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.

Gene expression databases

BgeeiENSG00000198598.
CleanExiHS_MMP17.
ExpressionAtlasiQ9ULZ9. baseline and differential.
GenevisibleiQ9ULZ9. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000353767.

Chemistry databases

BindingDBiQ9ULZ9.

Structurei

3D structure databases

ProteinModelPortaliQ9ULZ9.
SMRiQ9ULZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati333 – 378Hemopexin 1Add BLAST46
Repeati382 – 427Hemopexin 2Add BLAST46
Repeati428 – 475Hemopexin 3Add BLAST48
Repeati476 – 523Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi108 – 115Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi122 – 125Poly-Arg4

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.
HOVERGENiHBG052484.
InParanoidiQ9ULZ9.
KOiK07997.
OMAiAHNDRTY.
OrthoDBiEOG091G03DP.
PhylomeDBiQ9ULZ9.
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. 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.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q9ULZ9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRRRAARGPG PPPPGPGLSR LPLPLLLLLA LGTRGGCAAP APAPRAEDLS
60 70 80 90 100
LGVEWLSRFG YLPPADPTTG QLQTQEELSK AITAMQQFGG LEATGILDEA
110 120 130 140 150
TLALMKTPRC SLPDLPVLTQ ARRRRQAPAP TKWNKRNLSW RVRTFPRDSP
160 170 180 190 200
LGHDTVRALM YYALKVWSDI APLNFHEVAG SAADIQIDFS KADHNDGYPF
210 220 230 240 250
DGPGGTVAHA FFPGHHHTAG DTHFDDDEAW TFRSSDAHGM DLFAVAVHEF
260 270 280 290 300
GHAIGLSHVA AAHSIMRPYY QGPVGDPLRY GLPYEDKVRV WQLYGVRESV
310 320 330 340 350
SPTAQPEEPP LLPEPPDNRS SAPPRKDVPH RCSTHFDAVA QIRGEAFFFK
360 370 380 390 400
GKYFWRLTRD RHLVSLQPAQ MHRFWRGLPL HLDSVDAVYE RTSDHKIVFF
410 420 430 440 450
KGDRYWVFKD NNVEEGYPRP VSDFSLPPGG IDAAFSWAHN DRTYFFKDQL
460 470 480 490 500
YWRYDDHTRH MDPGYPAQSP LWRGVPSTLD DAMRWSDGAS YFFRGQEYWK
510 520 530 540 550
VLDGELEVAP GYPQSTARDW LVCGDSQADG SVAAGVDAAE GPRAPPGQHD
560 570 580 590 600
QSRSEDGYEV CSCTSGASSP PGAPGPLVAA TMLLLLPPLS PGALWTAAQA

LTL
Length:603
Mass (Da):66,653
Last modified:May 18, 2010 - v4
Checksum:iBB297B21973C7A0B
GO
Isoform Short (identifier: Q9ULZ9-2) [UniParc]FASTAAdd to basket
Also known as: Puente

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Show »
Length:519
Mass (Da):57,938
Checksum:iEB74B32E8A7619C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23L → LLPL in BAA82707 (PubMed:10471807).Curated1
Sequence conflicti23L → LLPL in CAA61753 (Ref. 2) Curated1
Sequence conflicti182A → T in BAA82707 (PubMed:10471807).Curated1
Sequence conflicti182A → T in CAA61753 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0054561 – 84Missing in isoform Short. 1 PublicationAdd BLAST84

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021225 mRNA. Translation: BAA82707.2.
X89576 mRNA. Translation: CAA61753.1.
AC131009 Genomic DNA. No translation available.
CCDSiCCDS31927.1. [Q9ULZ9-1]
RefSeqiNP_057239.4. NM_016155.5. [Q9ULZ9-1]
XP_011536657.1. XM_011538355.2. [Q9ULZ9-2]
XP_011536658.1. XM_011538356.2. [Q9ULZ9-2]
XP_011536659.1. XM_011538357.2. [Q9ULZ9-2]
UniGeneiHs.709245.

Genome annotation databases

EnsembliENST00000360564; ENSP00000353767; ENSG00000198598. [Q9ULZ9-1]
ENST00000535291; ENSP00000441106; ENSG00000198598. [Q9ULZ9-2]
GeneIDi4326.
KEGGihsa:4326.
UCSCiuc001ujc.2. human. [Q9ULZ9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021225 mRNA. Translation: BAA82707.2.
X89576 mRNA. Translation: CAA61753.1.
AC131009 Genomic DNA. No translation available.
CCDSiCCDS31927.1. [Q9ULZ9-1]
RefSeqiNP_057239.4. NM_016155.5. [Q9ULZ9-1]
XP_011536657.1. XM_011538355.2. [Q9ULZ9-2]
XP_011536658.1. XM_011538356.2. [Q9ULZ9-2]
XP_011536659.1. XM_011538357.2. [Q9ULZ9-2]
UniGeneiHs.709245.

3D structure databases

ProteinModelPortaliQ9ULZ9.
SMRiQ9ULZ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000353767.

Chemistry databases

BindingDBiQ9ULZ9.
ChEMBLiCHEMBL2937.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1641.

Protein family/group databases

MEROPSiM10.017.

PTM databases

iPTMnetiQ9ULZ9.
PhosphoSitePlusiQ9ULZ9.

Polymorphism and mutation databases

BioMutaiMMP17.
DMDMi296439485.

Proteomic databases

PaxDbiQ9ULZ9.
PeptideAtlasiQ9ULZ9.
PRIDEiQ9ULZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360564; ENSP00000353767; ENSG00000198598. [Q9ULZ9-1]
ENST00000535291; ENSP00000441106; ENSG00000198598. [Q9ULZ9-2]
GeneIDi4326.
KEGGihsa:4326.
UCSCiuc001ujc.2. human. [Q9ULZ9-1]

Organism-specific databases

CTDi4326.
DisGeNETi4326.
GeneCardsiMMP17.
H-InvDBHIX0036662.
HGNCiHGNC:7163. MMP17.
MIMi602285. gene.
neXtProtiNX_Q9ULZ9.
OpenTargetsiENSG00000198598.
PharmGKBiPA30875.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOVERGENiHBG052484.
InParanoidiQ9ULZ9.
KOiK07997.
OMAiAHNDRTY.
OrthoDBiEOG091G03DP.
PhylomeDBiQ9ULZ9.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiR-HSA-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

GeneWikiiMMP17.
GenomeRNAii4326.
PROiQ9ULZ9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198598.
CleanExiHS_MMP17.
ExpressionAtlasiQ9ULZ9. baseline and differential.
GenevisibleiQ9ULZ9. HS.

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. 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.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP17_HUMAN
AccessioniPrimary (citable) accession number: Q9ULZ9
Secondary accession number(s): Q14850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.