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Protein

Matrix metalloproteinase-25

Gene

Mmp25

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

Functioni

May activate progelatinase A.By similarity

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 bindingi145Zinc; in inhibited formBy similarity1
Metal bindingi287Zinc; catalyticPROSITE-ProRule annotation1
Active sitei288PROSITE-ProRule annotation1
Metal bindingi291Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi297Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • hard palate development Source: MGI
  • inflammatory response Source: InterPro
  • proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiM10.024.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-25 (EC:3.4.24.-)
Short name:
MMP-25
Gene namesi
Name:Mmp25
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2443938. Mmp25.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei53 – 73HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00002886351 – 162By similarityAdd BLAST162
ChainiPRO_0000288636163 – 593Matrix metalloproteinase-25Add BLAST431
PropeptideiPRO_0000288637594 – 615Removed in mature formSequence analysisAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi371 ↔ 562By similarity
Lipidationi593GPI-anchor amidated alanineSequence analysis1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

Proteomic databases

MaxQBiQ3U435.
PaxDbiQ3U435.
PRIDEiQ3U435.

PTM databases

PhosphoSitePlusiQ3U435.

Expressioni

Gene expression databases

BgeeiENSMUSG00000023903.
CleanExiMM_MMP25.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024696.

Structurei

3D structure databases

ProteinModelPortaliQ3U435.
SMRiQ3U435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati368 – 417Hemopexin 1Add BLAST50
Repeati421 – 466Hemopexin 2Add BLAST46
Repeati467 – 515Hemopexin 3Add BLAST49
Repeati516 – 562Hemopexin 4Add BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi143 – 150Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi158 – 162Poly-Arg5
Compositional biasi340 – 368Pro-richAdd BLAST29

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, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ3U435.
KOiK08003.
OMAiHYWRFPK.
OrthoDBiEOG091G03DP.
PhylomeDBiQ3U435.
TreeFamiTF315428.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028733. MMP25.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF142. PTHR10201:SF142. 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]

Sequencei

Sequence statusi: Complete.

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

Q3U435-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCFPGSQISP ARLYYLVSAP WICTGSLTSS RLPRRRESGP LRVPPRSVQA
60 70 80 90 100
ERILRLPAFG LPLLALLLVP LLPVRAQNPD AKVVSMGVEW LTRYGYLPPA
110 120 130 140 150
DPVHAQMQSL EKLQDAIKVM QRFAGLPETG QMDPMTIKTM RKPRCSLPDV
160 170 180 190 200
LGAAGLVRRR RRYSLSGSVW KKRTLTWSIR SFSQKSQLSP QIVRTLLSYA
210 220 230 240 250
LAVWATESGL TFQEVNSQYQ EPDIIIHFAR AYHQDSYPFD GSGGTLAHAF
260 270 280 290 300
FPGEHPISGD THFDDEETWT FGSTDDNGID LFAVAVHEFG HALGLGHSSA
310 320 330 340 350
PNSIMRPFYQ GPVGDPATYR LPQDDRDGLQ QLYGRVSQNP NARPTRKPLV
360 370 380 390 400
PPPQPPAMPP DSPATPVPDR CEGNFDAVAN IRGEIFLFKG PWFWRLQPSG
410 420 430 440 450
QLVSPRPAGL HRFWEGLPTH VKVIQAAYAR PLDGRIILFS GPQFWVFQER
460 470 480 490 500
QLEGAARPLV EFGLPPGEDV DAVFSWPHNG KTYLIRGQKY WRYDEVAARP
510 520 530 540 550
DPGYPRALSL WDGAPFAPDD VTISNTGDTY FFKGTHFWRF AEGSVKAESD
560 570 580 590 600
SPQPIGPKWL DCPAPNSDPR VTSPPKTTSK TRSCDCHCEL NQASEQLSPL
610
LLPLLPLVAG EVFSY
Length:615
Mass (Da):68,496
Last modified:October 11, 2005 - v1
Checksum:i7B0842CACF06382D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154458 mRNA. Translation: BAE32600.1.
BC112379 mRNA. Translation: AAI12380.1.
CCDSiCCDS28452.1.
RefSeqiNP_001028511.1. NM_001033339.4.
UniGeneiMm.235343.

Genome annotation databases

EnsembliENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
GeneIDi240047.
KEGGimmu:240047.
UCSCiuc008asq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154458 mRNA. Translation: BAE32600.1.
BC112379 mRNA. Translation: AAI12380.1.
CCDSiCCDS28452.1.
RefSeqiNP_001028511.1. NM_001033339.4.
UniGeneiMm.235343.

3D structure databases

ProteinModelPortaliQ3U435.
SMRiQ3U435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024696.

Protein family/group databases

MEROPSiM10.024.

PTM databases

PhosphoSitePlusiQ3U435.

Proteomic databases

MaxQBiQ3U435.
PaxDbiQ3U435.
PRIDEiQ3U435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
GeneIDi240047.
KEGGimmu:240047.
UCSCiuc008asq.1. mouse.

Organism-specific databases

CTDi64386.
MGIiMGI:2443938. Mmp25.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ3U435.
KOiK08003.
OMAiHYWRFPK.
OrthoDBiEOG091G03DP.
PhylomeDBiQ3U435.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiQ3U435.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000023903.
CleanExiMM_MMP25.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028733. MMP25.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF142. PTHR10201:SF142. 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 nameiMMP25_MOUSE
AccessioniPrimary (citable) accession number: Q3U435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: November 30, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In contrast to the human ortholog it does not have a signal sequence as it has an additional 53 residue sequence at the N-terminus. At the position of the human initiation methionine there is a leucine (Leu-54).Curated

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.