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Protein

72 kDa type IV collagenase

Gene

MMP2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99Zinc 2; in inhibited formBy similarity1
Metal bindingi131Calcium 1By similarity1
Metal bindingi165Calcium 2By similarity1
Metal bindingi175Zinc 1By similarity1
Metal bindingi177Zinc 1By similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi183Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi190Zinc 1By similarity1
Metal bindingi197Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi199Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi201Calcium 2By similarity1
Metal bindingi203Zinc 1By similarity1
Metal bindingi205Calcium 3By similarity1
Metal bindingi206Calcium 1By similarity1
Metal bindingi208Calcium 3By similarity1
Metal bindingi400Zinc 2; catalyticBy similarity1
Active sitei401PROSITE-ProRule annotation1
Metal bindingi404Zinc 2; catalyticBy similarity1
Metal bindingi410Zinc 2; catalyticBy similarity1
Metal bindingi479Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi524Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi572Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi621Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • blood vessel maturation Source: Ensembl
  • bone trabecula formation Source: Ensembl
  • cellular response to amino acid stimulus Source: Ensembl
  • cellular response to insulin-like growth factor stimulus Source: AgBase
  • collagen catabolic process Source: UniProtKB-KW
  • endodermal cell differentiation Source: Ensembl
  • face morphogenesis Source: Ensembl
  • intramembranous ossification Source: Ensembl
  • negative regulation of cartilage condensation Source: AgBase
  • negative regulation of cartilage development Source: AgBase
  • negative regulation of focal adhesion assembly Source: AgBase
  • negative regulation of protein phosphorylation Source: AgBase
  • positive regulation of innate immune response Source: Ensembl
  • positive regulation of vascular smooth muscle cell proliferation Source: Ensembl
  • regulation of MAPK cascade Source: AgBase
  • response to hypoxia Source: Ensembl
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-GGA-1442490. Collagen degradation.
R-GGA-1474228. Degradation of the extracellular matrix.
R-GGA-1592389. Activation of Matrix Metalloproteinases.
R-GGA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.

Protein family/group databases

MEROPSiM10.003.

Names & Taxonomyi

Protein namesi
Recommended name:
72 kDa type IV collagenase (EC:3.4.24.24)
Alternative name(s):
72 kDa gelatinase
Gelatinase A
Matrix metalloproteinase-2
Short name:
MMP-2
Gene namesi
Name:MMP2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 11

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: AgBase
  • cell Source: AgBase
  • extracellular matrix Source: AgBase
  • extracellular space Source: AgBase
  • mitochondrion Source: Ensembl
  • plasma membrane Source: Ensembl
  • sarcomere Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
PropeptideiPRO_000002872227 – 106Activation peptide1 PublicationAdd BLAST80
ChainiPRO_0000028723107 – 66372 kDa type IV collagenaseAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi230 ↔ 256PROSITE-ProRule annotation
Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
Disulfide bondi346 ↔ 372PROSITE-ProRule annotation
Disulfide bondi360 ↔ 387PROSITE-ProRule annotation
Disulfide bondi472 ↔ 663PROSITE-ProRule annotation

Post-translational modificationi

The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3).By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ90611.
PRIDEiQ90611.

Expressioni

Tissue specificityi

Produced by normal skin fibroblasts.

Gene expression databases

BgeeiENSGALG00000003580.

Interactioni

Subunit structurei

Ligand for integrin alpha-V/beta-3.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005656.

Structurei

3D structure databases

ProteinModelPortaliQ90611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 273Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini283 – 331Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini341 – 389Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati475 – 519Hemopexin 1Add BLAST45
Repeati520 – 566Hemopexin 2Add BLAST47
Repeati568 – 616Hemopexin 3Add BLAST49
Repeati617 – 663Hemopexin 4Add BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni107 – 218Collagenase-like 1Add BLAST112
Regioni219 – 393Collagen-bindingAdd BLAST175
Regioni394 – 468Collagenase-like 2Add BLAST75

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi97 – 104Cysteine 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 3 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiQ90611.
KOiK01398.
OMAiKHESCTS.
OrthoDBiEOG091G03DP.
PhylomeDBiQ90611.
TreeFamiTF315428.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR028708. 72kDa_collagenase.
IPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF29. PTHR10201:SF29. 2 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. 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.

Q90611-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTHSVFGFF FKVLLIQVYL FNKTLAAPSP IIKFPGDSTP KTDKELAVQY
60 70 80 90 100
LNKYYGCPKD NCNLFVLKDT LKKMQKFFGL PETGDLDQNT IETMKKPRCG
110 120 130 140 150
NPDVANYNFF PRKPKWEKNH ITYRIIGYTP DLDPETVDDA FARAFKVWSD
160 170 180 190 200
VTPLRFNRIN DGEADIMINF GRWEHGDGYP FDGKDGLLAH AFAPGPGIGG
210 220 230 240 250
DSHFDDDELW TLGEGQVVRV KYGNADGEYC KFPFWFNGKE YNSCTDAGRN
260 270 280 290 300
DGFLWCSTTK DFDADGKYGF CPHESLFTMG GNGDGQPCKF PFKFQGQSYD
310 320 330 340 350
QCTTEGRTDG YRWCGTTEDY DRDKKYGFCP ETAMSTVGGN SEGAPCVFPF
360 370 380 390 400
IFLGNKYDSC TSAGRNDGKL WCASTSSYDD DRKWGFCPDQ GYSLFLVAAH
410 420 430 440 450
EFGHAMGLEH SEDPGALMAP IYTYTKNFRL SQDDIKGIQE LYEVSPDVEP
460 470 480 490 500
GPGPGPGPGP RPTLGPVTPE LCKHDIVFDG VAQIRGEIFF FKDRFMWRTV
510 520 530 540 550
NPRGKPTGPL LVATFWPDLP EKIDAVYESP QDEKAVFFAG NEYWVYTASN
560 570 580 590 600
LDRGYPKKLT SLGLPPDVQR IDAAFNWGRN KKTYIFSGDR YWKYNEEKKK
610 620 630 640 650
MELATPKFIA DSWNGVPDNL DAVLGLTDSG YTYFFKDQYY LQMEDKSLKI
660
VKIGKISSDW LGC
Length:663
Mass (Da):74,941
Last modified:November 1, 1997 - v1
Checksum:i8D6FDA4E67C3EBCA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40P → Q AA sequence (PubMed:1848240).Curated1
Sequence conflicti116W → T AA sequence (PubMed:1848240).Curated1
Sequence conflicti122T → I AA sequence (PubMed:1848240).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07775 mRNA. Translation: AAA19596.1.
PIRiS46492.
RefSeqiNP_989751.1. NM_204420.2.
UniGeneiGga.3199.

Genome annotation databases

EnsembliENSGALT00000005666; ENSGALP00000005656; ENSGALG00000003580.
GeneIDi386583.
KEGGigga:386583.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07775 mRNA. Translation: AAA19596.1.
PIRiS46492.
RefSeqiNP_989751.1. NM_204420.2.
UniGeneiGga.3199.

3D structure databases

ProteinModelPortaliQ90611.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005656.

Protein family/group databases

MEROPSiM10.003.

Proteomic databases

PaxDbiQ90611.
PRIDEiQ90611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000005666; ENSGALP00000005656; ENSGALG00000003580.
GeneIDi386583.
KEGGigga:386583.

Organism-specific databases

CTDi4313.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiQ90611.
KOiK01398.
OMAiKHESCTS.
OrthoDBiEOG091G03DP.
PhylomeDBiQ90611.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiR-GGA-1442490. Collagen degradation.
R-GGA-1474228. Degradation of the extracellular matrix.
R-GGA-1592389. Activation of Matrix Metalloproteinases.
R-GGA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

PROiQ90611.

Gene expression databases

BgeeiENSGALG00000003580.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR028708. 72kDa_collagenase.
IPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF29. PTHR10201:SF29. 2 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP2_CHICK
AccessioniPrimary (citable) accession number: Q90611
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 139 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, Direct protein sequencing, 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.