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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Zinc 2; in inhibited formBy similarity
Metal bindingi131 – 1311Calcium 1By similarity
Metal bindingi165 – 1651Calcium 2By similarity
Metal bindingi175 – 1751Zinc 1By similarity
Metal bindingi177 – 1771Zinc 1By similarity
Metal bindingi182 – 1821Calcium 3By similarity
Metal bindingi183 – 1831Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi190 – 1901Zinc 1By similarity
Metal bindingi197 – 1971Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi199 – 1991Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi201 – 2011Calcium 2By similarity
Metal bindingi203 – 2031Zinc 1By similarity
Metal bindingi205 – 2051Calcium 3By similarity
Metal bindingi206 – 2061Calcium 1By similarity
Metal bindingi208 – 2081Calcium 3By similarity
Metal bindingi400 – 4001Zinc 2; catalyticBy similarity
Active sitei401 – 4011PROSITE-ProRule annotation
Metal bindingi404 – 4041Zinc 2; catalyticBy similarity
Metal bindingi410 – 4101Zinc 2; catalyticBy similarity
Metal bindingi479 – 4791Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi524 – 5241Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi572 – 5721Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi621 – 6211Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

  • metalloendopeptidase activity Source: AgBase
  • zinc ion binding Source: InterPro

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
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Propeptidei27 – 10680Activation peptide1 PublicationPRO_0000028722Add
BLAST
Chaini107 – 66355772 kDa type IV collagenasePRO_0000028723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.

Expressioni

Tissue specificityi

Produced by normal skin fibroblasts.

Interactioni

Subunit structurei

Ligand for integrin alpha-V/beta-3.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005656.

Structurei

3D structure databases

ProteinModelPortaliQ90611.
SMRiQ90611. Positions 29-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 27349Fibronectin type-II 1PROSITE-ProRule annotationAdd
BLAST
Domaini283 – 33149Fibronectin type-II 2PROSITE-ProRule annotationAdd
BLAST
Domaini341 – 38949Fibronectin type-II 3PROSITE-ProRule annotationAdd
BLAST
Repeati475 – 51945Hemopexin 1Add
BLAST
Repeati520 – 56647Hemopexin 2Add
BLAST
Repeati568 – 61649Hemopexin 3Add
BLAST
Repeati617 – 66347Hemopexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 218112Collagenase-like 1Add
BLAST
Regioni219 – 393175Collagen-bindingAdd
BLAST
Regioni394 – 46875Collagenase-like 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi97 – 1048Cysteine switchBy similarity

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.
GeneTreeiENSGT00830000128254.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiQ90611.
KOiK01398.
OMAiPCKFPFR.
OrthoDBiEOG70KGNX.
PhylomeDBiQ90611.
TreeFamiTF315428.

Family and domain databases

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401P → Q AA sequence (PubMed:1848240).Curated
Sequence conflicti116 – 1161W → T AA sequence (PubMed:1848240).Curated
Sequence conflicti122 – 1221T → I AA sequence (PubMed:1848240).Curated

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.
SMRiQ90611. Positions 29-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005656.

Protein family/group databases

MEROPSiM10.003.

Proteomic databases

PaxDbiQ90611.

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.
GeneTreeiENSGT00830000128254.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiQ90611.
KOiK01398.
OMAiPCKFPFR.
OrthoDBiEOG70KGNX.
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

NextBioi20813946.
PROiQ90611.

Family and domain databases

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.
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...

Publicationsi

  1. "Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation."
    Aimes R.T., French D.L., Quigley J.P.
    Biochem. J. 300:729-736(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts."
    Chen J.-M., Aimes R.T., Ward G.R., Youngleib G.L., Quigley J.P.
    J. Biol. Chem. 266:5113-5121(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41 AND 107-122.

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: April 13, 2016
This is version 134 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.