MMP2_CHICK
ID MMP2_CHICK Reviewed; 663 AA.
AC Q90611;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=72 kDa type IV collagenase;
DE EC=3.4.24.24 {ECO:0000250|UniProtKB:P08253};
DE AltName: Full=72 kDa gelatinase;
DE AltName: Full=Gelatinase A;
DE AltName: Full=Matrix metalloproteinase-2;
DE Short=MMP-2;
DE Flags: Precursor;
GN Name=MMP2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8010954; DOI=10.1042/bj3000729;
RA Aimes R.T., French D.L., Quigley J.P.;
RT "Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken
RT embryo fibroblasts using gene family PCR: expression of the gelatinase
RT increases upon malignant transformation.";
RL Biochem. J. 300:729-736(1994).
RN [2]
RP PROTEIN SEQUENCE OF 27-41 AND 107-122.
RX PubMed=1848240; DOI=10.1016/s0021-9258(19)67762-8;
RA Chen J.-M., Aimes R.T., Ward G.R., Youngleib G.L., Quigley J.P.;
RT "Isolation and characterization of a 70-kDa metalloprotease (gelatinase)
RT that is elevated in Rous sarcoma virus-transformed chicken embryo
RT fibroblasts.";
RL J. Biol. Chem. 266:5113-5121(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X.
CC Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.;
CC EC=3.4.24.24; Evidence={ECO:0000250|UniProtKB:P08253};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P08253};
CC Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08253};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253};
CC -!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Produced by normal skin fibroblasts.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-
CC MMP3). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; U07775; AAA19596.1; -; mRNA.
DR PIR; S46492; S46492.
DR RefSeq; NP_989751.1; NM_204420.2.
DR AlphaFoldDB; Q90611; -.
DR SMR; Q90611; -.
DR STRING; 9031.ENSGALP00000005656; -.
DR MEROPS; M10.003; -.
DR PaxDb; Q90611; -.
DR Ensembl; ENSGALT00000005666; ENSGALP00000005656; ENSGALG00000003580.
DR GeneID; 386583; -.
DR KEGG; gga:386583; -.
DR CTD; 4313; -.
DR VEuPathDB; HostDB:geneid_386583; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000158511; -.
DR HOGENOM; CLU_015489_6_2_1; -.
DR InParanoid; Q90611; -.
DR OMA; RNDGFLW; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q90611; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.24; 1306.
DR Reactome; R-GGA-1442490; Collagen degradation.
DR Reactome; R-GGA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-GGA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:Q90611; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000003580; Expressed in colon and 12 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:AgBase.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030017; C:sarcomere; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001955; P:blood vessel maturation; IEA:Ensembl.
DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IMP:AgBase.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0071492; P:cellular response to UV-A; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:1904932; P:negative regulation of cartilage condensation; IMP:AgBase.
DR GO; GO:0061037; P:negative regulation of cartilage development; IMP:AgBase.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:AgBase.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:AgBase.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:AgBase.
DR GO; GO:1904645; P:response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR GO; GO:0048771; P:tissue remodeling; IBA:GO_Central.
DR CDD; cd00062; FN2; 3.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 2.
DR InterPro; IPR028708; 72kDa_collagenase.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR PANTHER; PTHR10201:SF29; PTHR10201:SF29; 1.
DR Pfam; PF00040; fn2; 3.
DR Pfam; PF00045; Hemopexin; 3.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00059; FN2; 3.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF57440; SSF57440; 3.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00023; FN2_1; 3.
DR PROSITE; PS51092; FN2_2; 3.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen degradation; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1848240"
FT PROPEP 27..106
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1848240"
FT /id="PRO_0000028722"
FT CHAIN 107..663
FT /note="72 kDa type IV collagenase"
FT /id="PRO_0000028723"
FT DOMAIN 225..273
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 283..331
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 341..389
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 475..519
FT /note="Hemopexin 1"
FT REPEAT 520..566
FT /note="Hemopexin 2"
FT REPEAT 568..616
FT /note="Hemopexin 3"
FT REPEAT 617..663
FT /note="Hemopexin 4"
FT REGION 107..218
FT /note="Collagenase-like 1"
FT REGION 219..393
FT /note="Collagen-binding"
FT REGION 394..468
FT /note="Collagenase-like 2"
FT REGION 445..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..104
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 449..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 524
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT DISULFID 230..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 244..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 288..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 302..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 346..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 360..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 472..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CONFLICT 40
FT /note="P -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="W -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="T -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 74941 MW; 8D6FDA4E67C3EBCA CRC64;
MKTHSVFGFF FKVLLIQVYL FNKTLAAPSP IIKFPGDSTP KTDKELAVQY LNKYYGCPKD
NCNLFVLKDT LKKMQKFFGL PETGDLDQNT IETMKKPRCG NPDVANYNFF PRKPKWEKNH
ITYRIIGYTP DLDPETVDDA FARAFKVWSD VTPLRFNRIN DGEADIMINF GRWEHGDGYP
FDGKDGLLAH AFAPGPGIGG DSHFDDDELW TLGEGQVVRV KYGNADGEYC KFPFWFNGKE
YNSCTDAGRN DGFLWCSTTK DFDADGKYGF CPHESLFTMG GNGDGQPCKF PFKFQGQSYD
QCTTEGRTDG YRWCGTTEDY DRDKKYGFCP ETAMSTVGGN SEGAPCVFPF IFLGNKYDSC
TSAGRNDGKL WCASTSSYDD DRKWGFCPDQ GYSLFLVAAH EFGHAMGLEH SEDPGALMAP
IYTYTKNFRL SQDDIKGIQE LYEVSPDVEP GPGPGPGPGP RPTLGPVTPE LCKHDIVFDG
VAQIRGEIFF FKDRFMWRTV NPRGKPTGPL LVATFWPDLP EKIDAVYESP QDEKAVFFAG
NEYWVYTASN LDRGYPKKLT SLGLPPDVQR IDAAFNWGRN KKTYIFSGDR YWKYNEEKKK
MELATPKFIA DSWNGVPDNL DAVLGLTDSG YTYFFKDQYY LQMEDKSLKI VKIGKISSDW
LGC
