MMP7_RAT
ID MMP7_RAT Reviewed; 267 AA.
AC P50280;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Matrilysin;
DE EC=3.4.24.23;
DE AltName: Full=Matrin;
DE AltName: Full=Matrix metalloproteinase-7;
DE Short=MMP-7;
DE AltName: Full=Pump-1 protease;
DE AltName: Full=Uterine metalloproteinase;
DE Flags: Precursor;
GN Name=Mmp7; Synonyms=Mmp-7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=7608162; DOI=10.1074/jbc.270.27.16016;
RA Abramson S.R., Conner G.E., Nagase H., Neuhaus I., Woessner J.F.;
RT "Characterization of rat uterine matrilysin and its cDNA. Relationship to
RT human pump-1 and activation of procollagenases.";
RL J. Biol. Chem. 270:16016-16022(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and
CC fibronectin. Activates procollagenase (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of
CC insulin. No action on collagen types I, II, IV, V. Cleaves gelatin
CC chain alpha2(I) > alpha1(I).; EC=3.4.24.23;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; L24374; AAA99432.1; -; mRNA.
DR EMBL; BC064657; AAH64657.1; -; mRNA.
DR PIR; A57490; A57490.
DR RefSeq; NP_036996.1; NM_012864.2.
DR AlphaFoldDB; P50280; -.
DR SMR; P50280; -.
DR STRING; 10116.ENSRNOP00000014041; -.
DR MEROPS; M10.008; -.
DR PhosphoSitePlus; P50280; -.
DR PaxDb; P50280; -.
DR PRIDE; P50280; -.
DR Ensembl; ENSRNOT00000014041; ENSRNOP00000014041; ENSRNOG00000010507.
DR GeneID; 25335; -.
DR KEGG; rno:25335; -.
DR UCSC; RGD:3100; rat.
DR CTD; 4316; -.
DR RGD; 3100; Mmp7.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000160903; -.
DR HOGENOM; CLU_015489_4_1_1; -.
DR InParanoid; P50280; -.
DR OMA; GINFLYV; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P50280; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.23; 5301.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P50280; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010507; Expressed in ovary and 8 other tissues.
DR Genevisible; P50280; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0002780; P:antibacterial peptide biosynthetic process; ISO:RGD.
DR GO; GO:0002779; P:antibacterial peptide secretion; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:RGD.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR028707; Matrilysin.
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:SF143; PTHR10201:SF143; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen degradation; Extracellular matrix; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..97
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028742"
FT CHAIN 98..267
FT /note="Matrilysin"
FT /id="PRO_0000028743"
FT MOTIF 88..95
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 267 AA; 29885 MW; EBA3C3D9527A4C7B CRC64;
MAAMRLTLFR IVCLLPGCLA LPLSQEAGEV TALQWEQAQN YLRKFYLHDS KTKKATSAVD
KLREMQKFFG LPETGKLSPR VMEIMQKPRC GVPDVAEFSL MPNSPKWHSR TVTYRIVSYT
TDLPRFLVDQ IVKRALRMWS MQIPLNFKRV SWGTADIIIG FARGDHGDNF PFDGPGNTLG
HAFAPGPGLG GDAHFDKDEY WTDGEDSGVN FLFVATHELG HSLGLGHSSV PSSVMYPTYQ
GDHSEDFSLT KDDIAGIQKL YGKRNKL
