MMP7_HUMAN
ID MMP7_HUMAN Reviewed; 267 AA.
AC P09237; Q9BTK9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 214.
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=MPSL1, PUMP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2844164; DOI=10.1042/bj2530187;
RA Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J.,
RA Breathnach R.;
RT "The collagenase gene family in humans consists of at least four members.";
RL Biochem. J. 253:187-192(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1497627; DOI=10.1042/bj2850899;
RA Marti H.P., McNeil L., Thomas G., Davies M., Lovett D.H.;
RT "Molecular characterization of a low-molecular-mass matrix
RT metalloproteinase secreted by glomerular mesangial cells as PUMP-1.";
RL Biochem. J. 285:899-905(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8294454; DOI=10.1016/s0021-9258(17)42131-4;
RA Gaire M., Magbanua Z., McDonnell S., McNeil L.B., Lovett D.H.,
RA Matrisian L.M.;
RT "Structure and expression of the human gene for the matrix
RT metalloproteinase matrilysin.";
RL J. Biol. Chem. 269:2032-2040(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-77; ASP-137 AND
RP LEU-241.
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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).
RN [6]
RP PROTEIN SEQUENCE OF 18-42.
RX PubMed=2253219;
RA Miyazaki K., Hattori Y., Umenishi F., Yasumitsu H., Umeda M.;
RT "Purification and characterization of extracellular matrix-degrading
RT metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma
RT cell line.";
RL Cancer Res. 50:7758-7764(1990).
RN [7]
RP FUNCTION.
RX PubMed=2550050; DOI=10.1021/bi00439a004;
RA Quantin B., Murphy G., Breathnach R.;
RT "Pump-1 cDNA codes for a protein with characteristics similar to those of
RT classical collagenase family members.";
RL Biochemistry 28:5327-5334(1989).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=7756291; DOI=10.1021/bi00020a004;
RA Browner M.F., Smith W.W., Castelhano A.L.;
RT "Matrilysin-inhibitor complexes: common themes among metalloproteases.";
RL Biochemistry 34:6602-6610(1995).
CC -!- FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and
CC fibronectin. Activates procollagenase. {ECO:0000269|PubMed:2550050}.
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;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- INTERACTION:
CC P09237; P17931: LGALS3; NbExp=5; IntAct=EBI-6595344, EBI-1170392;
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}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mmp7/";
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DR EMBL; X07819; CAA30678.1; -; mRNA.
DR EMBL; Z11887; CAA77942.1; -; mRNA.
DR EMBL; L22524; AAC37543.1; -; Genomic_DNA.
DR EMBL; L22519; AAC37543.1; JOINED; Genomic_DNA.
DR EMBL; L22520; AAC37543.1; JOINED; Genomic_DNA.
DR EMBL; L22521; AAC37543.1; JOINED; Genomic_DNA.
DR EMBL; L22522; AAC37543.1; JOINED; Genomic_DNA.
DR EMBL; L22523; AAC37543.1; JOINED; Genomic_DNA.
DR EMBL; AY795972; AAV40839.1; -; Genomic_DNA.
DR EMBL; BC003635; AAH03635.1; -; mRNA.
DR CCDS; CCDS8317.1; -.
DR PIR; B28816; KCHUM.
DR RefSeq; NP_002414.1; NM_002423.4.
DR PDB; 1MMP; X-ray; 2.30 A; A/B=95-264.
DR PDB; 1MMQ; X-ray; 1.90 A; A=95-264.
DR PDB; 1MMR; X-ray; 2.40 A; A=95-264.
DR PDB; 2DDY; NMR; -; A=95-267.
DR PDB; 2MZE; NMR; -; A=18-267.
DR PDB; 2MZH; NMR; -; A=20-267.
DR PDB; 2MZI; NMR; -; A=18-267.
DR PDB; 2Y6C; X-ray; 1.70 A; A=95-258.
DR PDB; 2Y6D; X-ray; 1.60 A; A=95-267.
DR PDB; 5UE2; NMR; -; A=21-267.
DR PDB; 5UE5; NMR; -; A=21-267.
DR PDBsum; 1MMP; -.
DR PDBsum; 1MMQ; -.
DR PDBsum; 1MMR; -.
DR PDBsum; 2DDY; -.
DR PDBsum; 2MZE; -.
DR PDBsum; 2MZH; -.
DR PDBsum; 2MZI; -.
DR PDBsum; 2Y6C; -.
DR PDBsum; 2Y6D; -.
DR PDBsum; 5UE2; -.
DR PDBsum; 5UE5; -.
DR AlphaFoldDB; P09237; -.
DR BMRB; P09237; -.
DR SMR; P09237; -.
DR BioGRID; 110459; 23.
DR IntAct; P09237; 18.
DR MINT; P09237; -.
DR STRING; 9606.ENSP00000260227; -.
DR BindingDB; P09237; -.
DR ChEMBL; CHEMBL4073; -.
DR DrugBank; DB08170; (1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDE.
DR DrugBank; DB08493; 5-METHYL-3-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YLCARBAMOYL)-HEXANOIC ACID.
DR DrugBank; DB00786; Marimastat.
DR DrugBank; DB08489; N4-HYDROXY-2-ISOBUTYL-N1-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YL)-SUCCINAMIDE.
DR DrugCentral; P09237; -.
DR GuidetoPHARMACOLOGY; 1631; -.
DR MEROPS; M10.008; -.
DR iPTMnet; P09237; -.
DR PhosphoSitePlus; P09237; -.
DR BioMuta; MMP7; -.
DR DMDM; 116861; -.
DR jPOST; P09237; -.
DR MassIVE; P09237; -.
DR PaxDb; P09237; -.
DR PeptideAtlas; P09237; -.
DR PRIDE; P09237; -.
DR ProteomicsDB; 52210; -.
DR ABCD; P09237; 1 sequenced antibody.
DR Antibodypedia; 18007; 870 antibodies from 42 providers.
DR DNASU; 4316; -.
DR Ensembl; ENST00000260227.5; ENSP00000260227.4; ENSG00000137673.9.
DR GeneID; 4316; -.
DR KEGG; hsa:4316; -.
DR MANE-Select; ENST00000260227.5; ENSP00000260227.4; NM_002423.5; NP_002414.1.
DR UCSC; uc001phb.4; human.
DR CTD; 4316; -.
DR DisGeNET; 4316; -.
DR GeneCards; MMP7; -.
DR HGNC; HGNC:7174; MMP7.
DR HPA; ENSG00000137673; Tissue enhanced (gallbladder, salivary gland, urinary bladder).
DR MIM; 178990; gene.
DR neXtProt; NX_P09237; -.
DR OpenTargets; ENSG00000137673; -.
DR PharmGKB; PA30887; -.
DR VEuPathDB; HostDB:ENSG00000137673; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000160903; -.
DR HOGENOM; CLU_015489_4_1_1; -.
DR InParanoid; P09237; -.
DR OMA; GINFLYV; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P09237; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.23; 2681.
DR PathwayCommons; P09237; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR SABIO-RK; P09237; -.
DR SignaLink; P09237; -.
DR SIGNOR; P09237; -.
DR BioGRID-ORCS; 4316; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; MMP7; human.
DR EvolutionaryTrace; P09237; -.
DR GeneWiki; MMP7; -.
DR GenomeRNAi; 4316; -.
DR Pharos; P09237; Tchem.
DR PRO; PR:P09237; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P09237; protein.
DR Bgee; ENSG00000137673; Expressed in gall bladder and 107 other tissues.
DR Genevisible; P09237; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:CAFA.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:ARUK-UCL.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IMP:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:CAFA.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Collagen degradation; Direct protein sequencing;
KW Extracellular matrix; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2253219"
FT PROPEP 18..94
FT /note="Activation peptide"
FT /id="PRO_0000028738"
FT CHAIN 95..267
FT /note="Matrilysin"
FT /id="PRO_0000028739"
FT MOTIF 85..92
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 215
FT BINDING 87
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 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT VARIANT 77
FT /note="R -> H (in dbSNP:rs10502001)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_006729"
FT VARIANT 137
FT /note="G -> D (in dbSNP:rs17884789)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021027"
FT VARIANT 241
FT /note="P -> L (in dbSNP:rs17886506)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021028"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2MZE"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:2MZE"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2MZH"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2MZE"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5UE5"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:2MZE"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5UE2"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2MZE"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1MMP"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1MMQ"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2Y6D"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5UE2"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2Y6D"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:2Y6D"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:2Y6D"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1MMQ"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2DDY"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:2Y6D"
SQ SEQUENCE 267 AA; 29677 MW; F6BD1FC0ADA23603 CRC64;
MRLTVLCAVC LLPGSLALPL PQEAGGMSEL QWEQAQDYLK RFYLYDSETK NANSLEAKLK
EMQKFFGLPI TGMLNSRVIE IMQKPRCGVP DVAEYSLFPN SPKWTSKVVT YRIVSYTRDL
PHITVDRLVS KALNMWGKEI PLHFRKVVWG TADIMIGFAR GAHGDSYPFD GPGNTLAHAF
APGTGLGGDA HFDEDERWTD GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD
PQNFKLSQDD IKGIQKLYGK RSNSRKK
