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Matrilysin (EC 3.4.24.23) (Matrin) (Matrix metalloproteinase-7) (MMP-7) (Pump-1 protease) (Uterine metalloproteinase)

 MMP7_HUMAN              Reviewed;         267 AA.
P09237; Q9BTK9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
12-SEP-2018, entry version 193.
RecName: Full=Matrilysin;
EC=3.4.24.23;
AltName: Full=Matrin;
AltName: Full=Matrix metalloproteinase-7;
Short=MMP-7;
AltName: Full=Pump-1 protease;
AltName: Full=Uterine metalloproteinase;
Flags: Precursor;
Name=MMP7; Synonyms=MPSL1, PUMP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2844164; DOI=10.1042/bj2530187;
Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J.,
Breathnach R.;
"The collagenase gene family in humans consists of at least four
members.";
Biochem. J. 253:187-192(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1497627; DOI=10.1042/bj2850899;
Marti H.P., McNeil L., Thomas G., Davies M., Lovett D.H.;
"Molecular characterization of a low-molecular-mass matrix
metalloproteinase secreted by glomerular mesangial cells as PUMP-1.";
Biochem. J. 285:899-905(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8294454;
Gaire M., Magbanua Z., McDonnell S., McNeil L.B., Lovett D.H.,
Matrisian L.M.;
"Structure and expression of the human gene for the matrix
metalloproteinase matrilysin.";
J. Biol. Chem. 269:2032-2040(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-77; ASP-137 AND
LEU-241.
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 18-42.
PubMed=2253219;
Miyazaki K., Hattori Y., Umenishi F., Yasumitsu H., Umeda M.;
"Purification and characterization of extracellular matrix-degrading
metalloproteinase, matrin (pump-1), secreted from human rectal
carcinoma cell line.";
Cancer Res. 50:7758-7764(1990).
[7]
FUNCTION.
PubMed=2550050; DOI=10.1021/bi00439a004;
Quantin B., Murphy G., Breathnach R.;
"Pump-1 cDNA codes for a protein with characteristics similar to those
of classical collagenase family members.";
Biochemistry 28:5327-5334(1989).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=7756291; DOI=10.1021/bi00020a004;
Browner M.F., Smith W.W., Castelhano A.L.;
"Matrilysin-inhibitor complexes: common themes among
metalloproteases.";
Biochemistry 34:6602-6610(1995).
-!- FUNCTION: Degrades casein, gelatins of types I, III, IV, and V,
and fibronectin. Activates procollagenase.
{ECO:0000269|PubMed:2550050}.
-!- CATALYTIC ACTIVITY: Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-
17 in B chain of insulin. No action on collagen types I, II, IV,
V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- INTERACTION:
P17931:LGALS3; NbExp=5; IntAct=EBI-6595344, EBI-1170392;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- DOMAIN: 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.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp7/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X07819; CAA30678.1; -; mRNA.
EMBL; Z11887; CAA77942.1; -; mRNA.
EMBL; L22524; AAC37543.1; -; Genomic_DNA.
EMBL; L22519; AAC37543.1; JOINED; Genomic_DNA.
EMBL; L22520; AAC37543.1; JOINED; Genomic_DNA.
EMBL; L22521; AAC37543.1; JOINED; Genomic_DNA.
EMBL; L22522; AAC37543.1; JOINED; Genomic_DNA.
EMBL; L22523; AAC37543.1; JOINED; Genomic_DNA.
EMBL; AY795972; AAV40839.1; -; Genomic_DNA.
EMBL; BC003635; AAH03635.1; -; mRNA.
CCDS; CCDS8317.1; -.
PIR; B28816; KCHUM.
RefSeq; NP_002414.1; NM_002423.4.
UniGene; Hs.2256; -.
PDB; 1MMP; X-ray; 2.30 A; A/B=95-264.
PDB; 1MMQ; X-ray; 1.90 A; A=95-264.
PDB; 1MMR; X-ray; 2.40 A; A=95-264.
PDB; 2DDY; NMR; -; A=95-267.
PDB; 2MZE; NMR; -; A=18-267.
PDB; 2MZH; NMR; -; A=20-267.
PDB; 2MZI; NMR; -; A=18-267.
PDB; 2Y6C; X-ray; 1.70 A; A=95-258.
PDB; 2Y6D; X-ray; 1.60 A; A=95-267.
PDB; 5UE2; NMR; -; A=21-267.
PDB; 5UE5; NMR; -; A=21-267.
PDBsum; 1MMP; -.
PDBsum; 1MMQ; -.
PDBsum; 1MMR; -.
PDBsum; 2DDY; -.
PDBsum; 2MZE; -.
PDBsum; 2MZH; -.
PDBsum; 2MZI; -.
PDBsum; 2Y6C; -.
PDBsum; 2Y6D; -.
PDBsum; 5UE2; -.
PDBsum; 5UE5; -.
ProteinModelPortal; P09237; -.
SMR; P09237; -.
BioGrid; 110459; 24.
IntAct; P09237; 3.
MINT; P09237; -.
STRING; 9606.ENSP00000260227; -.
BindingDB; P09237; -.
ChEMBL; CHEMBL4073; -.
DrugBank; DB00786; Marimastat.
GuidetoPHARMACOLOGY; 1631; -.
MEROPS; M10.008; -.
iPTMnet; P09237; -.
PhosphoSitePlus; P09237; -.
BioMuta; MMP7; -.
DMDM; 116861; -.
PaxDb; P09237; -.
PeptideAtlas; P09237; -.
PRIDE; P09237; -.
ProteomicsDB; 52210; -.
DNASU; 4316; -.
Ensembl; ENST00000260227; ENSP00000260227; ENSG00000137673.
GeneID; 4316; -.
KEGG; hsa:4316; -.
UCSC; uc001phb.4; human.
CTD; 4316; -.
DisGeNET; 4316; -.
EuPathDB; HostDB:ENSG00000137673.8; -.
GeneCards; MMP7; -.
HGNC; HGNC:7174; MMP7.
HPA; CAB025869; -.
HPA; HPA051358; -.
MIM; 178990; gene.
neXtProt; NX_P09237; -.
OpenTargets; ENSG00000137673; -.
PharmGKB; PA30887; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000239471; -.
HOVERGEN; HBG052484; -.
InParanoid; P09237; -.
KO; K01397; -.
OMA; YPTYGNG; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P09237; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.23; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
SABIO-RK; P09237; -.
SIGNOR; P09237; -.
ChiTaRS; MMP7; human.
EvolutionaryTrace; P09237; -.
GeneWiki; MMP7; -.
GenomeRNAi; 4316; -.
PMAP-CutDB; P09237; -.
PRO; PR:P09237; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137673; Expressed in 113 organ(s), highest expression level in islet of Langerhans.
CleanEx; HS_MMP7; -.
Genevisible; P09237; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008237; F:metallopeptidase activity; IDA:CAFA.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR028707; Matrilysin.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF143; PTHR10201:SF143; 1.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Calcium; Collagen degradation; Complete proteome;
Direct protein sequencing; Extracellular matrix; Hydrolase;
Metal-binding; Metalloprotease; Polymorphism; Protease;
Reference proteome; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000269|PubMed:2253219}.
PROPEP 18 94 Activation peptide.
/FTId=PRO_0000028738.
CHAIN 95 267 Matrilysin.
/FTId=PRO_0000028739.
MOTIF 85 92 Cysteine switch. {ECO:0000250}.
ACT_SITE 215 215
METAL 87 87 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 153 153 Calcium 1.
METAL 163 163 Zinc 1.
METAL 165 165 Zinc 1.
METAL 170 170 Calcium 2.
METAL 171 171 Calcium 2; via carbonyl oxygen.
METAL 173 173 Calcium 2; via carbonyl oxygen.
METAL 175 175 Calcium 2; via carbonyl oxygen.
METAL 178 178 Zinc 1.
METAL 185 185 Calcium 1; via carbonyl oxygen.
METAL 187 187 Calcium 1; via carbonyl oxygen.
METAL 189 189 Calcium 1.
METAL 191 191 Zinc 1.
METAL 193 193 Calcium 2.
METAL 196 196 Calcium 2.
METAL 214 214 Zinc 2; catalytic.
METAL 218 218 Zinc 2; catalytic.
METAL 224 224 Zinc 2; catalytic.
VARIANT 77 77 R -> H (in dbSNP:rs10502001).
{ECO:0000269|Ref.4}.
/FTId=VAR_006729.
VARIANT 137 137 G -> D (in dbSNP:rs17884789).
{ECO:0000269|Ref.4}.
/FTId=VAR_021027.
VARIANT 241 241 P -> L (in dbSNP:rs17886506).
{ECO:0000269|Ref.4}.
/FTId=VAR_021028.
HELIX 24 26 {ECO:0000244|PDB:2MZE}.
HELIX 29 41 {ECO:0000244|PDB:2MZE}.
TURN 47 49 {ECO:0000244|PDB:2MZH}.
HELIX 53 66 {ECO:0000244|PDB:2MZE}.
STRAND 74 76 {ECO:0000244|PDB:5UE5}.
HELIX 77 83 {ECO:0000244|PDB:2MZE}.
STRAND 94 97 {ECO:0000244|PDB:5UE2}.
STRAND 99 103 {ECO:0000244|PDB:2MZE}.
STRAND 106 113 {ECO:0000244|PDB:2Y6D}.
STRAND 118 120 {ECO:0000244|PDB:1MMP}.
HELIX 122 137 {ECO:0000244|PDB:2Y6D}.
STRAND 143 146 {ECO:0000244|PDB:2Y6D}.
STRAND 148 150 {ECO:0000244|PDB:1MMQ}.
STRAND 153 159 {ECO:0000244|PDB:2Y6D}.
HELIX 161 163 {ECO:0000244|PDB:5UE2}.
STRAND 164 166 {ECO:0000244|PDB:2Y6D}.
STRAND 171 174 {ECO:0000244|PDB:2Y6D}.
STRAND 177 179 {ECO:0000244|PDB:2Y6D}.
STRAND 182 184 {ECO:0000244|PDB:2Y6D}.
TURN 185 188 {ECO:0000244|PDB:2Y6D}.
STRAND 190 193 {ECO:0000244|PDB:2Y6D}.
STRAND 198 207 {ECO:0000244|PDB:2Y6D}.
HELIX 208 219 {ECO:0000244|PDB:2Y6D}.
STRAND 233 236 {ECO:0000244|PDB:1MMQ}.
STRAND 241 243 {ECO:0000244|PDB:2DDY}.
HELIX 248 257 {ECO:0000244|PDB:2Y6D}.
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


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