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Neutrophil collagenase (EC 3.4.24.34) (Matrix metalloproteinase-8) (MMP-8)

 MMP8_RAT                Reviewed;         466 AA.
O88766;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
05-DEC-2018, entry version 143.
RecName: Full=Neutrophil collagenase;
EC=3.4.24.34;
AltName: Full=Matrix metalloproteinase-8;
Short=MMP-8;
Flags: Precursor;
Name=Mmp8;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Lewis;
Overall C.M., Lowne D., Wells G., Burel S., Clements J.M.;
"Cloning, expression, characterization and activation properties of
rat neutrophil collagenase (MMP-8).";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Can degrade fibrillar type I, II, and III collagens.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of interstitial collagens in the triple helical
domain. Unlike EC 3.4.24.7, this enzyme cleaves type III
collagen more slowly than type I.; EC=3.4.24.34;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Cannot be activated without removal of the
activation peptide. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular
space, extracellular matrix {ECO:0000250}. Note=Stored in
intracellular granules.
-!- 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}.
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EMBL; AJ007288; CAA07432.1; -; mRNA.
RefSeq; NP_071557.1; NM_022221.1.
UniGene; Rn.44474; -.
ProteinModelPortal; O88766; -.
SMR; O88766; -.
STRING; 10116.ENSRNOP00000013936; -.
BindingDB; O88766; -.
ChEMBL; CHEMBL2312; -.
MEROPS; M10.002; -.
PaxDb; O88766; -.
PRIDE; O88766; -.
GeneID; 63849; -.
KEGG; rno:63849; -.
UCSC; RGD:631408; rat.
CTD; 4317; -.
RGD; 631408; Mmp8.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; O88766; -.
KO; K01402; -.
PhylomeDB; O88766; -.
PRO; PR:O88766; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IMP:RGD.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; IDA:RGD.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IMP:RGD.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0001503; P:ossification; IEP:RGD.
GO; GO:0150078; P:positive regulation of neuroinflammatory response; IMP:ARUK-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:ARUK-UCL.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:ARUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:RGD.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028709; MMP8.
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:SF137; PTHR10201:SF137; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Collagen degradation; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Repeat; Secreted;
Signal; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000250}.
PROPEP 21 101 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028748.
CHAIN 102 466 Neutrophil collagenase.
/FTId=PRO_0000028749.
REPEAT 277 326 Hemopexin 1.
REPEAT 327 373 Hemopexin 2.
REPEAT 375 421 Hemopexin 3.
REPEAT 422 465 Hemopexin 4.
MOTIF 90 97 Cysteine switch. {ECO:0000250}.
ACT_SITE 219 219 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 92 92 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 158 158 Calcium 1. {ECO:0000250}.
METAL 168 168 Zinc 1. {ECO:0000250}.
METAL 170 170 Zinc 1. {ECO:0000250}.
METAL 175 175 Calcium 2. {ECO:0000250}.
METAL 176 176 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 178 178 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 180 180 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 183 183 Zinc 1. {ECO:0000250}.
METAL 190 190 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 192 192 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 194 194 Calcium 1. {ECO:0000250}.
METAL 196 196 Zinc 1. {ECO:0000250}.
METAL 198 198 Calcium 2. {ECO:0000250}.
METAL 201 201 Calcium 2. {ECO:0000250}.
METAL 218 218 Zinc 2; catalytic. {ECO:0000250}.
METAL 222 222 Zinc 2; catalytic. {ECO:0000250}.
METAL 228 228 Zinc 2; catalytic. {ECO:0000250}.
METAL 287 287 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 379 379 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 426 426 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 280 465 {ECO:0000305}.
SEQUENCE 466 AA; 53277 MW; 8B9DE97576E76C90 CRC64;
MLHLKTLPFL FFFHTQLATA LPVPPEHLEE KNMKTAENYL RKFYHLPSNQ FRSARNATMI
AEKLKEMQRF FGLPETGKPD AATIEIMEKP RCGVPDSGDF LLTPGSPKWT HTNLTYRIIN
HTPQMSKAEV KTEIEKAFKI WSVPSTLTFT ETLEGEADIN IAFVSRDHGD NSPFDGPNGI
LAHAFQPGRG IGGDAHFDSE ETWTQDSKNY NLFLVAAHEF GHSLGLSHST DPGALMYPNY
AYREPSTYSL PQDDINGIQT IYGPSDNPVQ PTGPSTPTAC DPHLRFDAAT TLRGEIYFFK
DKYFWRRHPQ LRTVDLNFIS LFWPFLPNGL QAAYEDFDRD LVFLFKGRQY WALSAYDLQQ
GYPRDISNYG FPRSVQAIDA AVSYNGKTYF FVNNQCWRYD NQRRSMDPGY PTSIASVFPG
INCRIDAVFQ QDSFFLFFSG PQYFAFNLVS RRVTRVARSN LWLNCP


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