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Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB)

 MMP9_RAT                Reviewed;         708 AA.
P50282;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 158.
RecName: Full=Matrix metalloproteinase-9;
Short=MMP-9;
EC=3.4.24.35;
AltName: Full=92 kDa gelatinase;
AltName: Full=92 kDa type IV collagenase;
AltName: Full=Gelatinase B;
Short=GELB;
Flags: Precursor;
Name=Mmp9;
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=Wistar;
PubMed=7590350; DOI=10.1016/0378-1119(95)00447-E;
Okada A., Santavicca M., Basset P.;
"The cDNA cloning and expression of the gene encoding rat gelatinase
B.";
Gene 164:317-321(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer 344;
PubMed=8605986; DOI=10.1016/0014-5793(96)00185-8;
Xia Y., Garcia G., Chen S., Wilson C.B., Feng L.;
"Cloning of rat 92-kDa type IV collagenase and expression of an active
recombinant catalytic domain.";
FEBS Lett. 382:285-288(1996).
-!- FUNCTION: Could play a role in bone osteoclastic resorption.
Cleaves type IV and type V collagen into large C-terminal three
quarter fragments and shorter N-terminal one quarter fragments (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of gelatin types I and V and collagen types IV
and V.; EC=3.4.24.35;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: Exists as monomer or homodimer; disulfide-linked. Exists
also as heterodimer with LCN2. Interacts with ECM1.
{ECO:0000250|UniProtKB:P14780}.
-!- 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.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U24441; AAA90911.1; -; mRNA.
EMBL; U36476; AAB01721.1; -; mRNA.
PIR; JC4364; JC4364.
PIR; S62907; S62907.
RefSeq; NP_112317.1; NM_031055.1.
UniGene; Rn.10209; -.
ProteinModelPortal; P50282; -.
SMR; P50282; -.
STRING; 10116.ENSRNOP00000023965; -.
BindingDB; P50282; -.
ChEMBL; CHEMBL3870; -.
MEROPS; M10.004; -.
PaxDb; P50282; -.
PRIDE; P50282; -.
GeneID; 81687; -.
KEGG; rno:81687; -.
CTD; 4318; -.
RGD; 621320; Mmp9.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217926; -.
HOVERGEN; HBG052484; -.
InParanoid; P50282; -.
KO; K01403; -.
PhylomeDB; P50282; -.
BRENDA; 3.4.24.35; 5301.
PRO; PR:P50282; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0001968; F:fibronectin binding; IPI:RGD.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; IDA:RGD.
GO; GO:0008233; F:peptidase activity; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007568; P:aging; IDA:RGD.
GO; GO:0071460; P:cellular response to cell-matrix adhesion; IMP:RGD.
GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071283; P:cellular response to iron(III) ion; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0030574; P:collagen catabolic process; IDA:RGD.
GO; GO:0007507; P:heart development; IDA:RGD.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:RGD.
GO; GO:0001503; P:ossification; IEP:RGD.
GO; GO:0007567; P:parturition; IEP:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
GO; GO:0002687; P:positive regulation of leukocyte migration; IDA:RGD.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:RGD.
GO; GO:0051259; P:protein complex oligomerization; IDA:RGD.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0009644; P:response to high light intensity; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0048771; P:tissue remodeling; IDA:RGD.
GO; GO:0019087; P:transformation of host cell by virus; IDA:RGD.
CDD; cd00062; FN2; 3.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.10.10.10; -; 3.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR013806; Kringle-like.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028688; MMP9.
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.
InterPro; IPR036366; PGBDSf.
InterPro; IPR006970; PT.
PANTHER; PTHR10201:SF30; PTHR10201:SF30; 1.
Pfam; PF00040; fn2; 3.
Pfam; PF00045; Hemopexin; 1.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
Pfam; PF04886; PT; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00059; FN2; 3.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
SUPFAM; SSF57440; SSF57440; 3.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00023; FN2_1; 2.
PROSITE; PS51092; FN2_2; 3.
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 19 {ECO:0000250}.
PROPEP 20 107 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028762.
CHAIN 108 708 Matrix metalloproteinase-9.
/FTId=PRO_0000028763.
DOMAIN 226 274 Fibronectin type-II 1.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 284 332 Fibronectin type-II 2.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 343 391 Fibronectin type-II 3.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 521 566 Hemopexin 1.
REPEAT 567 611 Hemopexin 2.
REPEAT 613 660 Hemopexin 3.
REPEAT 661 707 Hemopexin 4.
MOTIF 98 105 Cysteine switch. {ECO:0000250}.
ACT_SITE 403 403 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 100 100 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 132 132 Calcium 1. {ECO:0000250}.
METAL 166 166 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 176 176 Zinc 1; structural. {ECO:0000250}.
METAL 178 178 Zinc 1; structural. {ECO:0000250}.
METAL 183 183 Calcium 3. {ECO:0000250}.
METAL 184 184 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 186 186 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 188 188 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 191 191 Zinc 1; structural. {ECO:0000250}.
METAL 198 198 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 200 200 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 202 202 Calcium 2. {ECO:0000250}.
METAL 204 204 Zinc 1; structural. {ECO:0000250}.
METAL 206 206 Calcium 3. {ECO:0000250}.
METAL 207 207 Calcium 1. {ECO:0000250}.
METAL 209 209 Calcium 1. {ECO:0000250}.
METAL 209 209 Calcium 3. {ECO:0000250}.
METAL 402 402 Zinc 2; catalytic. {ECO:0000250}.
METAL 406 406 Zinc 2; catalytic. {ECO:0000250}.
METAL 412 412 Zinc 2; catalytic. {ECO:0000250}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 231 257 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 245 272 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 289 315 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 303 330 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 348 374 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 362 389 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 519 707 {ECO:0000255|PROSITE-ProRule:PRU00479}.
CONFLICT 2 2 S -> N (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 112 112 D -> E (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 326 327 AD -> LY (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 364 364 S -> G (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 441 441 H -> Q (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 472 472 S -> P (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 515 515 D -> V (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 551 551 N -> S (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 566 566 F -> L (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 568 568 S -> A (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 579 579 P -> S (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 586 589 LWAQ -> SGRK (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 597 597 S -> T (in Ref. 1; AAA90911).
{ECO:0000305}.
CONFLICT 669 669 Q -> H (in Ref. 1; AAA90911).
{ECO:0000305}.
SEQUENCE 708 AA; 78611 MW; D57DC0D1B93A778C CRC64;
MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL YRYGYTRAAQ
MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC GVPDVGKFQT FDGDLKWHHH
NITYWIQSYT EDLPRDVIDD SFARAFAVWS AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY
PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR
SYLSCTTDGR NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF PFVFLGKQYS
TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM
YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP DPRPPATTAA EPQPTAPPTM CSTAPPMAYP
TGGPTVAPTG APSPGPTGPP TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG
RYWKFSNHGG NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV TRLDNEFSGV
PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV TYDLLQCP


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