MMP9_MOUSE
ID MMP9_MOUSE Reviewed; 730 AA.
AC P41245; Q06788; Q80XI8; Q9DC02;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Matrix metalloproteinase-9;
DE Short=MMP-9;
DE EC=3.4.24.35 {ECO:0000250|UniProtKB:P14780};
DE AltName: Full=92 kDa gelatinase;
DE AltName: Full=92 kDa type IV collagenase;
DE AltName: Full=Gelatinase B;
DE Short=GELB;
DE Flags: Precursor;
GN Name=Mmp9; Synonyms=Clg4b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8382489; DOI=10.1006/bbrc.1993.1110;
RA Tanaka H., Hojo K., Yoshida H., Yoshioka T., Sugita K.;
RT "Molecular cloning and expression of the mouse 105-kDa gelatinase cDNA.";
RL Biochem. Biophys. Res. Commun. 190:732-740(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-514; PRO-639 AND PRO-711.
RX PubMed=8219207;
RA Graubert T., Johnston J., Berliner N.;
RT "Cloning and expression of the cDNA encoding mouse neutrophil gelatinase:
RT demonstration of coordinate secondary granule protein gene expression
RT during terminal neutrophil maturation.";
RL Blood 82:3192-3197(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=8243459; DOI=10.1111/j.1432-1033.1993.tb18359.x;
RA Masure S., Nys G., Fiten P., van Damme J., Opdenakker G.;
RT "Mouse gelatinase B. cDNA cloning, regulation of expression and
RT glycosylation in WEHI-3 macrophages and gene organisation.";
RL Eur. J. Biochem. 218:129-141(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Bone;
RX PubMed=8132709; DOI=10.1083/jcb.124.6.1091;
RA Reponen P., Sahlberg C., Munaut C., Thesleff I., Tryggvason K.;
RT "High expression of 92-kD type IV collagenase (gelatinase B) in the
RT osteoclast lineage during mouse development.";
RL J. Cell Biol. 124:1091-1102(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [8]
RP INDUCTION BY MYCOBACTERIA.
RC STRAIN=BALB/cJ; TISSUE=Liver, Lung, Macrophage, and Spleen;
RX PubMed=11500442; DOI=10.1128/iai.69.9.5661-5670.2001;
RA Quiding-Jaerbrink M., Smith D.A., Bancroft G.J.;
RT "Production of matrix metalloproteinases in response to mycobacterial
RT infection.";
RL Infect. Immun. 69:5661-5670(2001).
RN [9]
RP INDUCTION.
RX PubMed=19893577; DOI=10.1038/embor.2009.233;
RA Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
RA Ohwada S., Akiyama T.;
RT "The adenomatous polyposis coli-associated exchange factors Asef and Asef2
RT are required for adenoma formation in Apc(Min/+)mice.";
RL EMBO Rep. 10:1355-1362(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=23142597; DOI=10.1016/j.bbrc.2012.10.099;
RA Ahn B.J., Le H., Shin M.W., Bae S.J., Lee E.J., Wee H.J., Cha J.H.,
RA Park J.H., Lee H.S., Lee H.J., Jung H., Park Z.Y., Park S.H., Han B.W.,
RA Seo J.H., Lo E.H., Kim K.W.;
RT "The N-terminal ectodomain of Ninjurin1 liberated by MMP9 has chemotactic
RT activity.";
RL Biochem. Biophys. Res. Commun. 428:438-444(2012).
RN [12]
RP FUNCTION.
RX PubMed=32883094; DOI=10.1161/circulationaha.120.046907;
RA Jeon S., Kim T.K., Jeong S.J., Jung I.H., Kim N., Lee M.N., Sonn S.K.,
RA Seo S., Jin J., Kweon H.Y., Kim S., Shim D., Park Y.M., Lee S.H., Kim K.W.,
RA Cybulsky M.I., Shim H., Roh T.Y., Park W.Y., Lee H.O., Choi J.H.,
RA Park S.H., Oh G.T.;
RT "Anti-inflammatory actions of soluble ninjurin-1 ameliorate
RT atherosclerosis.";
RL Circulation 142:1736-1751(2020).
CC -!- FUNCTION: Matrix metalloproteinase that plays an essential role in
CC local proteolysis of the extracellular matrix and in leukocyte
CC migration (By similarity). Could play a role in bone osteoclastic
CC resorption (PubMed:8132709). Cleaves KiSS1 at a Gly-|-Leu bond (By
CC similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form
CC (PubMed:23142597, PubMed:32883094). Cleaves type IV and type V collagen
CC into large C-terminal three quarter fragments and shorter N-terminal
CC one quarter fragments. Degrades fibronectin but not laminin or Pz-
CC peptide (By similarity). {ECO:0000250|UniProtKB:P14780,
CC ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094,
CC ECO:0000269|PubMed:8132709}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of gelatin types I and V and collagen types IV and
CC V.; EC=3.4.24.35; Evidence={ECO:0000250|UniProtKB:P14780};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P14780};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14780};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
CC -!- ACTIVITY REGULATION: Inhibited by histatin-3 1/24 (histatin-5).
CC Inhibited by ECM1. {ECO:0000250|UniProtKB:P14780}.
CC -!- SUBUNIT: Exists as monomer or homodimer; disulfide-linked. Exists also
CC as heterodimer with LCN2. Macrophages and transformed cell lines
CC produce only the monomeric form. Interacts with ECM1.
CC {ECO:0000250|UniProtKB:P14780}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P14780}.
CC -!- INDUCTION: Up-regulated by ARHGEF4, SPATA13 and APC via the JNK
CC signaling pathway in colorectal tumor cells.
CC {ECO:0000269|PubMed:19893577}.
CC -!- INDUCTION: (Microbial infection) Induced in macrophages as well as in
CC whole animals (spleen, lung and liver) by incubation or infection with
CC M.bovis BCG and M.tuberculosis H37Rv (at protein level)
CC (PubMed:11500442). {ECO:0000269|PubMed:11500442}.
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. {ECO:0000250|UniProtKB:P14780}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P14780}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; D12712; BAA02208.1; -; mRNA.
DR EMBL; S67830; AAB28942.1; -; mRNA.
DR EMBL; X72794; CAA51314.1; -; Genomic_DNA.
DR EMBL; X72795; CAA51315.1; -; mRNA.
DR EMBL; Z27231; CAA81745.1; -; mRNA.
DR EMBL; AK004651; BAB23442.1; -; mRNA.
DR EMBL; AK159292; BAE34968.1; -; mRNA.
DR EMBL; AL591495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046991; AAH46991.1; -; mRNA.
DR CCDS; CCDS17066.1; -.
DR PIR; I52580; I52580.
DR PIR; JC1456; JC1456.
DR RefSeq; NP_038627.1; NM_013599.4.
DR AlphaFoldDB; P41245; -.
DR SMR; P41245; -.
DR BioGRID; 201454; 2.
DR STRING; 10090.ENSMUSP00000017881; -.
DR BindingDB; P41245; -.
DR ChEMBL; CHEMBL2214; -.
DR MEROPS; M10.004; -.
DR CarbonylDB; P41245; -.
DR GlyGen; P41245; 3 sites.
DR PhosphoSitePlus; P41245; -.
DR CPTAC; non-CPTAC-4047; -.
DR MaxQB; P41245; -.
DR PaxDb; P41245; -.
DR PeptideAtlas; P41245; -.
DR PRIDE; P41245; -.
DR ProteomicsDB; 290265; -.
DR ABCD; P41245; 2 sequenced antibodies.
DR Antibodypedia; 774; 2071 antibodies from 53 providers.
DR DNASU; 17395; -.
DR Ensembl; ENSMUST00000017881; ENSMUSP00000017881; ENSMUSG00000017737.
DR GeneID; 17395; -.
DR KEGG; mmu:17395; -.
DR UCSC; uc008nwt.2; mouse.
DR CTD; 4318; -.
DR MGI; MGI:97011; Mmp9.
DR VEuPathDB; HostDB:ENSMUSG00000017737; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000157415; -.
DR HOGENOM; CLU_015489_6_2_1; -.
DR InParanoid; P41245; -.
DR OMA; DVFQYRE; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P41245; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.35; 3474.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 17395; 2 hits in 75 CRISPR screens.
DR PRO; PR:P41245; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P41245; protein.
DR Bgee; ENSMUSG00000017737; Expressed in granulocyte and 194 other tissues.
DR ExpressionAtlas; P41245; baseline and differential.
DR Genevisible; P41245; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
DR GO; GO:0071460; P:cellular response to cell-matrix adhesion; ISO:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0071492; P:cellular response to UV-A; ISO:MGI.
DR GO; GO:0030574; P:collagen catabolic process; IDA:MGI.
DR GO; GO:0007566; P:embryo implantation; IDA:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001258; P:negative regulation of cation channel activity; ISO:MGI.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2000697; P:negative regulation of epithelial cell differentiation involved in kidney development; IDA:ARUK-UCL.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1900122; P:positive regulation of receptor binding; ISO:MGI.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:1904645; P:response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0048771; P:tissue remodeling; ISO:MGI.
DR GO; GO:0019087; P:transformation of host cell by virus; ISO:MGI.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 2.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028688; MMP9.
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 InterPro; IPR006970; PT.
DR PANTHER; PTHR10201:SF30; PTHR10201:SF30; 1.
DR Pfam; PF00040; fn2; 3.
DR Pfam; PF00045; Hemopexin; 2.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF04886; PT; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00059; FN2; 3.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF57440; SSF57440; 3.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00023; FN2_1; 3.
DR PROSITE; PS51092; FN2_2; 3.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen degradation; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT PROPEP 20..107
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT /id="PRO_0000028758"
FT CHAIN 108..730
FT /note="Matrix metalloproteinase-9"
FT /id="PRO_0000028759"
FT DOMAIN 225..273
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 283..331
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 342..390
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 536..581
FT /note="Hemopexin 1"
FT REPEAT 582..626
FT /note="Hemopexin 2"
FT REPEAT 628..675
FT /note="Hemopexin 3"
FT REPEAT 676..729
FT /note="Hemopexin 4"
FT REGION 442..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..105
FT /note="Cysteine switch"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT COMPBIAS 454..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 100
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|UniProtKB:P14780"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 244..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 288..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 302..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 347..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 361..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 534..729
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT VARIANT 514
FT /note="P -> A"
FT /evidence="ECO:0000269|PubMed:8219207"
FT VARIANT 639
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:8219207"
FT VARIANT 711
FT /note="H -> P"
FT /evidence="ECO:0000269|PubMed:8219207"
FT CONFLICT 20
FT /note="A -> C (in Ref. 2; AAB28942)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="QP -> HA (in Ref. 2; AAB28942)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="P -> T (in Ref. 5; BAB23442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 730 AA; 80535 MW; E16F45C24D4D1024 CRC64;
MSPWQPLLLA LLAFGCSSAA PYQRQPTFVV FPKDLKTSNL TDTQLAEAYL YRYGYTRAAQ
MMGEKQSLRP ALLMLQKQLS LPQTGELDSQ TLKAIRTPRC GVPDVGRFQT FKGLKWDHHN
ITYWIQNYSE DLPRDMIDDA FARAFAVWGE VAPLTFTRVY GPEADIVIQF GVAEHGDGYP
FDGKDGLLAH AFPPGAGVQG DAHFDDDELW SLGKGVVIPT YYGNSNGAPC HFPFTFEGRS
YSACTTDGRN DGTPWCSTTA DYDKDGKFGF CPSERLYTEH GNGEGKPCVF PFIFEGRSYS
ACTTKGRSDG YRWCATTANY DQDKLYGFCP TRVDATVVGG NSAGELCVFP FVFLGKQYSS
CTSDGRRDGR LWCATTSNFD TDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY
PLYSYLEGFP LNKDDIDGIQ YLYGRGSKPD PRPPATTTTE PQPTAPPTMC PTIPPTAYPT
VGPTVGPTGA PSPGPTSSPS PGPTGAPSPG PTAPPTAGSS EASTESLSPA DNPCNVDVFD
AIAEIQGALH FFKDGWYWKF LNHRGSPLQG PFLTARTWPA LPATLDSAFE DPQTKRVFFF
SGRQMWVYTG KTVLGPRSLD KLGLGPEVTH VSGLLPRRLG KALLFSKGRV WRFDLKSQKV
DPQSVIRVDK EFSGVPWNSH DIFQYQDKAY FCHGKFFWRV SFQNEVNKVD HEVNQVDDVG
YVTYDLLQCP
