[1]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37, AND VARIANT ARG-279. PubMed=2551898 [NCBI, ExPASy, EBI, Israel, Japan] Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G.A., Goldberg G.I.; "SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages."; J. Biol. Chem. 264:17213-17221(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1653238 [NCBI, ExPASy, EBI, Israel, Japan] Huhtala P., Tuuttila A., Chow L.T., Lohi J., Keski-Oja J., Tryggvason K.; "Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells."; J. Biol. Chem. 266:16485-16490(1991).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Umbilical cord blood; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-20; LYS-127; ARG-279; ARG-574 AND GLN-668. SeattleSNPs variation discovery resource; Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-20; HIS-239; VAL-571; ARG-574 AND GLN-668. NIEHS SNPs program; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-574. DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan] Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; "The DNA sequence and comparative analysis of human chromosome 20."; Nature 414:865-871(2001).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-279. TISSUE=B-cell; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. PubMed=8426746 [NCBI, ExPASy, EBI, Israel, Japan] Sato H., Seiki M.; "Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells."; Oncogene 8:395-405(1993).
[9]	PROTEIN SEQUENCE OF 20-39, AND GLYCOSYLATION. TISSUE=Neutrophil; PubMed=1464361 [NCBI, ExPASy, EBI, Israel, Japan] Kjeldsen L., Bjerrum O.W., Hovgaard D., Johnsen A.H., Sehested M., Borregaard N.; "Human neutrophil gelatinase: a marker for circulating blood neutrophils. Purification and quantitation by enzyme linked immunosorbent assay."; Eur. J. Haematol. 49:180-191(1992).
[10]	PROTEIN SEQUENCE OF 20-37. DOI=10.1016/1043-4666(91)90021-5; PubMed=1653055 [NCBI, ExPASy, EBI, Israel, Japan] van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F., Auwerx J., van Damme J., Opdenakker G.; "The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers."; Cytokine 3:231-239(1991).
[11]	PROTEIN SEQUENCE OF 20-34; 60-71 AND 107-118, INDUCTION, AND PROTEOLYTIC PROCESSING BY MMP3. PubMed=1371271 [NCBI, ExPASy, EBI, Israel, Japan] Ogata Y., Enghild J.J., Nagase H.; "Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9."; J. Biol. Chem. 267:3581-3584(1992).
[12]	PROTEIN SEQUENCE OF 20-32 AND 94-111, PROTEOLYTIC PROCESSING, AND INDUCTION. TISSUE=Fibrosarcoma; PubMed=1400481 [NCBI, ExPASy, EBI, Israel, Japan] Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K., Yamashita K., Hayakawa T.; "Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties."; J. Biol. Chem. 267:21712-21719(1992).
[13]	PROTEIN SEQUENCE OF 20-27; 60-67; 94-101 AND 107-113. DOI=10.1016/0167-4838(95)00086-A; PubMed=7669817 [NCBI, ExPASy, EBI, Israel, Japan] Sang Q.X., Birkedal-Hansen H., Van Wart H.E.; "Proteolytic and non-proteolytic activation of human neutrophil progelatinase B."; Biochim. Biophys. Acta 1251:99-108(1995).
[14]	PROTEIN SEQUENCE OF 28-60. TISSUE=Neutrophil; DOI=10.1111/j.1432-1033.1991.tb16027.x; PubMed=1645657 [NCBI, ExPASy, EBI, Israel, Japan] Masure S., Proost P., van Damme J., Opdenakker G.; "Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8."; Eur. J. Biochem. 198:391-398(1991).
[15]	PROTEIN SEQUENCE OF 28-37. PubMed=1932376 [NCBI, ExPASy, EBI, Israel, Japan] Opdenakker G., Masure S., Grillet B., Van Damme J.; "Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis."; Lymphokine Cytokine Res. 10:317-324(1991).
[16]	PROTEIN SEQUENCE OF 93-115, FUNCTION, AND CATALYTIC ACTIVITY. TISSUE=Blood; PubMed=1480034 [NCBI, ExPASy, EBI, Israel, Japan] Tschesche H., Knaeuper V., Kraemer S., Michaelis J., Oberhoff R., Reinke H.; "Latent collagenase and gelatinase from human neutrophils and their activation."; Matrix Suppl. 1:245-255(1992).
[17]	CHARACTERIZATION. Kang K., Lee D.-H.; "Purification and characterization of human 92-kDa type IV collagenase (gelatinase B)."; Exp. Mol. Med. 28:161-165(1996).
[18]	SUBUNIT. DOI=10.1074/jbc.275.4.2661; PubMed=10644727 [NCBI, ExPASy, EBI, Israel, Japan] Olson M.W., Bernardo M.M., Pietila M., Gervasi D.C., Toth M., Kotra L.P., Massova I., Mobashery S., Fridman R.; "Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1."; J. Biol. Chem. 275:2661-2668(2000).
[19]	ENZYME REGULATION. DOI=10.1128/IAI.69.3.1402-1408.2001; PubMed=11179305 [NCBI, ExPASy, EBI, Israel, Japan] Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G.; "Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease."; Infect. Immun. 69:1402-1408(2001).
[20]	PROTEOLYTIC PROCESSING OF KISS1. DOI=10.1038/sj.onc.1206542; PubMed=12879005 [NCBI, ExPASy, EBI, Israel, Japan] Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y., Seiki M., Sato H.; "Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases."; Oncogene 22:4617-4626(2003).
[21]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-444 IN COMPLEX WITH ZINC AND MAGNESIUM IONS. DOI=10.1107/S0907444902007849; PubMed=12077439 [NCBI, ExPASy, EBI, Israel, Japan] Elkins P.A., Ho Y.S., Smith W.W., Janson C.A., D'Alessio K.J., McQueney M.S., Cummings M.D., Romanic A.M.; "Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase."; Acta Crystallogr. D 58:1182-1192(2002).
[22]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 107-215 IN COMPLEX WITH INHIBITOR; ZINC AND CALCIUM IONS, AND MUTAGENESIS OF GLU-402. DOI=10.1016/S0022-2836(02)00262-0; PubMed=12051944 [NCBI, ExPASy, EBI, Israel, Japan] Rowsell S., Hawtin P., Minshull C.A., Jepson H., Brockbank S.M.V., Barratt D.G., Slater A.M., McPheat W.L., Waterson D., Henney A.M., Pauptit R.A.; "Crystal structure of human MMP9 in complex with a reverse hydroxamate inhibitor."; J. Mol. Biol. 319:173-181(2002).
[23]	X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 513-707, AND SUBUNIT. DOI=10.1016/S0022-2836(02)00558-2; PubMed=12126625 [NCBI, ExPASy, EBI, Israel, Japan] Cha H., Kopetzki E., Huber R., Lanzendoerfer M., Brandstetter H.; "Structural basis of the adaptive molecular recognition by MMP9."; J. Mol. Biol. 320:1065-1079(2002).
[24]	3D-STRUCTURE MODELING. Mallena S.C., Sagajkar R.D.; "Theoretical model of human type IV collagenase precursor."; Submitted (APR-2002) to the PDB data bank.
[25]	VARIANTS VAL-20; LYS-82 AND ARG-279. DOI=10.1007/s004390051124; PubMed=10598806 [NCBI, ExPASy, EBI, Israel, Japan] Zhang B., Henney A., Eriksson P., Hamsten A., Watkins H., Ye S.; "Genetic variation at the matrix metalloproteinase-9 locus on chromosome 20q12.2-13.1."; Hum. Genet. 105:418-423(1999).
[26]	INVOLVEMENT IN SUSCEPTIBILITY TO LDH. DOI=10.1016/j.ajhg.2008.03.013; PubMed=18455130 [NCBI, ExPASy, EBI, Israel, Japan] Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y., Mikami Y., Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K., Takahashi A., Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y., Ikegawa S.; "A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation."; Am. J. Hum. Genet. 82:1122-1129(2008).

Comments

FUNCTION: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
CATALYTIC ACTIVITY: Cleavage of gelatin types I and V and collagen types IV and V.
COFACTOR: Binds 2 zinc ions per subunit.
COFACTOR: Binds 3 calcium ions per subunit.
ENZYME REGULATION: Inhibited by histatin-3 1/24 (histatin-5).
SUBUNIT: Exists as monomer, disulfide-linked homodimer, and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (Probable).
TISSUE SPECIFICITY: Produced by normal alveolar macrophages and granulocytes.
INDUCTION: Activated by 4-aminophenylmercuric acetate and phorbol ester.
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: Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
PTM: N- and O-glycosylated.
DISEASE: Defects in MMP9 may be a cause of susceptibility to lumbar disk herniation (LDH) [MIM:603932]. LDH is the predominant cause of low-back pain and unilateral leg pain.
MISCELLANEOUS: In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.
SIMILARITY: Belongs to the peptidase M10A family [view classification].
SIMILARITY: Contains 3 fibronectin type-II domains.
SIMILARITY: Contains 4 hemopexin-like domains.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MMP9ID41408ch20q11.html";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp9/";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/mmp9/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J05070; AAA51539.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M68343; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68344; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68345; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68346; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68347; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68348; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68349; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68350; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68351; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68352; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68353; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68354; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M68355; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AK313137; BAG35956.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF538844; AAM97934.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ194553; ABA03169.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL162458; CAC10459.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006093; AAH06093.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10051; BAA20967.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00027509; -.

A34458; A34458.

NP_004985.2; -.

3D structure databases

PDB

1GKC; X-ray; 2.30 A; A/B=107-443.	[ExPASy / RCSB / EBI]
1GKD; X-ray; 2.10 A; A/B=107-443.	[ExPASy / RCSB / EBI]
1ITV; X-ray; 1.95 A; A/B=513-707.	[ExPASy / RCSB / EBI]
1L6J; X-ray; 2.50 A; A=20-444.	[ExPASy / RCSB / EBI]
1LKG; Model; -; A=1-707.	[ExPASy / RCSB / EBI]
2OVX; X-ray; 2.00 A; A/B=110-443.	[ExPASy / RCSB / EBI]
2OVZ; X-ray; 2.00 A; A/B=110-443.	[ExPASy / RCSB / EBI]
2OW0; X-ray; 2.00 A; A/B=110-443.	[ExPASy / RCSB / EBI]
2OW1; X-ray; 2.20 A; A/B=110-443.	[ExPASy / RCSB / EBI]
2OW2; X-ray; 2.90 A; A/B=110-443.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GKC; -.
1GKD; -.
1ITV; -.
1L6J; -.
1LKG; -.
2OVX; -.
2OVZ; -.
2OW0; -.
2OW1; -.
2OW2; -.

ModBase

P14780.

Protein family/group databases

MEROPS

M10.004; -.

PTM databases

GlycoSuiteDB

P14780; -.

Enzyme and pathway databases

BRENDA

3.4.24.35; 247.

Pathway_Interaction_DB

amb2_neutrophils_pathway; amb2 Integrin signaling.
fgf_pathway; FGF signaling pathway.
lysophospholipid_pathway; LPA receptor mediated events.
avb3_opn_pathway; Osteopontin-mediated events.
er_nongenomic_pathway; Plasma membrane estrogen receptor signaling.
syndecan_4_pathway; Syndecan-4-mediated signaling events.

Organism-specific databases

GC20P044070; -.

HIX0015874; -.

HGNC:7176; MMP9.

CAB000348; -.
HPA001238; -.

MIM

120361; gene. [NCBI / EBI]
603932; phenotype. [NCBI / EBI]

PharmGKB

PA30889; -.

Gene expression databases

Bgee

P14780; -.

CleanEx

HS_MMP9; -.

GermOnline

ENSG00000100985; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005578;	Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005518;	Molecular function: collagen binding (traceable author statement from UniProtKB).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (traceable author statement from UniProtKB).
GO:0030574;	Biological process: collagen catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0030225;	Biological process: macrophage differentiation (traceable author statement from UniProtKB).
GO:0051549;	Biological process: positive regulation of keratinocyte migration (inferred from mutant phenotype from UniProtKB).
GO:0006508;	Biological process: proteolysis (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000562; FN_type2_col_bd.
IPR000585; Hemopexin/matrixin.
IPR018486; Hemopexin/matrixin_CS.
IPR018487; Hemopexin/matrixin_repeat.
IPR001818; Pept_M10A_M12B.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
IPR006970; PT.
Graphical view of domain structure.

Gene3D

G3DSA:2.110.10.10; Hemopexin; 1.

Pfam

PF00040; fn2; 3.
PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
PF04886; PT; 1.
Pfam graphical view of domain structure.

PRINTS

PR00013; FNTYPEII.
PR00138; MATRIXIN.

ProDom

PD000995; FN_Type_II; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00059; FN2; 3.
SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.

PROSITE

PS00546; CYSTEINE_SWITCH; 1.
PS00023; FN2_1; 3.
PS51092; FN2_2; 3.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

P14780; -.

PRIDE

P14780; -.

Genome annotation databases

Ensembl

ENSG00000100985; Homo sapiens. [Contig view]

GeneID

4318; -.

KEGG

hsa:4318; -.

Phylogenomic databases

HOGENOM

P14780; -.

HOVERGEN

P14780; -.

Other

DrugBank

DB01296; Glucosamine.
DB00786; Marimastat.
DB01017; Minocycline.
DB00641; Simvastatin.

16989; -.

MMP9; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Collagen degradation; Direct protein sequencing; Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Repeat; Secreted; Signal; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`PROPEP`	`20 93`	`74`	`Activation peptide.`	`PRO_0000028754`
`CHAIN`	`94 ?`		`67 kDa matrix metalloproteinase-9.`	`PRO_0000028755`
`CHAIN`	`107 707`	`601`	`82 kDa matrix metalloproteinase-9.`	`PRO_0000028756`
`PROPEP`	`? 707`		`Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9.`	`PRO_0000028757`
`DOMAIN`	`225 273`	`49`	`Fibronectin type-II 1.`
`DOMAIN`	`283 331`	`49`	`Fibronectin type-II 2.`
`DOMAIN`	`342 390`	`49`	`Fibronectin type-II 3.`
`DOMAIN`	`521 565`	`45`	`Hemopexin-like 1.`
`DOMAIN`	`567 608`	`42`	`Hemopexin-like 2.`
`DOMAIN`	`613 659`	`47`	`Hemopexin-like 3.`
`DOMAIN`	`661 704`	`44`	`Hemopexin-like 4.`
`MOTIF`	`97 104`	`8`	`Cysteine switch (By similarity).`
`ACT_SITE`	`402 402`
`METAL`	`99 99`		`Zinc 2; in inhibited form.`
`METAL`	`131 131`		`Calcium 1.`
`METAL`	`165 165`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`175 175`		`Zinc 1; structural.`
`METAL`	`177 177`		`Zinc 1; structural.`
`METAL`	`182 182`		`Calcium 3.`
`METAL`	`183 183`		`Calcium 3; via carbonyl oxygen.`
`METAL`	`185 185`		`Calcium 3; via carbonyl oxygen.`
`METAL`	`187 187`		`Calcium 3; via carbonyl oxygen.`
`METAL`	`190 190`		`Zinc 1; structural.`
`METAL`	`197 197`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`199 199`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`201 201`		`Calcium 2.`
`METAL`	`203 203`		`Zinc 1; structural.`
`METAL`	`205 205`		`Calcium 3.`
`METAL`	`206 206`		`Calcium 1.`
`METAL`	`208 208`		`Calcium 1.`
`METAL`	`208 208`		`Calcium 3.`
`METAL`	`401 401`		`Zinc 2; catalytic.`
`METAL`	`405 405`		`Zinc 2; catalytic.`
`METAL`	`411 411`		`Zinc 2; catalytic.`
`SITE`	`59 60`	`2`	`Cleavage; by MMP3.`
`SITE`	`106 107`	`2`	`Cleavage; by MMP3.`
`CARBOHYD`	`38 38`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`120 120`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`127 127`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`230 256`		`By similarity.`
`DISULFID`	`244 271`		`By similarity.`
`DISULFID`	`288 314`		`By similarity.`
`DISULFID`	`302 329`		`By similarity.`
`DISULFID`	`347 373`		`By similarity.`
`DISULFID`	`361 388`		`By similarity.`
`DISULFID`	`516 704`
`VARIANT`	`20 20`	`1`	`A -> V (in dbSNP:rs1805088 [NCBI]).`	`VAR_013780`
`VARIANT`	`38 38`	`1`	`N -> S (in dbSNP:rs41427445 [NCBI]).`	`VAR_037004`
`VARIANT`	`82 82`	`1`	`E -> K (in dbSNP:rs1805089 [NCBI]).`	`VAR_013781`
`VARIANT`	`127 127`	`1`	`N -> K (in dbSNP:rs3918252 [NCBI]).`	`VAR_020054`
`VARIANT`	`239 239`	`1`	`R -> H (in dbSNP:rs28763886 [NCBI]).`	`VAR_025165`
`VARIANT`	`279 279`	`1`	`Q -> R (common polymorphism; may be associated with susceptibility to LDH; dbSNP:rs17576 [NCBI]).`	`VAR_013782`
`VARIANT`	`571 571`	`1`	`F -> V (in dbSNP:rs35691798 [NCBI]).`	`VAR_025166 [3D]`
`VARIANT`	`574 574`	`1`	`P -> R (in dbSNP:rs2250889 [NCBI]).`	`VAR_024595 [3D]`
`VARIANT`	`668 668`	`1`	`R -> Q (in dbSNP:rs17577 [NCBI]).`	`VAR_014742 [3D]`
`MUTAGEN`	`402 402`		`E->Q: Loss of activity.`
`CONFLICT`	`110 110`		`F -> L (in Ref. 3; BAG35956).`
`HELIX`	`41 51`	`11`
`HELIX`	`68 78`	`11`
`HELIX`	`88 94`	`7`
`STRAND`	`103 105`	`3`
`STRAND`	`119 125`	`7`
`STRAND`	`130 132`	`3`
`HELIX`	`134 149`	`16`
`STRAND`	`151 153`	`3`
`STRAND`	`155 158`	`4`
`STRAND`	`164 171`	`8`
`STRAND`	`176 178`	`3`
`STRAND`	`183 186`	`4`
`STRAND`	`189 191`	`3`
`STRAND`	`194 196`	`3`
`TURN`	`197 200`	`4`
`STRAND`	`202 205`	`4`
`STRAND`	`213 219`	`7`
`HELIX`	`220 231`	`12`
`STRAND`	`245 247`	`3`
`STRAND`	`255 261`	`7`
`HELIX`	`262 265`	`4`
`STRAND`	`268 270`	`3`
`TURN`	`274 276`	`3`
`STRAND`	`279 283`	`5`
`STRAND`	`290 294`	`5`
`STRAND`	`297 301`	`5`
`STRAND`	`313 319`	`7`
`HELIX`	`320 323`	`4`
`STRAND`	`326 328`	`3`
`HELIX`	`333 335`	`3`
`TURN`	`340 344`	`5`
`STRAND`	`349 353`	`5`
`STRAND`	`356 358`	`3`
`STRAND`	`372 378`	`7`
`HELIX`	`379 382`	`4`
`STRAND`	`385 387`	`3`
`STRAND`	`391 394`	`4`
`HELIX`	`395 406`	`12`
`STRAND`	`420 422`	`3`
`HELIX`	`433 442`	`10`
`HELIX`	`515 517`	`3`
`STRAND`	`522 527`	`6`
`STRAND`	`530 535`	`6`
`STRAND`	`538 542`	`5`
`STRAND`	`545 547`	`3`
`STRAND`	`551 555`	`5`
`HELIX`	`556 559`	`4`
`STRAND`	`568 572`	`5`
`TURN`	`574 576`	`3`
`STRAND`	`579 583`	`5`
`STRAND`	`586 591`	`6`
`STRAND`	`594 600`	`7`
`HELIX`	`601 604`	`4`
`STRAND`	`615 618`	`4`
`STRAND`	`623 628`	`6`
`STRAND`	`631 636`	`6`
`TURN`	`637 640`	`4`
`HELIX`	`644 646`	`3`
`HELIX`	`650 653`	`4`
`STRAND`	`662 667`	`6`
`STRAND`	`670 675`	`6`
`STRAND`	`678 683`	`6`
`STRAND`	`690 696`	`7`
`TURN`	`697 700`	`4`

Sequence information

Length: 707 AA [This is the length of the unprocessed precursor]

Molecular weight: 78399 Da [This is the MW of the unprocessed precursor]

CRC64: 7B65AC8E2B47880A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY RYGYTRVAEM 

        70         80         90        100        110        120 
RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG VPDLGRFQTF EGDLKWHHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY SRDADIVIQF GVAEHGDGYP 

       190        200        210        220        230        240 
FDGKDGLLAH AFPPGPGIQG DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS 

       250        260        270        280        290        300 
YSACTTDGRS DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS 

       310        320        330        340        350        360 
ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP FTFLGKEYST 

       370        380        390        400        410        420 
CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY 

       430        440        450        460        470        480 
PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER 

       490        500        510        520        530        540 
PTAGPTGPPS AGPTGPPTAG PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW 

       550        560        570        580        590        600 
RFSEGRGSRP QGPFLIADKW PALPRKLDSV FEEPLSKKLF FFSGRQVWVY TGASVLGPRR 

       610        620        630        640        650        660 
LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV DRMFPGVPLD 

       670        680        690        700 
THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD ILQCPED

P14780 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools