ID MMP19_HUMAN Reviewed; 508 AA. AC Q99542; B4E030; O15278; O95606; Q99580; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 24-JAN-2024, entry version 218. DE RecName: Full=Matrix metalloproteinase-19; DE Short=MMP-19; DE EC=3.4.24.-; DE AltName: Full=Matrix metalloproteinase RASI; DE AltName: Full=Matrix metalloproteinase-18; DE Short=MMP-18; DE Flags: Precursor; GN Name=MMP19; Synonyms=MMP18, RASI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Mammary gland; RX PubMed=8920941; DOI=10.1006/bbrc.1996.1688; RA Cossins J., Dudgeon T.J., Catlin G., Gearing A.J.H., Clements J.M.; RT "Identification of MMP-18, a putative novel human matrix RT metalloproteinase."; RL Biochem. Biophys. Res. Commun. 228:494-498(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=9020145; DOI=10.1074/jbc.272.7.4281; RA Pendas A.M., Knaeuper V.V., Puente X.S., Llano E., Mattei M.-G., Apte S., RA Murphy G., Lopez-Otin C.; RT "Identification and characterization of a novel human matrix RT metalloproteinase with unique structural characteristics, chromosomal RT location and tissue distribution."; RL J. Biol. Chem. 272:4281-4286(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Rheumatoid arthritic synovial fluid; RX PubMed=9232430; DOI=10.1016/s0165-2478(97)00057-6; RA Kolb C., Mauch S., Peter H.-H., Krawinkel U., Sedlacek R.; RT "The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels RT of a rheumatoid arthritis patient."; RL Immunol. Lett. 57:83-88(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Rheumatoid arthritic synovial fluid; RX PubMed=9562866; DOI=10.1016/s0171-2985(98)80049-1; RA Sedlacek R., Mauch S., Kolb B., Schaetzlein C., Eibel H., Peter H.-H., RA Schmitt J., Krawinkel U.; RT "Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of RT activated peripheral blood mononuclear cells and is detected as an RT autoantigen in rheumatoid arthritis."; RL Immunobiology 198:408-423(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). RA Mauch S., Sedlacek R., Krawinkel U., Schaetzlein C.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-103; THR-488 AND RP MET-491. RG NIEHS SNPs program; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [10] RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND MUTAGENESIS. RX PubMed=10809722; DOI=10.1074/jbc.275.20.14809; RA Stracke J.O., Hutton M., Stewart M., Pendas A.M., Smith B., Lopez-Otin C., RA Murphy G., Knaeuper V.; RT "Biochemical characterization of the catalytic domain of human matrix RT metalloproteinase 19. Evidence for a role as a potent basement membrane RT degrading enzyme."; RL J. Biol. Chem. 275:14809-14816(2000). RN [11] RP FUNCTION. RX PubMed=10922468; DOI=10.1016/s0014-5793(00)01819-6; RA Stracke J.O., Fosang A.J., Last K., Mercuri F.A., Pendas A.M., Llano E., RA Perris R., Di Cesare P.E., Murphy G., Knaeuper V.; RT "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage RT oligomeric matrix protein (COMP)."; RL FEBS Lett. 478:52-56(2000). RN [12] RP PHOSPHORYLATION. RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048; RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr., RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M., RA Dixon J.E., Yeo C.Y., Whitman M.; RT "A secreted tyrosine kinase acts in the extracellular environment."; RL Cell 158:1033-1044(2014). RN [13] RP INVOLVEMENT IN CODA. RX PubMed=25581579; DOI=10.1002/humu.22754; RA Hazlewood R.J., Roos B.R., Solivan-Timpe F., Honkanen R.A., Jampol L.M., RA Gieser S.C., Meyer K.J., Mullins R.F., Kuehn M.H., Scheetz T.E., Kwon Y.H., RA Alward W.L., Stone E.M., Fingert J.H.; RT "Heterozygous triplication of upstream regulatory sequences leads to RT dysregulation of matrix metalloproteinase 19 in patients with cavitary RT optic disc anomaly."; RL Hum. Mutat. 36:369-378(2015). CC -!- FUNCTION: Endopeptidase that degrades various components of the CC extracellular matrix, such as aggrecan and cartilage oligomeric matrix CC protein (comp), during development, haemostasis and pathological CC conditions (arthritic disease). May also play a role in CC neovascularization or angiogenesis. Hydrolyzes collagen type IV, CC laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin. CC {ECO:0000269|PubMed:10809722, ECO:0000269|PubMed:10922468}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Strongly inhibited by TIMP-2, TIMP-3 and TIMP-4, CC while TIMP-1 is less efficient. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=RASI-1, RASI-11; CC IsoId=Q99542-1; Sequence=Displayed; CC Name=2; Synonyms=RASI-9; CC IsoId=Q99542-3; Sequence=VSP_005457, VSP_005458; CC Name=3; Synonyms=RASI-6; CC IsoId=Q99542-4; Sequence=VSP_041893, VSP_041894; CC Name=4; CC IsoId=Q99542-5; Sequence=VSP_054573, VSP_054574, VSP_054575; CC -!- TISSUE SPECIFICITY: Expressed in mammary gland, placenta, lung, CC pancreas, ovary, small intestine, spleen, thymus, prostate, testis CC colon, heart and blood vessel walls. Not detected in brain and CC peripheral blood leukocytes. Also expressed in the synovial fluid of CC normal and rheumatoid patients (PubMed:8920941). CC {ECO:0000269|PubMed:8920941}. 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. CC -!- PTM: Activated by autolytic cleavage after Lys-97. CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK. CC {ECO:0000269|PubMed:25171405}. CC -!- DISEASE: Cavitary optic disc anomalies (CODA) [MIM:611543]: An ocular CC disease characterized by a profound excavation of the optic nerve. CC Clinical phenotype is variable and includes congenitally excavated CC optic nerves as well as other features of optic pit, optic nerve CC coloboma, and morning glory disk anomaly. Patients with CODA have a CC strong predilection for retinal detachment and/or separation of the CC retinal layers (retinoschisis) that lead to profound central vision CC loss. {ECO:0000269|PubMed:25581579}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Autoantigen anti-MMP19 are frequent in RA patients. CC {ECO:0000269|PubMed:9562866}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC99995.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/mmp19/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y08622; CAA69913.1; -; mRNA. DR EMBL; X92521; CAA63299.1; -; mRNA. DR EMBL; U37791; AAC51521.1; -; mRNA. DR EMBL; U38321; AAB63008.1; -; mRNA. DR EMBL; U38431; AAC99995.1; ALT_SEQ; mRNA. DR EMBL; U38322; AAB63009.1; -; mRNA. DR EMBL; AK303202; BAG64292.1; -; mRNA. DR EMBL; AY706993; AAT97983.1; -; Genomic_DNA. DR EMBL; AC023055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC050368; AAH50368.1; -; mRNA. DR CCDS; CCDS61146.1; -. [Q99542-5] DR CCDS; CCDS8895.1; -. [Q99542-1] DR PIR; JC5082; JC5082. DR RefSeq; NP_001259030.1; NM_001272101.1. [Q99542-5] DR RefSeq; NP_002420.1; NM_002429.5. [Q99542-1] DR AlphaFoldDB; Q99542; -. DR SMR; Q99542; -. DR BioGRID; 110470; 10. DR IntAct; Q99542; 1. DR STRING; 9606.ENSP00000313437; -. DR BindingDB; Q99542; -. DR ChEMBL; CHEMBL1938214; -. DR DrugBank; DB00786; Marimastat. DR MEROPS; M10.021; -. DR GlyCosmos; Q99542; 2 sites, 1 glycan. DR GlyGen; Q99542; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q99542; -. DR PhosphoSitePlus; Q99542; -. DR BioMuta; MMP19; -. DR DMDM; 12643345; -. DR jPOST; Q99542; -. DR MassIVE; Q99542; -. DR PaxDb; 9606-ENSP00000313437; -. DR PeptideAtlas; Q99542; -. DR ProteomicsDB; 5645; -. DR ProteomicsDB; 78315; -. [Q99542-1] DR ProteomicsDB; 78316; -. [Q99542-3] DR Antibodypedia; 2017; 513 antibodies from 36 providers. DR DNASU; 4327; -. DR Ensembl; ENST00000322569.9; ENSP00000313437.4; ENSG00000123342.16. [Q99542-1] DR Ensembl; ENST00000409200.7; ENSP00000386625.3; ENSG00000123342.16. [Q99542-5] DR Ensembl; ENST00000552872.5; ENSP00000446776.1; ENSG00000123342.16. [Q99542-4] DR GeneID; 4327; -. DR KEGG; hsa:4327; -. DR MANE-Select; ENST00000322569.9; ENSP00000313437.4; NM_002429.6; NP_002420.1. DR UCSC; uc001sib.5; human. [Q99542-1] DR AGR; HGNC:7165; -. DR CTD; 4327; -. DR DisGeNET; 4327; -. DR GeneCards; MMP19; -. DR HGNC; HGNC:7165; MMP19. DR HPA; ENSG00000123342; Tissue enhanced (adipose). DR MalaCards; MMP19; -. DR MIM; 601807; gene. DR MIM; 611543; phenotype. DR neXtProt; NX_Q99542; -. DR OpenTargets; ENSG00000123342; -. DR Orphanet; 464760; Familial cavitary optic disc anomaly. DR PharmGKB; PA30876; -. DR VEuPathDB; HostDB:ENSG00000123342; -. DR eggNOG; KOG1565; Eukaryota. DR GeneTree; ENSGT00940000158593; -. DR HOGENOM; CLU_015489_8_3_1; -. DR InParanoid; Q99542; -. DR OMA; VMGYWRK; -. DR OrthoDB; 2225278at2759; -. DR PhylomeDB; Q99542; -. DR TreeFam; TF315428; -. DR PathwayCommons; Q99542; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR SignaLink; Q99542; -. DR SIGNOR; Q99542; -. DR BioGRID-ORCS; 4327; 11 hits in 1167 CRISPR screens. DR ChiTaRS; MMP19; human. DR GeneWiki; MMP19; -. DR GenomeRNAi; 4327; -. DR Pharos; Q99542; Tbio. DR PRO; PR:Q99542; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q99542; Protein. DR Bgee; ENSG00000123342; Expressed in left uterine tube and 163 other cell types or tissues. DR ExpressionAtlas; Q99542; baseline and differential. DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome. DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB. DR CDD; cd00094; HX; 1. DR CDD; cd04278; ZnMc_MMP; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 2. DR InterPro; IPR000585; Hemopexin-like_dom. DR InterPro; IPR036375; Hemopexin-like_dom_sf. DR InterPro; IPR018487; Hemopexin-like_repeat. DR InterPro; IPR033739; M10A_MMP. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001818; Pept_M10_metallopeptidase. DR InterPro; IPR021190; Pept_M10A. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR002477; Peptidoglycan-bd-like. DR InterPro; IPR036365; PGBD-like_sf. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. DR PANTHER; PTHR10201:SF166; MATRIX METALLOPROTEINASE-19; 1. DR Pfam; PF00045; Hemopexin; 4. DR Pfam; PF00413; Peptidase_M10; 1. DR Pfam; PF01471; PG_binding_1; 1. DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1. DR PRINTS; PR00138; MATRIXIN. DR SMART; SM00120; HX; 4. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; Q99542; HS. PE 1: Evidence at protein level; KW Alternative splicing; Angiogenesis; Calcium; Collagen degradation; KW Developmental protein; Differentiation; Direct protein sequencing; KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; KW Metal-binding; Metalloprotease; Phosphoprotein; Protease; KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT PROPEP 19..97 FT /evidence="ECO:0000269|PubMed:10809722" FT /id="PRO_0000028826" FT CHAIN 98..508 FT /note="Matrix metalloproteinase-19" FT /id="PRO_0000028827" FT REPEAT 286..333 FT /note="Hemopexin 1" FT REPEAT 334..380 FT /note="Hemopexin 2" FT REPEAT 381..425 FT /note="Hemopexin 3" FT REPEAT 426..472 FT /note="Hemopexin 4" FT REGION 262..288 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 83..90 FT /note="Cysteine switch" FT /evidence="ECO:0000250" FT ACT_SITE 213 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /note="in inhibited form" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 216 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 222 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT CARBOHYD 464 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 289..472 FT /evidence="ECO:0000250" FT VAR_SEQ 1..286 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_005457" FT VAR_SEQ 58..63 FT /note="RAFQEA -> SLRSAG (in isoform 3)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_041893" FT VAR_SEQ 64..508 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_041894" FT VAR_SEQ 174..255 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054573" FT VAR_SEQ 287..298 FT /note="DPCSSELDAMML -> MGVTWDFSMSNG (in isoform 2)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_005458" FT VAR_SEQ 300..387 FT /note="PRGKTYAFKGDYVWTVSDSGPGPLFRVSALWEGLPGNLDAAVYSPRTQWIHF FT FKGDKVWRYINFKMSPGFPKKLNRVEPNLDAALYWP -> EAPPLQAVGRRWGQPADPE FT AWTNGSDMGLQHEQWRAPWEDLCFQGGLCVDCIRFRTGPLVPSVCPLGGAPRKPGCCCL FT LASNTMDSLL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054574" FT VAR_SEQ 388..508 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054575" FT VARIANT 103 FT /note="R -> C (in dbSNP:rs17844794)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_021036" FT VARIANT 245 FT /note="P -> S (in dbSNP:rs1056784)" FT /id="VAR_054006" FT VARIANT 488 FT /note="P -> T (in dbSNP:rs17118042)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_021037" FT VARIANT 491 FT /note="T -> M (in dbSNP:rs17844806)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_021038" FT MUTAGEN 88 FT /note="E->P: Reduced autolysis rate." FT /evidence="ECO:0000269|PubMed:10809722" FT MUTAGEN 90 FT /note="P->V: Reduced autolysis rate." FT /evidence="ECO:0000269|PubMed:10809722" FT CONFLICT 376 FT /note="V -> S (in Ref. 1; CAA69913)" FT /evidence="ECO:0000305" SQ SEQUENCE 508 AA; 57357 MW; BA480549AA9A8972 CRC64; MNCQQLWLGF LLPMTVSGRV LGLAEVAPVD YLSQYGYLQK PLEGSNNFKP EDITEALRAF QEASELPVSG QLDDATRARM RQPRCGLEDP FNQKTLKYLL LGRWRKKHLT FRILNLPSTL PPHTARAALR QAFQDWSNVA PLTFQEVQAG AADIRLSFHG RQSSYCSNTF DGPGRVLAHA DIPELGSVHF DEDEFWTEGT YRGVNLRIIA AHEVGHALGL GHSRYSQALM APVYEGYRPH FKLHPDDVAG IQALYGKKSP VIRDEEEEET ELPTVPPVPT EPSPMPDPCS SELDAMMLGP RGKTYAFKGD YVWTVSDSGP GPLFRVSALW EGLPGNLDAA VYSPRTQWIH FFKGDKVWRY INFKMSPGFP KKLNRVEPNL DAALYWPLNQ KVFLFKGSGY WQWDELARTD FSSYPKPIKG LFTGVPNQPS AAMSWQDGRV YFFKGKVYWR LNQQLRVEKG YPRNISHNWM HCRPRTIDTT PSGGNTTPSG TGITLDTTLS ATETTFEY //