MMP19_HUMAN
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 03-AUG-2022, entry version 210.
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/";
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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 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; Q99542; -.
DR PeptideAtlas; Q99542; -.
DR PRIDE; Q99542; -.
DR ProteomicsDB; 5645; -.
DR ProteomicsDB; 78315; -. [Q99542-1]
DR ProteomicsDB; 78316; -. [Q99542-3]
DR Antibodypedia; 2017; 487 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 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; RTDFSHY; -.
DR OrthoDB; 1075463at2759; -.
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; 10 hits in 1082 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 161 other tissues.
DR ExpressionAtlas; Q99542; baseline and differential.
DR Genevisible; Q99542; HS.
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:0001554; P:luteolysis; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 2.
DR Gene3D; 3.40.390.10; -; 1.
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; IPR028724; MMP19.
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:SF166; PTHR10201:SF166; 1.
DR Pfam; PF00045; Hemopexin; 3.
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; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
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
