ID   MMP19_MOUSE             Reviewed;         527 AA.
AC   Q9JHI0; Q8C360;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 197.
DE   RecName: Full=Matrix metalloproteinase-19;
DE            Short=MMP-19;
DE            EC=3.4.24.-;
DE   AltName: Full=Matrix metalloproteinase RASI;
DE   Flags: Precursor;
GN   Name=Mmp19; Synonyms=Rasi;
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].
RC   STRAIN=C3H/HeJ;
RX   PubMed=11092553; DOI=10.1023/a:1007196529604;
RA   Caterina J.J., Shi J., Kozak C.A., Engler J.A., Birkedal-Hansen H.;
RT   "Characterization, expression analysis and chromosomal mapping of mouse
RT   matrix metalloproteinase-19 (MMP-19).";
RL   Mol. Biol. Rep. 27:73-79(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hurskainen T., Seldin M.F., Pendas A., Lopez-Otin C., Apte S.S.;
RT   "Mmp19 encodes a GPI anchored matrix metalloprotease expressed in
RT   musculoskeletal, neural and epithelial tissues.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Ola;
RX   PubMed=11054540; DOI=10.1016/s0378-1119(00)00369-3;
RA   Mueller M.S., Harnasch M., Kolb C., Kusch J., Sadowski T., Sedlacek R.;
RT   "The murine ortholog of matrix metalloproteinase 19: its cloning, gene
RT   organization, and expression.";
RL   Gene 256:101-111(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-527.
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).
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 (By similarity). Hydrolyzes collagen
CC       type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I
CC       gelatin (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted,
CC       extracellular space, extracellular matrix {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the liver. Expressed in the
CC       arterial tunica media of large blood vessels.
CC   -!- DEVELOPMENTAL STAGE: Expressed in proliferating chondrocytes in the
CC       chondroepiphysis during musculoskeletal development.
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-98. {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC       {ECO:0000250|UniProtKB:Q99542}.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; AF155221; AAF73292.1; -; mRNA.
DR   EMBL; AF162446; AAF80464.1; -; mRNA.
DR   EMBL; AF153199; AAG29880.1; -; mRNA.
DR   EMBL; AK086808; BAC39747.1; -; mRNA.
DR   CCDS; CCDS24292.1; -.
DR   RefSeq; NP_067387.1; NM_021412.3.
DR   AlphaFoldDB; Q9JHI0; -.
DR   SMR; Q9JHI0; -.
DR   STRING; 10090.ENSMUSP00000026411; -.
DR   MEROPS; M10.021; -.
DR   GlyCosmos; Q9JHI0; 4 sites, No reported glycans.
DR   GlyGen; Q9JHI0; 4 sites.
DR   iPTMnet; Q9JHI0; -.
DR   PhosphoSitePlus; Q9JHI0; -.
DR   MaxQB; Q9JHI0; -.
DR   PaxDb; 10090-ENSMUSP00000026411; -.
DR   ProteomicsDB; 291476; -.
DR   Antibodypedia; 2017; 513 antibodies from 36 providers.
DR   DNASU; 58223; -.
DR   Ensembl; ENSMUST00000026411.8; ENSMUSP00000026411.7; ENSMUSG00000025355.8.
DR   GeneID; 58223; -.
DR   KEGG; mmu:58223; -.
DR   UCSC; uc007hof.1; mouse.
DR   AGR; MGI:1927899; -.
DR   CTD; 4327; -.
DR   MGI; MGI:1927899; Mmp19.
DR   VEuPathDB; HostDB:ENSMUSG00000025355; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00940000158593; -.
DR   HOGENOM; CLU_015489_8_3_1; -.
DR   InParanoid; Q9JHI0; -.
DR   OMA; VMGYWRK; -.
DR   OrthoDB; 2225278at2759; -.
DR   PhylomeDB; Q9JHI0; -.
DR   TreeFam; TF315428; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   BioGRID-ORCS; 58223; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Mmp19; mouse.
DR   PRO; PR:Q9JHI0; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9JHI0; Protein.
DR   Bgee; ENSMUSG00000025355; Expressed in liver and 103 other cell types or tissues.
DR   ExpressionAtlas; Q9JHI0; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:MGI.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR018486; Hemopexin_CS.
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; PS00024; HEMOPEXIN; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q9JHI0; MM.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Calcium; Cell membrane; Collagen degradation;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
KW   Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..98
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028828"
FT   CHAIN           99..512
FT                   /note="Matrix metalloproteinase-19"
FT                   /id="PRO_0000028829"
FT   PROPEP          513..527
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028830"
FT   REPEAT          286..333
FT                   /note="Hemopexin 1"
FT   REPEAT          334..372
FT                   /note="Hemopexin 2"
FT   REPEAT          377..425
FT                   /note="Hemopexin 3"
FT   REPEAT          426..471
FT                   /note="Hemopexin 4"
FT   REGION          473..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           84..91
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         86
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         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   LIPID           512
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        289..471
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   527 AA;  59122 MW;  8AD0AE41A1CD335E CRC64;
     MDWQQLWLAF LLPMTVSGRA LGPTEKEAVL DYLLQYGYLQ KPLEGADDFR LEDITEALRT
     FQEASGLPIS GQMDDATRAR MKQPRCGLED PFNQKSLKYL LLGHWRKKNL TFRIFNVPST
     LSLPRVRAAL HQAFKYWSSV APLTFREVKA GWADIRLSFH GRQSLYCSNT FDGPGKVLAH
     ADIPELGSIH FDKDELWTEG TYQGVNLRII AAHEVGHALG LGHSRYTQAL MAPVYAGYQP
     FFKLHPDDVA GIQALYGKRS PETRDEEEET EMLTVSPVTA KPGPMPNPCS GEVDAMVLGP
     RGKTYAFKGD YVWTVTDSGP GPLFQISALW EGLPGNLDAA VYSPRTRRTH FFKGNKVWRY
     VDFKMSPGFP MKFNRVEPNL DAALYWPVNQ KVFLFKGSGY WQWDELARTD LSRYPKPIKE
     LFTGVPDRPS AAMSWQDGQV YFFKGKEYWR LNQQLRVAKG YPRNTTHWMH CGSQTPDTNS
     STGDVTPSTT DTVLGTTPST MGSTLDIPSA TDSASLSFSA NVTLLGA
//