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Matrix metalloproteinase-19 (MMP-19) (EC 3.4.24.-) (Matrix metalloproteinase RASI)

 MMP19_MOUSE             Reviewed;         527 AA.
Q9JHI0; Q8C360;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-DEC-2018, entry version 172.
RecName: Full=Matrix metalloproteinase-19;
Short=MMP-19;
EC=3.4.24.-;
AltName: Full=Matrix metalloproteinase RASI;
Flags: Precursor;
Name=Mmp19; Synonyms=Rasi;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ;
PubMed=11092553; DOI=10.1023/A:1007196529604;
Caterina J.J., Shi J., Kozak C.A., Engler J.A., Birkedal-Hansen H.;
"Characterization, expression analysis and chromosomal mapping of
mouse matrix metalloproteinase-19 (MMP-19).";
Mol. Biol. Rep. 27:73-79(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Hurskainen T., Seldin M.F., Pendas A., Lopez-Otin C., Apte S.S.;
"Mmp19 encodes a GPI anchored matrix metalloprotease expressed in
musculoskeletal, neural and epithelial tissues.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/Ola;
PubMed=11054540; DOI=10.1016/S0378-1119(00)00369-3;
Mueller M.S., Harnasch M., Kolb C., Kusch J., Sadowski T.,
Sedlacek R.;
"The murine ortholog of matrix metalloproteinase 19: its cloning, gene
organization, and expression.";
Gene 256:101-111(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-527.
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
-!- FUNCTION: Endopeptidase that degrades various components of the
extracellular matrix, such as aggrecan and cartilage oligomeric
matrix protein (comp), during development, haemostasis and
pathological conditions (arthritic disease). May also play a role
in neovascularization or angiogenesis (By similarity). Hydrolyzes
collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin,
and type I gelatin (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}.
Secreted, extracellular space, extracellular matrix {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in the liver. Expressed in
the arterial tunica media of large blood vessels.
-!- DEVELOPMENTAL STAGE: Expressed in proliferating chondrocytes in
the chondroepiphysis during musculoskeletal development.
-!- 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: Activated by autolytic cleavage after Lys-98. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000250|UniProtKB:Q99542}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF155221; AAF73292.1; -; mRNA.
EMBL; AF162446; AAF80464.1; -; mRNA.
EMBL; AF153199; AAG29880.1; -; mRNA.
EMBL; AK086808; BAC39747.1; -; mRNA.
CCDS; CCDS24292.1; -.
RefSeq; NP_067387.1; NM_021412.3.
UniGene; Mm.131266; -.
ProteinModelPortal; Q9JHI0; -.
STRING; 10090.ENSMUSP00000026411; -.
MEROPS; M10.021; -.
iPTMnet; Q9JHI0; -.
PhosphoSitePlus; Q9JHI0; -.
MaxQB; Q9JHI0; -.
PaxDb; Q9JHI0; -.
PRIDE; Q9JHI0; -.
Ensembl; ENSMUST00000026411; ENSMUSP00000026411; ENSMUSG00000025355.
GeneID; 58223; -.
KEGG; mmu:58223; -.
UCSC; uc007hof.1; mouse.
CTD; 4327; -.
MGI; MGI:1927899; Mmp19.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00940000158593; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9JHI0; -.
KO; K07998; -.
OMA; ALYWPLN; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q9JHI0; -.
TreeFam; TF315428; -.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
PRO; PR:Q9JHI0; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000025355; Expressed in 98 organ(s), highest expression level in liver.
CleanEx; MM_MMP19; -.
ExpressionAtlas; Q9JHI0; baseline and differential.
Genevisible; Q9JHI0; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0001554; P:luteolysis; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028724; MMP19.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF166; PTHR10201:SF166; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Angiogenesis; Calcium; Cell membrane; Collagen degradation;
Complete proteome; Developmental protein; Differentiation;
Disulfide bond; Extracellular matrix; Glycoprotein; GPI-anchor;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease;
Phosphoprotein; Protease; Reference proteome; Repeat; Secreted;
Signal; Zinc; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 98 {ECO:0000250}.
/FTId=PRO_0000028828.
CHAIN 99 512 Matrix metalloproteinase-19.
/FTId=PRO_0000028829.
PROPEP 513 527 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000028830.
REPEAT 286 333 Hemopexin 1.
REPEAT 334 372 Hemopexin 2.
REPEAT 377 425 Hemopexin 3.
REPEAT 426 471 Hemopexin 4.
MOTIF 84 91 Cysteine switch. {ECO:0000250}.
COMPBIAS 266 271 Poly-Glu.
ACT_SITE 214 214 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 86 86 Zinc; in inhibited form. {ECO:0000250}.
METAL 213 213 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 217 217 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 223 223 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
LIPID 512 512 GPI-anchor amidated aspartate.
{ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 521 521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 289 471 {ECO:0000250}.
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


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