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Q9JHI0

- MMP19_MOUSE

UniProt

Q9JHI0 - MMP19_MOUSE

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Protein

Matrix metalloproteinase-19

Gene

Mmp19

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Cleaves aggrecan at the 360-Ser-|-Phe-361 site.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi86 – 861Zinc; in inhibited formBy similarity
Metal bindingi213 – 2131Zinc; catalyticPROSITE-ProRule annotation
Active sitei214 – 2141PROSITE-ProRule annotation
Metal bindingi217 – 2171Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi223 – 2231Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. collagen catabolic process Source: UniProtKB-KW
  4. luteolysis Source: Ensembl
  5. ovarian follicle development Source: Ensembl
  6. ovulation from ovarian follicle Source: Ensembl
  7. response to cAMP Source: Ensembl
  8. response to hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Collagen degradation, Differentiation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM10.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-19 (EC:3.4.24.-)
Short name:
MMP-19
Alternative name(s):
Matrix metalloproteinase RASI
Gene namesi
Name:Mmp19
Synonyms:Rasi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1927899. Mmp19.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. extracellular region Source: Reactome
  3. plasma membrane Source: UniProtKB-KW
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 9880By similarityPRO_0000028828Add
BLAST
Chaini99 – 512414Matrix metalloproteinase-19PRO_0000028829Add
BLAST
Propeptidei513 – 52715Removed in mature formSequence AnalysisPRO_0000028830Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi289 ↔ 471By similarity
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
Lipidationi512 – 5121GPI-anchor amidated aspartateSequence Analysis
Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Activated by autolytic cleavage after Lys-98.By similarity
Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiQ9JHI0.
PRIDEiQ9JHI0.

PTM databases

PhosphoSiteiQ9JHI0.

Expressioni

Tissue specificityi

Highly expressed in the liver. Expressed in the arterial tunica media of large blood vessels.

Developmental stagei

Expressed in proliferating chondrocytes in the chondroepiphysis during musculoskeletal development.

Gene expression databases

BgeeiQ9JHI0.
CleanExiMM_MMP19.
ExpressionAtlasiQ9JHI0. baseline and differential.
GenevestigatoriQ9JHI0.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026411.

Structurei

3D structure databases

ProteinModelPortaliQ9JHI0.
SMRiQ9JHI0. Positions 39-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati286 – 33348Hemopexin 1Add
BLAST
Repeati334 – 37239Hemopexin 2Add
BLAST
Repeati377 – 42549Hemopexin 3Add
BLAST
Repeati426 – 47146Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi84 – 918Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi266 – 2716Poly-Glu

Domaini

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.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9JHI0.
KOiK07998.
OMAiVAKGYPR.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ9JHI0.
TreeFamiTF315428.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028724. MMP19.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF117. PTHR10201:SF117. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JHI0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDWQQLWLAF LLPMTVSGRA LGPTEKEAVL DYLLQYGYLQ KPLEGADDFR
60 70 80 90 100
LEDITEALRT FQEASGLPIS GQMDDATRAR MKQPRCGLED PFNQKSLKYL
110 120 130 140 150
LLGHWRKKNL TFRIFNVPST LSLPRVRAAL HQAFKYWSSV APLTFREVKA
160 170 180 190 200
GWADIRLSFH GRQSLYCSNT FDGPGKVLAH ADIPELGSIH FDKDELWTEG
210 220 230 240 250
TYQGVNLRII AAHEVGHALG LGHSRYTQAL MAPVYAGYQP FFKLHPDDVA
260 270 280 290 300
GIQALYGKRS PETRDEEEET EMLTVSPVTA KPGPMPNPCS GEVDAMVLGP
310 320 330 340 350
RGKTYAFKGD YVWTVTDSGP GPLFQISALW EGLPGNLDAA VYSPRTRRTH
360 370 380 390 400
FFKGNKVWRY VDFKMSPGFP MKFNRVEPNL DAALYWPVNQ KVFLFKGSGY
410 420 430 440 450
WQWDELARTD LSRYPKPIKE LFTGVPDRPS AAMSWQDGQV YFFKGKEYWR
460 470 480 490 500
LNQQLRVAKG YPRNTTHWMH CGSQTPDTNS STGDVTPSTT DTVLGTTPST
510 520
MGSTLDIPSA TDSASLSFSA NVTLLGA
Length:527
Mass (Da):59,122
Last modified:October 1, 2000 - v1
Checksum:i8AD0AE41A1CD335E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155221 mRNA. Translation: AAF73292.1.
AF162446 mRNA. Translation: AAF80464.1.
AF153199 mRNA. Translation: AAG29880.1.
AK086808 mRNA. Translation: BAC39747.1.
CCDSiCCDS24292.1.
RefSeqiNP_067387.1. NM_021412.2.
UniGeneiMm.131266.

Genome annotation databases

EnsembliENSMUST00000026411; ENSMUSP00000026411; ENSMUSG00000025355.
GeneIDi58223.
KEGGimmu:58223.
UCSCiuc007hof.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155221 mRNA. Translation: AAF73292.1 .
AF162446 mRNA. Translation: AAF80464.1 .
AF153199 mRNA. Translation: AAG29880.1 .
AK086808 mRNA. Translation: BAC39747.1 .
CCDSi CCDS24292.1.
RefSeqi NP_067387.1. NM_021412.2.
UniGenei Mm.131266.

3D structure databases

ProteinModelPortali Q9JHI0.
SMRi Q9JHI0. Positions 39-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000026411.

Protein family/group databases

MEROPSi M10.021.

PTM databases

PhosphoSitei Q9JHI0.

Proteomic databases

MaxQBi Q9JHI0.
PRIDEi Q9JHI0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026411 ; ENSMUSP00000026411 ; ENSMUSG00000025355 .
GeneIDi 58223.
KEGGi mmu:58223.
UCSCi uc007hof.1. mouse.

Organism-specific databases

CTDi 4327.
MGIi MGI:1927899. Mmp19.

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000119132.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi Q9JHI0.
KOi K07998.
OMAi VAKGYPR.
OrthoDBi EOG7XPZ57.
PhylomeDBi Q9JHI0.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_199052. Degradation of the extracellular matrix.

Miscellaneous databases

NextBioi 314237.
PROi Q9JHI0.
SOURCEi Search...

Gene expression databases

Bgeei Q9JHI0.
CleanExi MM_MMP19.
ExpressionAtlasi Q9JHI0. baseline and differential.
Genevestigatori Q9JHI0.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028724. MMP19.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF117. PTHR10201:SF117. 1 hit.
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization, expression analysis and chromosomal mapping of mouse matrix metalloproteinase-19 (MMP-19)."
    Caterina J.J., Shi J., Kozak C.A., Engler J.A., Birkedal-Hansen H.
    Mol. Biol. Rep. 27:73-79(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  2. "Mmp19 encodes a GPI anchored matrix metalloprotease expressed in musculoskeletal, neural and epithelial tissues."
    Hurskainen T., Seldin M.F., Pendas A., Lopez-Otin C., Apte S.S.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The murine ortholog of matrix metalloproteinase 19: its cloning, gene organization, and expression."
    Mueller M.S., Harnasch M., Kolb C., Kusch J., Sadowski T., Sedlacek R.
    Gene 256:101-111(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Ola.
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-527.
    Strain: C57BL/6J.
    Tissue: Lung.

Entry informationi

Entry nameiMMP19_MOUSE
AccessioniPrimary (citable) accession number: Q9JHI0
Secondary accession number(s): Q8C360
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3