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Q9JHI0 (MMP19_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-19
Short name=MMP-19
EC=3.4.24.-
Alternative name(s):
Matrix metalloproteinase RASI
Gene names
Name:Mmp19
Synonyms:Rasi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side Probable. Secreted › extracellular space › extracellular matrix Probable.

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.

Post-translational modification

Activated by autolytic cleavage after Lys-98 By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin-like domains.

Ontologies

Keywords
   Biological processAngiogenesis
Collagen degradation
Differentiation
   Cellular componentCell membrane
Extracellular matrix
Membrane
Secreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

collagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

luteolysis

Inferred from electronic annotation. Source: Compara

ovarian follicle development

Inferred from electronic annotation. Source: Compara

ovulation from ovarian follicle

Inferred from electronic annotation. Source: Compara

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to cAMP

Inferred from electronic annotation. Source: Compara

response to hormone stimulus

Inferred from electronic annotation. Source: Compara

   Cellular_componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from sequence or structural similarity Ref.3. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 9880 By similarity
PRO_0000028828
Chain99 – 512414Matrix metalloproteinase-19
PRO_0000028829
Propeptide513 – 52715Removed in mature form Potential
PRO_0000028830

Regions

Domain293 – 33543Hemopexin-like 1
Domain337 – 37842Hemopexin-like 2
Domain380 – 42748Hemopexin-like 3
Domain429 – 47143Hemopexin-like 4
Motif84 – 918Cysteine switch By similarity
Compositional bias266 – 2716Poly-Glu

Sites

Active site2141 By similarity
Metal binding861Zinc; in inhibited form By similarity
Metal binding2131Zinc; catalytic By similarity
Metal binding2171Zinc; catalytic By similarity
Metal binding2231Zinc; catalytic By similarity

Amino acid modifications

Lipidation5121GPI-anchor amidated aspartate Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Glycosylation5211N-linked (GlcNAc...) Potential
Disulfide bond289 ↔ 471 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JHI0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8AD0AE41A1CD335E

FASTA52759,122
        10         20         30         40         50         60 
MDWQQLWLAF LLPMTVSGRA LGPTEKEAVL DYLLQYGYLQ KPLEGADDFR LEDITEALRT 

        70         80         90        100        110        120 
FQEASGLPIS GQMDDATRAR MKQPRCGLED PFNQKSLKYL LLGHWRKKNL TFRIFNVPST 

       130        140        150        160        170        180 
LSLPRVRAAL HQAFKYWSSV APLTFREVKA GWADIRLSFH GRQSLYCSNT FDGPGKVLAH 

       190        200        210        220        230        240 
ADIPELGSIH FDKDELWTEG TYQGVNLRII AAHEVGHALG LGHSRYTQAL MAPVYAGYQP 

       250        260        270        280        290        300 
FFKLHPDDVA GIQALYGKRS PETRDEEEET EMLTVSPVTA KPGPMPNPCS GEVDAMVLGP 

       310        320        330        340        350        360 
RGKTYAFKGD YVWTVTDSGP GPLFQISALW EGLPGNLDAA VYSPRTRRTH FFKGNKVWRY 

       370        380        390        400        410        420 
VDFKMSPGFP MKFNRVEPNL DAALYWPVNQ KVFLFKGSGY WQWDELARTD LSRYPKPIKE 

       430        440        450        460        470        480 
LFTGVPDRPS AAMSWQDGQV YFFKGKEYWR LNQQLRVAKG YPRNTTHWMH CGSQTPDTNS 

       490        500        510        520 
STGDVTPSTT DTVLGTTPST MGSTLDIPSA TDSASLSFSA NVTLLGA

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF155221 mRNA. Translation: AAF73292.1.
AF162446 mRNA. Translation: AAF80464.1.
AF153199 mRNA. Translation: AAG29880.1.
AK086808 mRNA. Translation: BAC39747.1.
IPIIPI00119421.
RefSeqNP_067387.1. NM_021412.2.
UniGeneMm.131266.
Mm.24630.

3D structure databases

ProteinModelPortalQ9JHI0.
SMRQ9JHI0. Positions 39-473.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000026411.

Protein family/group databases

MEROPSM10.021.

PTM databases

PhosphoSiteQ9JHI0.

Proteomic databases

PRIDEQ9JHI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026411; ENSMUSP00000026411; ENSMUSG00000025355.
GeneID58223.
KEGGmmu:58223.

Organism-specific databases

CTD4327.
MGIMGI:1927899. Mmp19.

Phylogenomic databases

eggNOGNOG295915.
GeneTreeENSGT00570000079061.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ9JHI0.
KOK07998.
OMAYWSSVAP.
OrthoDBEOG495ZRW.

Gene expression databases

ArrayExpressQ9JHI0.
BgeeQ9JHI0.
CleanExMM_MMP19.
GenevestigatorQ9JHI0.
GermOnlineENSMUSG00000025355. Mus musculus.

Family and domain databases

Gene3D1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_Metazoans.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. False negative.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314237.
SOURCESearch...

Entry information

Entry nameMMP19_MOUSE
AccessionPrimary (citable) accession number: Q9JHI0
Secondary accession number(s): Q8C360
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents