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Q8N119 (MMP21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-21

Short name=MMP-21
EC=3.4.24.-
Gene names
Name:MMP21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Secreted Potential.

Tissue specificity

Identified in fetal brain, kidney and liver. In adult tissues found primarily in ovary, kidney, liver, lung, placenta, brain and peripheral blood leukocytes. Expressed as well in various cancer cell lines. Ref.1 Ref.2

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

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 144120 By similarity
PRO_0000028839
Chain145 – 569425Matrix metalloproteinase-21
PRO_0000028840

Regions

Repeat330 – 38960Hemopexin 1
Repeat391 – 44757Hemopexin 2
Repeat448 – 49649Hemopexin 3
Repeat503 – 55957Hemopexin 4
Motif115 – 1228Cysteine switch By similarity

Sites

Active site2841 By similarity
Metal binding1171Zinc; in inhibited form By similarity
Metal binding2831Zinc; catalytic By similarity
Metal binding2871Zinc; catalytic By similarity
Metal binding2931Zinc; catalytic By similarity

Amino acid modifications

Glycosylation3721N-linked (GlcNAc...) Potential
Disulfide bond329 ↔ 560 By similarity

Natural variations

Natural variant951A → E. Ref.3
Corresponds to variant rs28381282 [ dbSNP | Ensembl ].
VAR_022291
Natural variant1151P → Q. Ref.3
Corresponds to variant rs28381284 [ dbSNP | Ensembl ].
VAR_022292
Natural variant1911V → A. Ref.2 Ref.3
Corresponds to variant rs10901425 [ dbSNP | Ensembl ].
VAR_019393
Natural variant2631D → E.
Corresponds to variant rs34811493 [ dbSNP | Ensembl ].
VAR_032824
Natural variant3111A → T.
Corresponds to variant rs17173746 [ dbSNP | Ensembl ].
VAR_057803
Natural variant3491E → G. Ref.3
Corresponds to variant rs28381302 [ dbSNP | Ensembl ].
VAR_022293
Natural variant3601R → H.
Corresponds to variant rs17153524 [ dbSNP | Ensembl ].
VAR_057804
Natural variant4541A → V. Ref.3
Corresponds to variant rs28381319 [ dbSNP | Ensembl ].
VAR_022294

Sequences

Sequence LengthMass (Da)Tools
Q8N119 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 6785EF34F5B5105E

FASTA56965,043
        10         20         30         40         50         60 
MLAASIFRPT LLLCWLAAPW PTQPESLFHS RDRSDLEPSP LRQAKPIADL HAAQRFLSRY 

        70         80         90        100        110        120 
GWSGVWAAWG PSPEGPPETP KGAALAEAVR RFQRANALPA SGELDAATLA AMNRPRCGVP 

       130        140        150        160        170        180 
DMRPPPPSAP PSPPGPPPRA RSRRSPRAPL SLSRRGWQPR GYPDGGAAQA FSKRTLSWRL 

       190        200        210        220        230        240 
LGEALSSQLS VADQRRIVAL AFRMWSEVTP LDFREDLAAP GAAVDIKLGF GRGRHLGCPR 

       250        260        270        280        290        300 
AFDGSGQEFA HAWRLGDIHF DDDEHFTPPT SDTGISLLKV AVHEIGHVLG LPHTYRTGSI 

       310        320        330        340        350        360 
MQPNYIPQEP AFELDWSDRK AIQKLYGSCE GSFDTAFDWI RKERNQYGEV MVRFSTYFFR 

       370        380        390        400        410        420 
NSWYWLYENR NNRTRYGDPI QILTGWPGIP THNIDAFVHI WTWKRDERYF FQGNQYWRYD 

       430        440        450        460        470        480 
SDKDQALTED EQGKSYPKLI SEGFPGIPSP LDTAFYDRRQ KLIYFFKESL VFAFDVNRNR 

       490        500        510        520        530        540 
VLNSYPKRIT EVFPAVIPQN HPFRNIDSAY YSYAYNSIFF FKGNAYWKVV NDKDKQQNSW 

       550        560 
LPANGLFPKK FISEKWFDVC DVHISTLNM 

« Hide

References

« Hide 'large scale' references
[1]"Matrix metalloproteinase-21, the human orthologue for XMMP, is expressed during fetal development and in cancer."
Ahokas K., Lohi J., Lohi H., Elomaa O., Karjalainen-Lindsberg M.-L., Kere J., Saarialho-Kere U.
Gene 301:31-41(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein."
Marchenko G.N., Marchenko N.D., Strongin A.Y.
Biochem. J. 372:503-515(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANT ALA-191.
Tissue: Kidney.
[3]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-95; GLN-115; ALA-191; GLY-349 AND VAL-454.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF331526 mRNA. Translation: AAM92903.1.
AY121358 Genomic DNA. Translation: AAM78033.1.
AF520613 mRNA. Translation: AAM75352.1.
AY885252 Genomic DNA. Translation: AAW62254.1.
AL158835, AL360176 Genomic DNA. Translation: CAH73211.1.
AL360176, AL158835 Genomic DNA. Translation: CAI12086.1.
RefSeqNP_671724.1. NM_147191.1.
UniGeneHs.314141.

3D structure databases

ProteinModelPortalQ8N119.
SMRQ8N119. Positions 52-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000357798.

Protein family/group databases

MEROPSM10.026.

PTM databases

PhosphoSiteQ8N119.

Polymorphism databases

DMDM317373390.

Proteomic databases

PaxDbQ8N119.
PRIDEQ8N119.

Protocols and materials databases

DNASU118856.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368808; ENSP00000357798; ENSG00000154485.
GeneID118856.
KEGGhsa:118856.
UCSCuc001liu.3. human.

Organism-specific databases

CTD118856.
GeneCardsGC10M127445.
HGNCHGNC:14357. MMP21.
HPAHPA024429.
MIM608416. gene.
neXtProtNX_Q8N119.
PharmGKBPA134885721.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG115777.
HOGENOMHOG000113608.
HOVERGENHBG052483.
InParanoidQ8N119.
KOK08000.
OMALYENRNN.
OrthoDBEOG7X9G6K.
PhylomeDBQ8N119.
TreeFamTF315428.

Gene expression databases

BgeeQ8N119.
CleanExHS_MMP21.
GenevestigatorQ8N119.

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.
IPR024079. MetalloPept_cat_dom.
IPR028719. MMP21.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF14. PTHR10201:SF14. 1 hit.
PfamPF00045. Hemopexin. 3 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]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP21.
GenomeRNAi118856.
NextBio80358.
PROQ8N119.
SOURCESearch...

Entry information

Entry nameMMP21_HUMAN
AccessionPrimary (citable) accession number: Q8N119
Secondary accession number(s): Q5VZP9, Q8NG02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM