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UniProtKB/Swiss-Prot entry Q8N119


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MMP21_HUMAN
Primary accession number Q8N119
Secondary accession numbers Q5VZP9 Q8NG02
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 62)
Name and origin of the protein
Protein name Matrix metalloproteinase-21 [Precursor]
Synonyms MMP-21
EC 3.4.24.-
Gene name
Name: MMP21
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT VAL-191.
DOI=10.1016/S0378-1119(02)01088-0; PubMed=12490321 [NCBI, ExPASy, EBI, Israel, Japan]
Ahokas K., Lohi J., Lohi H., Elomaa O., Karjalainen-Lindsberg M.-L., Kere J., Saarialho-Kere U.;
"Matrix metalloproteinase-21, the human orthologue for XMMP, is expressed during fetal development and in cancer.";
Gene 301:31-41(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
TISSUE=Kidney;
DOI=10.1042/BJ20030174; PubMed=12617721 [NCBI, ExPASy, EBI, Israel, Japan]
Marchenko G.N., Marchenko N.D., Strongin A.Y.;
"The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein.";
Biochem. J. 372:503-515(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-95; GLN-115; VAL-191; GLY-349 AND VAL-454.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-191.
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF331526; AAM92903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY121358; AAM78033.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF520613; AAM75352.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY885252; AAW62254.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158835; CAH73211.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL360176; CAH73211.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL360176; CAI12086.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158835; CAI12086.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00295606; -.
RefSeq NP_671724.1; -.
UniGene Hs.314141
3D structure databases
HSSP Q02853; 1HV5. [HSSP ENTRY / PDB]
ModBase Q8N119.
Protein family/group databases
MEROPS M10.026; -.
Organism-specific databases
GeneCards GC10M127445; -.
HGNC HGNC:14357; MMP21.
GenAtlas MMP21.
MIM 608416; gene. [NCBI / EBI]
PharmGKB PA134885721; -.
Gene expression databases
ArrayExpress Q8N119; -.
Bgee Q8N119; -.
CleanEx HS_MMP21; -.
GermOnline ENSG00000154485; Homo sapiens.
Ontologies
GO
GO:0005578; Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from InterPro).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000585; Hemopexin/matrixin.
IPR018486; Hemopexin/matrixin_CS.
IPR018487; Hemopexin/matrixin_repeat.
IPR001818; Pept_M10A_M12B.
IPR016293; Pept_M10A_matrix.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.
Gene3D G3DSA:2.110.10.10; Hemopexin; 1.
Pfam PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS PR00138; MATRIXIN.
SMART SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00546; CYSTEINE_SWITCH; FALSE_NEG.
PS00024; HEMOPEXIN; FALSE_NEG.
PS00142; ZINC_PROTEASE; 1.
Proteomic databases
PRIDE Q8N119; -.
Genome annotation databases
Ensembl ENSG00000154485; Homo sapiens. [Contig view]
GeneID 118856; -.
KEGG hsa:118856; -.
Phylogenomic databases
HOGENOM Q8N119; -.
HOVERGEN Q8N119; -.
Other
NextBio 80358; -.
SOURCE MMP21; Homo sapiens.
ProtoNet Q8N119.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Cleavage on pair of basic residues; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Repeat; Secreted; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     Potential. 
PROPEP   25   144  120     By similarity. PRO_0000028839
CHAIN   145   569  425     Matrix metalloproteinase-21. PRO_0000028840
DOMAIN   333   391  59     Hemopexin-like 1. 
DOMAIN   394   449  56     Hemopexin-like 2. 
DOMAIN   451   499  49     Hemopexin-like 3. 
DOMAIN   506   549  44     Hemopexin-like 4. 
MOTIF   115   122  8     Cysteine switch (By similarity). 
ACT_SITE   284   284        By similarity. 
METAL   117   117        Zinc; in inhibited form (By similarity). 
METAL   283   283        Zinc; catalytic (By similarity). 
METAL   287   287        Zinc; catalytic (By similarity). 
METAL   293   293        Zinc; catalytic (By similarity). 
CARBOHYD   372   372        N-linked (GlcNAc...) (Potential). 
DISULFID   329   560        By similarity. 
VARIANT   95    95  1     A -> E (in dbSNP:rs28381282 [NCBI]). VAR_022291 
VARIANT   115   115  1     P -> Q (in dbSNP:rs28381284 [NCBI]). VAR_022292 
VARIANT   191   191  1     A -> V (in dbSNP:rs10901425 [NCBI]). VAR_019393 
VARIANT   263   263  1     D -> E (in dbSNP:rs34811493 [NCBI]). VAR_032824 
VARIANT   311   311  1     A -> T (in dbSNP:rs17173746 [NCBI]). VAR_057803 
VARIANT   349   349  1     E -> G (in dbSNP:rs28381302 [NCBI]). VAR_022293 
VARIANT   360   360  1     R -> H (in dbSNP:rs17153524 [NCBI]). VAR_057804 
VARIANT   454   454  1     A -> V (in dbSNP:rs28381319 [NCBI]). VAR_022294 
Sequence information
Length: 569 AA [This is the length of the unprocessed precursor] Molecular weight: 65015 Da [This is the MW of the unprocessed precursor] CRC64: 6DB9BD18ADA515D5 [This is a checksum on the sequence]
        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 AADQRRIVAL 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 

Q8N119 in FASTA format

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