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Matrix metalloproteinase-21 (MMP-21) (EC 3.4.24.-)

 MMP21_HUMAN             Reviewed;         569 AA.
Q8N119; Q5VZP9; Q8NG02;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
28-FEB-2018, entry version 137.
RecName: Full=Matrix metalloproteinase-21;
Short=MMP-21;
EC=3.4.24.-;
Flags: Precursor;
Name=MMP21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=12490321; DOI=10.1016/S0378-1119(02)01088-0;
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], FUNCTION, TISSUE
SPECIFICITY, AND VARIANT ALA-191.
TISSUE=Kidney;
PubMed=12617721; DOI=10.1042/BJ20030174;
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;
ALA-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].
PubMed=15164054; DOI=10.1038/nature02462;
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).
[5]
INVOLVEMENT IN HTX7, AND FUNCTION.
PubMed=26429889; DOI=10.1136/jmedgenet-2015-103336;
Perles Z., Moon S., Ta-Shma A., Yaacov B., Francescatto L.,
Edvardson S., Rein A.J., Elpeleg O., Katsanis N.;
"A human laterality disorder caused by a homozygous deleterious
mutation in MMP21.";
J. Med. Genet. 52:840-847(2015).
[6]
INVOLVEMENT IN HTX7, VARIANTS HTX7 TRP-31; LYS-215; THR-226; PRO-321;
CYS-360; HIS-375 AND GLY-408, AND FUNCTION.
PubMed=26437028; DOI=10.1038/ng.3376;
Guimier A., Gabriel G.C., Bajolle F., Tsang M., Liu H., Noll A.,
Schwartz M., El Malti R., Smith L.D., Klena N.T., Jimenez G.,
Miller N.A., Oufadem M., Moreau de Bellaing A., Yagi H.,
Saunders C.J., Baker C.N., Di Filippo S., Peterson K.A., Thiffault I.,
Bole-Feysot C., Cooley L.D., Farrow E.G., Masson C., Schoen P.,
Deleuze J.F., Nitschke P., Lyonnet S., de Pontual L., Murray S.A.,
Bonnet D., Kingsmore S.F., Amiel J., Bouvagnet P., Lo C.W.,
Gordon C.T.;
"MMP21 is mutated in human heterotaxy and is required for normal left-
right asymmetry in vertebrates.";
Nat. Genet. 47:1260-1263(2015).
[7]
INVOLVEMENT IN HTX7, VARIANTS HTX7 TYR-283 AND THR-285, AND FUNCTION.
PubMed=26437029; DOI=10.1038/ng.3410;
DDD study;
Akawi N., McRae J., Ansari M., Balasubramanian M., Blyth M.,
Brady A.F., Clayton S., Cole T., Deshpande C., Fitzgerald T.W.,
Foulds N., Francis R., Gabriel G., Gerety S.S., Goodship J.,
Hobson E., Jones W.D., Joss S., King D., Klena N., Kumar A., Lees M.,
Lelliott C., Lord J., McMullan D., O'Regan M., Osio D., Piombo V.,
Prigmore E., Rajan D., Rosser E., Sifrim A., Smith A.,
Swaminathan G.J., Turnpenny P., Whitworth J., Wright C.F., Firth H.V.,
Barrett J.C., Lo C.W., FitzPatrick D.R., Hurles M.E.;
"Discovery of four recessive developmental disorders using
probabilistic genotype and phenotype matching among 4,125 families.";
Nat. Genet. 47:1363-1369(2015).
-!- FUNCTION: Plays a specialized role in the generation of left-right
asymmetry during embryogenesis. May act as a negative regulator of
the NOTCH-signaling pathway (PubMed:26429889, PubMed:26437028).
Cleaves alpha-1-antitrypsin (PubMed:12617721).
{ECO:0000269|PubMed:12617721, ECO:0000269|PubMed:26429889,
ECO:0000269|PubMed:26437028}.
-!- 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: Secreted {ECO:0000305}.
-!- 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. {ECO:0000269|PubMed:12490321,
ECO:0000269|PubMed:12617721}.
-!- 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: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- DISEASE: Heterotaxy, visceral, 7, autosomal (HTX7) [MIM:616749]: A
form of visceral heterotaxy, a complex disorder due to disruption
of the normal left-right asymmetry of the thoracoabdominal organs.
Visceral heterotaxy or situs ambiguus results in randomization of
the placement of visceral organs, including the heart, lungs,
liver, spleen, and stomach. The organs are oriented randomly with
respect to the left-right axis and with respect to one another. It
can been associated with a variety of congenital defects including
cardiac malformations. HTX7 inheritance is autosomal recessive.
{ECO:0000269|PubMed:26429889, ECO:0000269|PubMed:26437028,
ECO:0000269|PubMed:26437029}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp21/";
-----------------------------------------------------------------------
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EMBL; AF331526; AAM92903.1; -; mRNA.
EMBL; AY121358; AAM78033.1; -; Genomic_DNA.
EMBL; AF520613; AAM75352.1; -; mRNA.
EMBL; AY885252; AAW62254.1; -; Genomic_DNA.
EMBL; AL158835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL360176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS7647.1; -.
RefSeq; NP_671724.1; NM_147191.1.
UniGene; Hs.314141; -.
ProteinModelPortal; Q8N119; -.
SMR; Q8N119; -.
STRING; 9606.ENSP00000357798; -.
DrugBank; DB00786; Marimastat.
MEROPS; M10.026; -.
iPTMnet; Q8N119; -.
PhosphoSitePlus; Q8N119; -.
BioMuta; MMP21; -.
DMDM; 317373390; -.
PaxDb; Q8N119; -.
PRIDE; Q8N119; -.
DNASU; 118856; -.
Ensembl; ENST00000368808; ENSP00000357798; ENSG00000154485.
GeneID; 118856; -.
KEGG; hsa:118856; -.
UCSC; uc001liu.5; human.
CTD; 118856; -.
DisGeNET; 118856; -.
EuPathDB; HostDB:ENSG00000154485.4; -.
GeneCards; MMP21; -.
HGNC; HGNC:14357; MMP21.
MalaCards; MMP21; -.
MIM; 608416; gene.
MIM; 616749; phenotype.
neXtProt; NX_Q8N119; -.
OpenTargets; ENSG00000154485; -.
PharmGKB; PA134885721; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00910000144034; -.
HOGENOM; HOG000113608; -.
HOVERGEN; HBG052483; -.
InParanoid; Q8N119; -.
KO; K08000; -.
OMA; PLDTAFY; -.
OrthoDB; EOG091G0C9G; -.
PhylomeDB; Q8N119; -.
TreeFam; TF315428; -.
GeneWiki; MMP21; -.
GenomeRNAi; 118856; -.
PRO; PR:Q8N119; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000154485; -.
CleanEx; HS_MMP21; -.
Genevisible; Q8N119; HS.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0061371; P:determination of heart left/right asymmetry; ISS:UniProtKB.
GO; GO:0007368; P:determination of left/right symmetry; IMP:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 2.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
Pfam; PF00045; Hemopexin; 3.
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; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Glycoprotein; Heterotaxy; Hydrolase; Metal-binding;
Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 144 {ECO:0000250}.
/FTId=PRO_0000028839.
CHAIN 145 569 Matrix metalloproteinase-21.
/FTId=PRO_0000028840.
REPEAT 330 389 Hemopexin 1.
REPEAT 391 447 Hemopexin 2.
REPEAT 448 496 Hemopexin 3.
REPEAT 503 559 Hemopexin 4.
MOTIF 115 122 Cysteine switch. {ECO:0000250}.
ACT_SITE 284 284 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 117 117 Zinc; in inhibited form. {ECO:0000250}.
METAL 283 283 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 287 287 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 293 293 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 329 560 {ECO:0000250}.
VARIANT 31 31 R -> W (in HTX7; found associated with K-
215; dbSNP:rs746379956).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076319.
VARIANT 95 95 A -> E (in dbSNP:rs28381282).
{ECO:0000269|Ref.3}.
/FTId=VAR_022291.
VARIANT 115 115 P -> Q (in dbSNP:rs28381284).
{ECO:0000269|Ref.3}.
/FTId=VAR_022292.
VARIANT 191 191 V -> A (in dbSNP:rs10901425).
{ECO:0000269|PubMed:12617721,
ECO:0000269|Ref.3}.
/FTId=VAR_019393.
VARIANT 215 215 E -> K (in HTX7; found associated with W-
31; dbSNP:rs145789868).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076320.
VARIANT 226 226 I -> T (in HTX7; dbSNP:rs781127723).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076321.
VARIANT 263 263 D -> E (in dbSNP:rs34811493).
/FTId=VAR_032824.
VARIANT 283 283 H -> Y (in HTX7).
{ECO:0000269|PubMed:26437029}.
/FTId=VAR_076322.
VARIANT 285 285 I -> T (in HTX7; dbSNP:rs747668147).
{ECO:0000269|PubMed:26437029}.
/FTId=VAR_076323.
VARIANT 311 311 A -> T (in dbSNP:rs17173746).
/FTId=VAR_057803.
VARIANT 321 321 A -> P (in HTX7; dbSNP:rs773125891).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076324.
VARIANT 349 349 E -> G (in dbSNP:rs28381302).
{ECO:0000269|Ref.3}.
/FTId=VAR_022293.
VARIANT 360 360 R -> C (in HTX7; dbSNP:rs946722250).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076325.
VARIANT 360 360 R -> H (in dbSNP:rs17153524).
/FTId=VAR_057804.
VARIANT 375 375 R -> H (in HTX7).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076326.
VARIANT 408 408 R -> G (in HTX7; unknown pathological
significance; dbSNP:rs150320323).
{ECO:0000269|PubMed:26437028}.
/FTId=VAR_076327.
VARIANT 454 454 A -> V (in dbSNP:rs28381319).
{ECO:0000269|Ref.3}.
/FTId=VAR_022294.
SEQUENCE 569 AA; 65043 MW; 6785EF34F5B5105E CRC64;
MLAASIFRPT LLLCWLAAPW PTQPESLFHS RDRSDLEPSP LRQAKPIADL HAAQRFLSRY
GWSGVWAAWG PSPEGPPETP KGAALAEAVR RFQRANALPA SGELDAATLA AMNRPRCGVP
DMRPPPPSAP PSPPGPPPRA RSRRSPRAPL SLSRRGWQPR GYPDGGAAQA FSKRTLSWRL
LGEALSSQLS VADQRRIVAL AFRMWSEVTP LDFREDLAAP GAAVDIKLGF GRGRHLGCPR
AFDGSGQEFA HAWRLGDIHF DDDEHFTPPT SDTGISLLKV AVHEIGHVLG LPHTYRTGSI
MQPNYIPQEP AFELDWSDRK AIQKLYGSCE GSFDTAFDWI RKERNQYGEV MVRFSTYFFR
NSWYWLYENR NNRTRYGDPI QILTGWPGIP THNIDAFVHI WTWKRDERYF FQGNQYWRYD
SDKDQALTED EQGKSYPKLI SEGFPGIPSP LDTAFYDRRQ KLIYFFKESL VFAFDVNRNR
VLNSYPKRIT EVFPAVIPQN HPFRNIDSAY YSYAYNSIFF FKGNAYWKVV NDKDKQQNSW
LPANGLFPKK FISEKWFDVC DVHISTLNM


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