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Matrix metalloproteinase-19 (MMP-19) (EC 3.4.24.-) (Matrix metalloproteinase RASI) (Matrix metalloproteinase-18) (MMP-18)

 MMP19_HUMAN             Reviewed;         508 AA.
Q99542; B4E030; O15278; O95606; Q99580;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
20-JUN-2018, entry version 187.
RecName: Full=Matrix metalloproteinase-19;
Short=MMP-19;
EC=3.4.24.-;
AltName: Full=Matrix metalloproteinase RASI;
AltName: Full=Matrix metalloproteinase-18;
Short=MMP-18;
Flags: Precursor;
Name=MMP19; Synonyms=MMP18, RASI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Mammary gland;
PubMed=8920941; DOI=10.1006/bbrc.1996.1688;
Cossins J., Dudgeon T.J., Catlin G., Gearing A.J.H., Clements J.M.;
"Identification of MMP-18, a putative novel human matrix
metalloproteinase.";
Biochem. Biophys. Res. Commun. 228:494-498(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=9020145; DOI=10.1074/jbc.272.7.4281;
Pendas A.M., Knaeuper V.V., Puente X.S., Llano E., Mattei M.-G.,
Apte S., Murphy G., Lopez-Otin C.;
"Identification and characterization of a novel human matrix
metalloproteinase with unique structural characteristics, chromosomal
location and tissue distribution.";
J. Biol. Chem. 272:4281-4286(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Rheumatoid arthritic synovial fluid;
PubMed=9232430; DOI=10.1016/S0165-2478(97)00057-6;
Kolb C., Mauch S., Peter H.-H., Krawinkel U., Sedlacek R.;
"The matrix metalloproteinase RASI-1 is expressed in synovial blood
vessels of a rheumatoid arthritis patient.";
Immunol. Lett. 57:83-88(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Rheumatoid arthritic synovial fluid;
PubMed=9562866;
Sedlacek R., Mauch S., Kolb B., Schaetzlein C., Eibel H., Peter H.-H.,
Schmitt J., Krawinkel U.;
"Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface
of activated peripheral blood mononuclear cells and is detected as an
autoantigen in rheumatoid arthritis.";
Immunobiology 198:408-423(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Mauch S., Sedlacek R., Krawinkel U., Schaetzlein C.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-103; THR-488 AND
MET-491.
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND MUTAGENESIS.
PubMed=10809722; DOI=10.1074/jbc.275.20.14809;
Stracke J.O., Hutton M., Stewart M., Pendas A.M., Smith B.,
Lopez-Otin C., Murphy G., Knaeuper V.;
"Biochemical characterization of the catalytic domain of human matrix
metalloproteinase 19. Evidence for a role as a potent basement
membrane degrading enzyme.";
J. Biol. Chem. 275:14809-14816(2000).
[11]
FUNCTION.
PubMed=10922468; DOI=10.1016/S0014-5793(00)01819-6;
Stracke J.O., Fosang A.J., Last K., Mercuri F.A., Pendas A.M.,
Llano E., Perris R., Di Cesare P.E., Murphy G., Knaeuper V.;
"Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage
oligomeric matrix protein (COMP).";
FEBS Lett. 478:52-56(2000).
[12]
PHOSPHORYLATION.
PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L.,
Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.;
"A secreted tyrosine kinase acts in the extracellular environment.";
Cell 158:1033-1044(2014).
[13]
INVOLVEMENT IN CODA.
PubMed=25581579; DOI=10.1002/humu.22754;
Hazlewood R.J., Roos B.R., Solivan-Timpe F., Honkanen R.A.,
Jampol L.M., Gieser S.C., Meyer K.J., Mullins R.F., Kuehn M.H.,
Scheetz T.E., Kwon Y.H., Alward W.L., Stone E.M., Fingert J.H.;
"Heterozygous triplication of upstream regulatory sequences leads to
dysregulation of matrix metalloproteinase 19 in patients with cavitary
optic disc anomaly.";
Hum. Mutat. 36:369-378(2015).
-!- 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. Hydrolyzes collagen type
IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I
gelatin. {ECO:0000269|PubMed:10809722,
ECO:0000269|PubMed:10922468}.
-!- 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};
-!- ENZYME REGULATION: Strongly inhibited by TIMP-2, TIMP-3 and TIMP-
4, while TIMP-1 is less efficient.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=RASI-1, RASI-11;
IsoId=Q99542-1; Sequence=Displayed;
Name=2; Synonyms=RASI-9;
IsoId=Q99542-3; Sequence=VSP_005457, VSP_005458;
Name=3; Synonyms=RASI-6;
IsoId=Q99542-4; Sequence=VSP_041893, VSP_041894;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q99542-5; Sequence=VSP_054573, VSP_054574, VSP_054575;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in mammary gland, placenta, lung,
pancreas, ovary, small intestine, spleen, thymus, prostate, testis
colon, heart and blood vessel walls. Not detected in brain and
peripheral blood leukocytes. Also expressed in the synovial fluid
of normal and rheumatoid patients (PubMed:8920941).
{ECO:0000269|PubMed:8920941}.
-!- 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: Activated by autolytic cleavage after Lys-97.
-!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000269|PubMed:25171405}.
-!- DISEASE: Cavitary optic disc anomalies (CODA) [MIM:611543]: An
ocular disease characterized by a profound excavation of the optic
nerve. Clinical phenotype is variable and includes congenitally
excavated optic nerves as well as other features of optic pit,
optic nerve coloboma, and morning glory disk anomaly. Patients
with CODA have a strong predilection for retinal detachment and/or
separation of the retinal layers (retinoschisis) that lead to
profound central vision loss. {ECO:0000269|PubMed:25581579}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Autoantigen anti-MMP19 are frequent in RA patients.
{ECO:0000269|PubMed:9562866}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC99995.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp19/";
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EMBL; Y08622; CAA69913.1; -; mRNA.
EMBL; X92521; CAA63299.1; -; mRNA.
EMBL; U37791; AAC51521.1; -; mRNA.
EMBL; U38321; AAB63008.1; -; mRNA.
EMBL; U38431; AAC99995.1; ALT_SEQ; mRNA.
EMBL; U38322; AAB63009.1; -; mRNA.
EMBL; AK303202; BAG64292.1; -; mRNA.
EMBL; AY706993; AAT97983.1; -; Genomic_DNA.
EMBL; AC023055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050368; AAH50368.1; -; mRNA.
CCDS; CCDS61146.1; -. [Q99542-5]
CCDS; CCDS8895.1; -. [Q99542-1]
PIR; JC5082; JC5082.
RefSeq; NP_001259030.1; NM_001272101.1. [Q99542-5]
RefSeq; NP_002420.1; NM_002429.5. [Q99542-1]
UniGene; Hs.591033; -.
ProteinModelPortal; Q99542; -.
BioGrid; 110470; 8.
IntAct; Q99542; 1.
STRING; 9606.ENSP00000313437; -.
BindingDB; Q99542; -.
ChEMBL; CHEMBL1938214; -.
DrugBank; DB00786; Marimastat.
MEROPS; M10.021; -.
iPTMnet; Q99542; -.
PhosphoSitePlus; Q99542; -.
DMDM; 12643345; -.
PaxDb; Q99542; -.
PeptideAtlas; Q99542; -.
PRIDE; Q99542; -.
ProteomicsDB; 78315; -.
ProteomicsDB; 78316; -. [Q99542-3]
ProteomicsDB; 78317; -. [Q99542-4]
DNASU; 4327; -.
Ensembl; ENST00000322569; ENSP00000313437; ENSG00000123342. [Q99542-1]
Ensembl; ENST00000409200; ENSP00000386625; ENSG00000123342. [Q99542-5]
Ensembl; ENST00000552872; ENSP00000446776; ENSG00000123342. [Q99542-4]
GeneID; 4327; -.
KEGG; hsa:4327; -.
UCSC; uc001sib.5; human. [Q99542-1]
CTD; 4327; -.
DisGeNET; 4327; -.
EuPathDB; HostDB:ENSG00000123342.15; -.
GeneCards; MMP19; -.
HGNC; HGNC:7165; MMP19.
HPA; HPA070804; -.
MalaCards; MMP19; -.
MIM; 601807; gene.
MIM; 611543; phenotype.
neXtProt; NX_Q99542; -.
OpenTargets; ENSG00000123342; -.
PharmGKB; PA30876; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00910000144034; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; Q99542; -.
KO; K07998; -.
OMA; WIHFFKG; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q99542; -.
TreeFam; TF315428; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
ChiTaRS; MMP19; human.
GeneWiki; MMP19; -.
GenomeRNAi; 4327; -.
PRO; PR:Q99542; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123342; -.
CleanEx; HS_MMP19; -.
ExpressionAtlas; Q99542; baseline and differential.
Genevisible; Q99542; HS.
GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0001554; P:luteolysis; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
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; IPR028724; MMP19.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF166; PTHR10201:SF166; 1.
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.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Calcium; Collagen degradation;
Complete proteome; Developmental protein; Differentiation;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 97 {ECO:0000269|PubMed:10809722}.
/FTId=PRO_0000028826.
CHAIN 98 508 Matrix metalloproteinase-19.
/FTId=PRO_0000028827.
REPEAT 286 333 Hemopexin 1.
REPEAT 334 380 Hemopexin 2.
REPEAT 381 425 Hemopexin 3.
REPEAT 426 472 Hemopexin 4.
MOTIF 83 90 Cysteine switch. {ECO:0000250}.
COMPBIAS 265 271 Poly-Glu.
ACT_SITE 213 213 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 85 85 Zinc; in inhibited form. {ECO:0000250}.
METAL 212 212 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 216 216 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 222 222 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 289 472 {ECO:0000250}.
VAR_SEQ 1 286 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_005457.
VAR_SEQ 58 63 RAFQEA -> SLRSAG (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_041893.
VAR_SEQ 64 508 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_041894.
VAR_SEQ 174 255 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054573.
VAR_SEQ 287 298 DPCSSELDAMML -> MGVTWDFSMSNG (in isoform
2). {ECO:0000303|Ref.5}.
/FTId=VSP_005458.
VAR_SEQ 300 387 PRGKTYAFKGDYVWTVSDSGPGPLFRVSALWEGLPGNLDAA
VYSPRTQWIHFFKGDKVWRYINFKMSPGFPKKLNRVEPNLD
AALYWP -> EAPPLQAVGRRWGQPADPEAWTNGSDMGLQH
EQWRAPWEDLCFQGGLCVDCIRFRTGPLVPSVCPLGGAPRK
PGCCCLLASNTMDSLL (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054574.
VAR_SEQ 388 508 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054575.
VARIANT 103 103 R -> C (in dbSNP:rs17844794).
{ECO:0000269|Ref.7}.
/FTId=VAR_021036.
VARIANT 245 245 P -> S (in dbSNP:rs1056784).
/FTId=VAR_054006.
VARIANT 488 488 P -> T (in dbSNP:rs17118042).
{ECO:0000269|Ref.7}.
/FTId=VAR_021037.
VARIANT 491 491 T -> M (in dbSNP:rs17844806).
{ECO:0000269|Ref.7}.
/FTId=VAR_021038.
MUTAGEN 88 88 E->P: Reduced autolysis rate.
{ECO:0000269|PubMed:10809722}.
MUTAGEN 90 90 P->V: Reduced autolysis rate.
{ECO:0000269|PubMed:10809722}.
CONFLICT 376 376 V -> S (in Ref. 1; CAA69913).
{ECO:0000305}.
SEQUENCE 508 AA; 57357 MW; BA480549AA9A8972 CRC64;
MNCQQLWLGF LLPMTVSGRV LGLAEVAPVD YLSQYGYLQK PLEGSNNFKP EDITEALRAF
QEASELPVSG QLDDATRARM RQPRCGLEDP FNQKTLKYLL LGRWRKKHLT FRILNLPSTL
PPHTARAALR QAFQDWSNVA PLTFQEVQAG AADIRLSFHG RQSSYCSNTF DGPGRVLAHA
DIPELGSVHF DEDEFWTEGT YRGVNLRIIA AHEVGHALGL GHSRYSQALM APVYEGYRPH
FKLHPDDVAG IQALYGKKSP VIRDEEEEET ELPTVPPVPT EPSPMPDPCS SELDAMMLGP
RGKTYAFKGD YVWTVSDSGP GPLFRVSALW EGLPGNLDAA VYSPRTQWIH FFKGDKVWRY
INFKMSPGFP KKLNRVEPNL DAALYWPLNQ KVFLFKGSGY WQWDELARTD FSSYPKPIKG
LFTGVPNQPS AAMSWQDGRV YFFKGKVYWR LNQQLRVEKG YPRNISHNWM HCRPRTIDTT
PSGGNTTPSG TGITLDTTLS ATETTFEY


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