ID   ADAM9_MOUSE             Reviewed;         845 AA.
AC   Q61072; E9QPP2; Q60618; Q61853; Q80U94;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 183.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 9;
DE            Short=ADAM 9;
DE            EC=3.4.24.- {ECO:0000269|PubMed:9920899};
DE   AltName: Full=Meltrin-gamma;
DE   AltName: Full=Metalloprotease/disintegrin/cysteine-rich protein 9;
DE   AltName: Full=Myeloma cell metalloproteinase;
DE   Flags: Precursor;
GN   Name=Adam9 {ECO:0000312|MGI:MGI:105376};
GN   Synonyms=Kiaa0021 {ECO:0000312|EMBL:BAC65470.1}, Mdc9, Mltng;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=8647900; DOI=10.1083/jcb.132.4.717;
RA   Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P.;
RT   "MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3
RT   ligand domains.";
RL   J. Cell Biol. 132:717-726(1996).
RN   [2] {ECO:0000312|EMBL:BAC65470.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC65470.1};
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 426-575.
RX   PubMed=7566181; DOI=10.1038/377652a0;
RA   Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y.,
RA   Fujisawa-Sehara A.;
RT   "A metalloprotease-disintegrin participating in myoblast fusion.";
RL   Nature 377:652-656(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 432-478.
RC   STRAIN=BALB/cJ;
RX   PubMed=8146185; DOI=10.1073/pnas.91.7.2748;
RA   Weskamp G., Blobel C.P.;
RT   "A family of cellular proteins related to snake venom disintegrins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2748-2751(1994).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, ACTIVITY REGULATION, AND
RP   PROTEIN SEQUENCE OF 206-212.
RX   PubMed=9920899; DOI=10.1074/jbc.274.6.3531;
RA   Roghani M., Becherer J.D., Moss M.L., Atherton R.E., Erdjument-Bromage H.,
RA   Arribas J., Blackburn R.K., Weskamp G., Tempst P., Blobel C.P.;
RT   "Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic
RT   activity.";
RL   J. Biol. Chem. 274:3531-3540(1999).
RN   [8]
RP   INTERACTION WITH SH3GL2 AND SNX9.
RX   PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA   Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT   "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT   SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL   J. Biol. Chem. 274:31693-31699(1999).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH ITGA6.
RX   PubMed=10825303; DOI=10.1242/jcs.113.12.2319;
RA   Nath D., Slocombe P.M., Webster A., Stephens P.E., Docherty A.J.,
RA   Murphy G.;
RT   "Meltrin gamma(ADAM-9) mediates cellular adhesion through
RT   alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell
RT   motility.";
RL   J. Cell Sci. 113:2319-2328(2000).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11839819; DOI=10.1128/mcb.22.5.1537-1544.2002;
RA   Weskamp G., Cai H., Brodie T.A., Higashyama S., Manova K., Ludwig T.,
RA   Blobel C.P.;
RT   "Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident
RT   major abnormalities during development or adult life.";
RL   Mol. Cell. Biol. 22:1537-1544(2002).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19409519; DOI=10.1016/j.ajhg.2009.04.005;
RA   Parry D.A., Toomes C., Bida L., Danciger M., Towns K.V., McKibbin M.,
RA   Jacobson S.G., Logan C.V., Ali M., Bond J., Chance R., Swendeman S.,
RA   Daniele L.L., Springell K., Adams M., Johnson C.A., Booth A.P., Jafri H.,
RA   Rashid Y., Banin E., Strom T.M., Farber D.B., Sharon D., Blobel C.P.,
RA   Pugh E.N. Jr., Pierce E.A., Inglehearn C.F.;
RT   "Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans
RT   and retinal degeneration in mice.";
RL   Am. J. Hum. Genet. 84:683-691(2009).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF GLU-348.
RX   PubMed=19273593; DOI=10.1128/mcb.01460-08;
RA   Guaiquil V., Swendeman S., Yoshida T., Chavala S., Campochiaro P.A.,
RA   Blobel C.P.;
RT   "ADAM9 is involved in pathological retinal neovascularization.";
RL   Mol. Cell. Biol. 29:2694-2703(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [14]
RP   MUTAGENESIS OF ARG-53; ARG-56; ARG-202 AND ARG-205, SUBCELLULAR LOCATION,
RP   AND ACTIVITY REGULATION.
RX   PubMed=25795784; DOI=10.1074/jbc.m114.624072;
RA   Wong E., Maretzky T., Peleg Y., Blobel C.P., Sagi I.;
RT   "The functional maturation of a disintegrin and metalloproteinase (ADAM) 9,
RT   10, and 17 requires processing at a newly identified proprotein convertase
RT   (PC) cleavage site.";
RL   J. Biol. Chem. 290:12135-12146(2015).
CC   -!- FUNCTION: Metalloprotease that cleaves and releases a number of
CC       molecules with important roles in tumorigenesis and angiogenesis, such
CC       as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:9920899,
CC       PubMed:19273593). May mediate cell-cell, cell-matrix interactions and
CC       regulate the motility of cells via interactions with integrins
CC       (PubMed:10825303). {ECO:0000269|PubMed:10825303,
CC       ECO:0000269|PubMed:19273593, ECO:0000269|PubMed:9920899}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9BZ11};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9BZ11};
CC   -!- ACTIVITY REGULATION: Synthesized as an inactive form which is
CC       proteolytically cleaved to generate an active enzyme. Processing at the
CC       upstream site is particularly important for activation of the
CC       proenzyme, whereas processing at the boundary between the pro-domain
CC       and the catalytic domain does not appear to be essential
CC       (PubMed:25795784). Inhibited by hydroxamic acid-based inhibitors
CC       (PubMed:9920899). {ECO:0000269|PubMed:25795784,
CC       ECO:0000269|PubMed:9920899}.
CC   -!- SUBUNIT: Interacts with SH3GL2 and SNX9 through its cytoplasmic tail
CC       (PubMed:10531379). Interacts with ITGA6 (PubMed:10825303).
CC       {ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:10825303}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795784,
CC       ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC   -!- PTM: Proteolytically cleaved in the trans-Golgi network before it
CC       reaches the plasma membrane to generate a mature protein. The removal
CC       of the pro-domain occurs via cleavage at two different sites. Processed
CC       most likely by a pro-protein convertase such as furin, at the boundary
CC       between the pro-domain and the catalytic domain. An additional upstream
CC       cleavage pro-protein convertase site (Arg-56/Glu-57) has an important
CC       role in the activation of ADAM9. {ECO:0000269|PubMed:25795784,
CC       ECO:0000269|PubMed:9920899}.
CC   -!- PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-13-
CC       acetate (PMA) (PubMed:9920899). {ECO:0000269|PubMed:9920899}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice appear to develop normally, are
CC       viable and fertile, and do not have any major pathological phenotypes
CC       (PubMed:11839819). In adulthood, 20 months after birth, mice display
CC       progressive retinal degeneration, disorganized retinal layers and a
CC       degenerate retinal pigment epithelium (PubMed:19409519).
CC       {ECO:0000269|PubMed:11839819, ECO:0000269|PubMed:19409519}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65470.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U41765; AAC52446.1; -; mRNA.
DR   EMBL; AK122188; BAC65470.1; ALT_INIT; mRNA.
DR   EMBL; AC156553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047156; AAH47156.1; -; mRNA.
DR   EMBL; D50412; BAA08913.1; -; mRNA.
DR   EMBL; U06145; AAA18424.1; -; mRNA.
DR   PIR; I48943; I48943.
DR   PIR; S60259; S60259.
DR   RefSeq; NP_031430.2; NM_007404.2.
DR   AlphaFoldDB; Q61072; -.
DR   SMR; Q61072; -.
DR   BioGRID; 197973; 2.
DR   IntAct; Q61072; 3.
DR   STRING; 10090.ENSMUSP00000146545; -.
DR   MEROPS; M12.209; -.
DR   GlyConnect; 2260; 4 N-Linked glycans (1 site).
DR   GlyCosmos; Q61072; 6 sites, 4 glycans.
DR   GlyGen; Q61072; 6 sites, 4 N-linked glycans (1 site).
DR   iPTMnet; Q61072; -.
DR   PhosphoSitePlus; Q61072; -.
DR   CPTAC; non-CPTAC-3443; -.
DR   EPD; Q61072; -.
DR   MaxQB; Q61072; -.
DR   PaxDb; 10090-ENSMUSP00000081048; -.
DR   ProteomicsDB; 285760; -.
DR   Pumba; Q61072; -.
DR   Antibodypedia; 1281; 404 antibodies from 35 providers.
DR   DNASU; 11502; -.
DR   Ensembl; ENSMUST00000084035.12; ENSMUSP00000081048.6; ENSMUSG00000031555.16.
DR   GeneID; 11502; -.
DR   KEGG; mmu:11502; -.
DR   UCSC; uc009lfk.2; mouse.
DR   AGR; MGI:105376; -.
DR   CTD; 8754; -.
DR   MGI; MGI:105376; Adam9.
DR   VEuPathDB; HostDB:ENSMUSG00000031555; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000156239; -.
DR   HOGENOM; CLU_012714_4_1_1; -.
DR   InParanoid; Q61072; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q61072; -.
DR   TreeFam; TF314733; -.
DR   BRENDA; 3.4.24.B9; 3474.
DR   BioGRID-ORCS; 11502; 0 hits in 39 CRISPR screens.
DR   ChiTaRS; Adam9; mouse.
DR   PRO; PR:Q61072; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q61072; Protein.
DR   Bgee; ENSMUSG00000031555; Expressed in endothelial cell of lymphatic vessel and 262 other cell types or tissues.
DR   ExpressionAtlas; Q61072; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IMP:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0043236; F:laminin binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:1902945; F:metalloendopeptidase activity involved in amyloid precursor protein catabolic process; ISO:MGI.
DR   GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:BHF-UCL.
DR   GO; GO:0042987; P:amyloid precursor protein catabolic process; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR   GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR   GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISO:MGI.
DR   GO; GO:0042117; P:monocyte activation; ISO:MGI.
DR   GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:MGI.
DR   GO; GO:0034241; P:positive regulation of macrophage fusion; ISO:MGI.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0016485; P:protein processing; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR   GO; GO:0051384; P:response to glucocorticoid; IMP:BHF-UCL.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR   GO; GO:0010042; P:response to manganese ion; ISO:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF136; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q61072; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..845
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 9"
FT                   /id="PRO_0000029063"
FT   TOPO_DOM        30..697
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        698..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        719..845
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          212..406
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          414..501
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          644..698
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          729..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..798
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000250|UniProtKB:P78536,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT                   ProRule:PRU10095"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   SITE            56..57
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305|PubMed:25795784"
FT   SITE            205..206
FT                   /note="Cleavage; by furin-like protease"
FT                   /evidence="ECO:0000269|PubMed:9920899"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        636
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        322..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        363..385
FT                   /evidence="ECO:0000250|UniProtKB:P78536"
FT   DISULFID        365..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        473..493
FT                   /evidence="ECO:0000250"
FT   DISULFID        644..656
FT                   /evidence="ECO:0000250"
FT   DISULFID        650..662
FT                   /evidence="ECO:0000250"
FT   DISULFID        664..673
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         53
FT                   /note="R->A: Reduces the shedding activity; when associated
FT                   with A-56. Does not prevent pro-domain processing between
FT                   the pro- and metalloprotease domain; when associated with
FT                   A-56."
FT                   /evidence="ECO:0000269|PubMed:25795784"
FT   MUTAGEN         56
FT                   /note="R->A: Reduces the shedding activity; when associated
FT                   with A-56. Does not prevent pro-domain processing between
FT                   the pro- and metalloprotease domain; when associated with
FT                   A-56."
FT                   /evidence="ECO:0000269|PubMed:25795784"
FT   MUTAGEN         202
FT                   /note="R->A: Does not affect shedding activity; when
FT                   associated with A-205."
FT                   /evidence="ECO:0000269|PubMed:25795784"
FT   MUTAGEN         205
FT                   /note="R->A: Does not affect shedding activity; when
FT                   associated with A-203."
FT                   /evidence="ECO:0000269|PubMed:25795784"
FT   MUTAGEN         348
FT                   /note="E->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19273593"
FT   CONFLICT        296
FT                   /note="W -> R (in Ref. 1; AAC52446, 2; BAC65470 and 4;
FT                   AAH47156)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   845 AA;  92079 MW;  38C40F89D4A77725 CRC64;
     MGPRALSPLA SLRLRWLLAC GLLGPVLEAG RPDLEQTVHL SSYEIITPWR LTRERREALG
     PSSQQISYVI QAQGKQHIIH LERNTDLLPN DFVVYTYDKE GSLLSDHPNV QSHCHYRGYV
     EGVQNSAVAV SACFGLRGLL HLENASFGIE PLHNSSHFEH IFYPMDGIHQ EPLRCGVSNR
     DTEKEGTQGD EEEHPSVTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
     RLANYLDSMY IMLNIRIVLV GLEIWTDRNP INIIGGAGDV LGNFVQWREK FLITRWRHDS
     AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
     RECFCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGS CLLNIPKPDE AYSAPSCGNK
     LVDPGEECDC GTAKECEVDP CCEGSTCKLK SFAECAYGDC CKDCQFLPGG SMCRGKTSEC
     DVPEYCNGSS QFCPPDVFIQ NGYPCQNSKA YCYNGMCQYY DAQCQVIFGS KAKAAPRDCF
     IEVNSKGDRF GNCGFSGSEY KKCATGNALC GKLQCENVQD MPVFGIVPAI IQTPSRGTKC
     WGVDFQLGSD VPDPGMVNEG TKCDAGKICR NFQCVNASVL NYDCDIQGKC HGHGVCNSNK
     NCHCEDGWAP PHCDTKGYGG SVDSGPTYNA KSTALRDGLL VFFFLIVPLV AAAIFLFIKR
     DELRKTFRKK RSQMSDGRNQ ANVSRQPGDP SISRPPGGPN VSRPPGGPGV SRPPGGPGVS
     RPPGGPGVSR PPPGHGNRFP VPTYAAKQPA QFPSRPPPPQ PKISSQGNLI PARPAPAPPL
     YSSLT
//