ADAM9_MOUSE
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 03-AUG-2022, entry version 176.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 9;
DE Short=ADAM 9;
DE EC=3.4.24.-;
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, PHOSPHORYLATION, ACTIVITY REGULATION, AND PROTEIN SEQUENCE OF
RP 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: Cleaves and releases a number of molecules with important
CC roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40,
CC VCAM1 and CDH5 (PubMed:19273593). May mediate cell-cell, cell-matrix
CC interactions and regulate the motility of cells via interactions with
CC integrins (PubMed:10825303). {ECO:0000269|PubMed:10825303,
CC ECO:0000269|PubMed:19273593}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
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; 1.
DR IntAct; Q61072; 3.
DR STRING; 10090.ENSMUSP00000081048; -.
DR MEROPS; M12.209; -.
DR GlyConnect; 2260; 4 N-Linked glycans (1 site).
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; Q61072; -.
DR PRIDE; Q61072; -.
DR ProteomicsDB; 285760; -.
DR Antibodypedia; 1281; 354 antibodies from 34 providers.
DR DNASU; 11502; -.
DR Ensembl; ENSMUST00000084035; ENSMUSP00000081048; ENSMUSG00000031555.
DR GeneID; 11502; -.
DR KEGG; mmu:11502; -.
DR UCSC; uc009lfk.2; mouse.
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 PhylomeDB; Q61072; -.
DR TreeFam; TF314733; -.
DR BRENDA; 3.4.24.B9; 3474.
DR BioGRID-ORCS; 11502; 0 hits in 34 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 258 other tissues.
DR ExpressionAtlas; Q61072; baseline and differential.
DR Genevisible; Q61072; MM.
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:0005615; C:extracellular space; IMP:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IDA: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:0043406; P:positive regulation of MAP kinase activity; 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; -; 1.
DR Gene3D; 4.10.70.10; -; 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 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; SSF57552; 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.
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
