ADA_BOVIN
ID ADA_BOVIN Reviewed; 363 AA.
AC P56658; Q9MYY1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Adenosine deaminase;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P00813};
DE AltName: Full=Adenosine aminohydrolase;
GN Name=ADA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11067872; DOI=10.1084/jem.192.9.1223;
RA Richard E., Arredondo-Vega F.X., Santisteban I., Kelly S.J., Patel D.D.,
RA Hershfield M.S.;
RT "The binding site of human adenosine deaminase for CD26/dipeptidyl
RT peptidase IV: the Arg142Gln mutation impairs binding to CD26 but does not
RT cause immune deficiency.";
RL J. Exp. Med. 192:1223-1236(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-357, AND MASS SPECTROMETRY.
RX PubMed=8877857; DOI=10.1016/0731-7085(96)01845-6;
RA Kelly M.A., Vestling M.M., Murphy C.M., Hua S., Sumpter T., Fenselau C.;
RT "Primary structure of bovine adenosine deaminase.";
RL J. Pharm. Biomed. Anal. 14:1513-1519(1996).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23240012; DOI=10.1371/journal.pone.0051287;
RA Casanova V., Naval-Macabuhay I., Massanella M., Rodriguez-Garcia M.,
RA Blanco J., Gatell J.M., Garcia F., Gallart T., Lluis C., Mallol J.,
RA Franco R., Climent N., McCormick P.J.;
RT "Adenosine deaminase enhances the immunogenicity of human dendritic cells
RT from healthy and HIV-infected individuals.";
RL PLoS ONE 7:E51287-E51287(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-356 IN COMPLEX WITH ZINC IONS
RP AND TRANSITION STATE ANALOG 6-HYDROXY-1,6-DIHYDROPURINE RIBOSIDE.
RX PubMed=12554940; DOI=10.1107/s090744490202190x;
RA Kinoshita T., Nishio N., Nakanishi I., Sato A., Fujii T.;
RT "Structure of bovine adenosine deaminase complexed with 6-hydroxy-1,6-
RT dihydropurine riboside.";
RL Acta Crystallogr. D 59:299-303(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR
RP AND ZINC IONS.
RX PubMed=14709046; DOI=10.1021/ja038606l;
RA Terasaka T., Kinoshita T., Kuno M., Nakanishi I.;
RT "A highly potent non-nucleoside adenosine deaminase inhibitor: efficient
RT drug discovery by intentional lead hybridization.";
RL J. Am. Chem. Soc. 126:34-35(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-357 IN COMPLEX WITH ZINC IONS
RP AND DPP4, AND SUBUNIT.
RX PubMed=15213224; DOI=10.1074/jbc.m405001200;
RA Weihofen W.A., Liu J., Reutter W., Saenger W., Fan H.;
RT "Crystal structure of CD26/dipeptidyl-peptidase IV in complex with
RT adenosine deaminase reveals a highly amphiphilic interface.";
RL J. Biol. Chem. 279:43330-43335(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR.
RX PubMed=15139750; DOI=10.1021/jm0499559;
RA Terasaka T., Okumura H., Tsuji K., Kato T., Nakanishi I., Kinoshita T.,
RA Kato Y., Kuno M., Seki N., Naoe Y., Inoue T., Tanaka K., Nakamura K.;
RT "Structure-based design and synthesis of non-nucleoside, potent, and orally
RT bioavailable adenosine deaminase inhibitors.";
RL J. Med. Chem. 47:2728-2731(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR.
RX PubMed=15239652; DOI=10.1021/jm0306374;
RA Terasaka T., Kinoshita T., Kuno M., Seki N., Tanaka K., Nakanishi I.;
RT "Structure-based design, synthesis, and structure-activity relationship
RT studies of novel non-nucleoside adenosine deaminase inhibitors.";
RL J. Med. Chem. 47:3730-3743(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR.
RX PubMed=16060665; DOI=10.1021/bi050529e;
RA Kinoshita T., Nakanishi I., Terasaka T., Kuno M., Seki N., Warizaya M.,
RA Matsumura H., Inoue T., Takano K., Adachi H., Mori Y., Fujii T.;
RT "Structural basis of compound recognition by adenosine deaminase.";
RL Biochemistry 44:10562-10569(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 2-362 IN COMPLEX WITH DPP4 AND A
RP HIV-1 TAT PEPTIDE.
RX PubMed=15695814; DOI=10.1074/jbc.m413400200;
RA Weihofen W.A., Liu J., Reutter W., Saenger W., Fan H.;
RT "Crystal structures of HIV-1 Tat-derived nonapeptides Tat-(1-9) and Trp2-
RT Tat-(1-9) bound to the active site of dipeptidyl-peptidase IV (CD26).";
RL J. Biol. Chem. 280:14911-14917(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR
RP AND ZINC IONS.
RX PubMed=16033254; DOI=10.1021/jm050413g;
RA Terasaka T., Tsuji K., Kato T., Nakanishi I., Kinoshita T., Kato Y.,
RA Kuno M., Inoue T., Tanaka K., Nakamura K.;
RT "Rational design of non-nucleoside, potent, and orally bioavailable
RT adenosine deaminase inhibitors: predicting enzyme conformational change and
RT metabolism.";
RL J. Med. Chem. 48:4750-4753(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 2-357 IN COMPLEX WITH EHNA.
RX PubMed=18549808; DOI=10.1016/j.bbrc.2008.05.180;
RA Kinoshita T., Tada T., Nakanishi I.;
RT "Conformational change of adenosine deaminase during ligand-exchange in a
RT crystal.";
RL Biochem. Biophys. Res. Commun. 373:53-57(2008).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine (By similarity). Plays an important role in purine
CC metabolism and in adenosine homeostasis (By similarity). Modulates
CC signaling by extracellular adenosine, and so contributes indirectly to
CC cellular signaling events (By similarity). Acts as a positive regulator
CC of T-cell coactivation, by binding DPP4 (By similarity). Its
CC interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By
CC similarity). Enhances dendritic cell immunogenicity by affecting
CC dendritic cell costimulatory molecule expression and cytokines and
CC chemokines secretion (PubMed:23240012). Enhances CD4+ T-cell
CC differentiation and proliferation (By similarity). Acts as a positive
CC modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their
CC ligand affinity via conformational change (By similarity). Stimulates
CC plasminogen activation (By similarity). Plays a role in male fertility
CC (By similarity). Plays a protective role in early postimplantation
CC embryonic development (By similarity). {ECO:0000250|UniProtKB:P00813,
CC ECO:0000250|UniProtKB:P03958, ECO:0000269|PubMed:23240012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000250|UniProtKB:P00813};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046,
CC ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:16033254};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12554940};
CC -!- SUBUNIT: Interacts with DPP4 (via extracellular domain). Interacts with
CC PLG (via Kringle 4 domain); the interaction stimulates PLG activation
CC when in complex with DPP4. {ECO:0000250|UniProtKB:P00813}.
CC -!- INTERACTION:
CC P56658; P27487: DPP4; Xeno; NbExp=5; IntAct=EBI-7475530, EBI-2871277;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction
CC {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen
CC {ECO:0000250|UniProtKB:P03958}. Cytoplasm {ECO:0000250}. Lysosome
CC {ECO:0000250|UniProtKB:P00813}. Note=Colocalized with DPP4 at the cell
CC surface. {ECO:0000250|UniProtKB:P00813}.
CC -!- TISSUE SPECIFICITY: Expressed in gastrointestinal tissues (at protein
CC level). {ECO:0000269|PubMed:23240012}.
CC -!- MASS SPECTROMETRY: Mass=40549; Mass_error=16; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8877857};
CC -!- PHARMACEUTICAL: Available under the name Adagen (Enzon). This is a PEG-
CC conjugated form (pegademase). Used to treat patients with severe
CC combined immunodeficiency diseases (SCID).
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/ADA/";
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DR EMBL; AF280603; AAF91430.1; -; mRNA.
DR RefSeq; NP_776312.1; NM_173887.2.
DR PDB; 1KRM; X-ray; 2.50 A; A=2-357.
DR PDB; 1NDV; X-ray; 2.30 A; A=2-357.
DR PDB; 1NDW; X-ray; 2.00 A; A=2-357.
DR PDB; 1NDY; X-ray; 2.00 A; A=2-357.
DR PDB; 1NDZ; X-ray; 2.00 A; A=2-357.
DR PDB; 1O5R; X-ray; 2.35 A; A=2-357.
DR PDB; 1QXL; X-ray; 2.25 A; A=2-357.
DR PDB; 1UML; X-ray; 2.50 A; A=2-357.
DR PDB; 1V79; X-ray; 2.50 A; A=2-357.
DR PDB; 1V7A; X-ray; 2.50 A; A=2-357.
DR PDB; 1VFL; X-ray; 1.80 A; A=2-357.
DR PDB; 1W1I; X-ray; 3.03 A; E/F/G/H=1-357.
DR PDB; 1WXY; X-ray; 2.50 A; A=2-357.
DR PDB; 1WXZ; X-ray; 2.80 A; A=2-357.
DR PDB; 2BGN; X-ray; 3.15 A; E/F/G/H=2-363.
DR PDB; 2E1W; X-ray; 2.50 A; A=2-357.
DR PDB; 2Z7G; X-ray; 2.52 A; A=2-357.
DR PDBsum; 1KRM; -.
DR PDBsum; 1NDV; -.
DR PDBsum; 1NDW; -.
DR PDBsum; 1NDY; -.
DR PDBsum; 1NDZ; -.
DR PDBsum; 1O5R; -.
DR PDBsum; 1QXL; -.
DR PDBsum; 1UML; -.
DR PDBsum; 1V79; -.
DR PDBsum; 1V7A; -.
DR PDBsum; 1VFL; -.
DR PDBsum; 1W1I; -.
DR PDBsum; 1WXY; -.
DR PDBsum; 1WXZ; -.
DR PDBsum; 2BGN; -.
DR PDBsum; 2E1W; -.
DR PDBsum; 2Z7G; -.
DR AlphaFoldDB; P56658; -.
DR SMR; P56658; -.
DR IntAct; P56658; 1.
DR MINT; P56658; -.
DR STRING; 9913.ENSBTAP00000006947; -.
DR BindingDB; P56658; -.
DR ChEMBL; CHEMBL2966; -.
DR DrugCentral; P56658; -.
DR PaxDb; P56658; -.
DR PeptideAtlas; P56658; -.
DR PRIDE; P56658; -.
DR GeneID; 280712; -.
DR KEGG; bta:280712; -.
DR CTD; 100; -.
DR eggNOG; KOG1097; Eukaryota.
DR InParanoid; P56658; -.
DR OrthoDB; 1045809at2759; -.
DR BRENDA; 3.5.4.4; 908.
DR EvolutionaryTrace; P56658; -.
DR PRO; PR:P56658; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004000; F:adenosine deaminase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006154; P:adenosine catabolic process; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0060169; P:negative regulation of adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_00540; A_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR028893; A_deaminase.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell adhesion; Cell junction; Cell membrane;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Hydrolase;
KW Lysosome; Membrane; Metal-binding; Nucleotide metabolism; Pharmaceutical;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00813,
FT ECO:0000269|PubMed:8877857"
FT CHAIN 2..363
FT /note="Adenosine deaminase"
FT /id="PRO_0000194351"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652,
FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808,
FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV,
FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY,
FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R,
FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW,
FT ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ,
FT ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652,
FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808,
FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV,
FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY,
FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R,
FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808,
FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY,
FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R,
FT ECO:0007744|PDB:1QXL"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14709046,
FT ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY,
FT ECO:0007744|PDB:1WXY"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652,
FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808,
FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV,
FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY,
FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R,
FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652,
FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808,
FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV,
FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY,
FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R,
FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12554940,
FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750,
FT ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254,
FT ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW,
FT ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ,
FT ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL"
FT SITE 58
FT /note="Important for interaction with adenosine receptors
FT and increasing their affinity for agonists"
FT /evidence="ECO:0000250|UniProtKB:P00813"
FT SITE 62
FT /note="Important for interaction with adenosine receptors
FT and increasing their affinity for agonists"
FT /evidence="ECO:0000250|UniProtKB:P00813"
FT SITE 238
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00813"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00813"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00813"
FT VARIANT 199
FT /note="K -> Q"
FT VARIANT 246
FT /note="A -> T"
FT VARIANT 352
FT /note="G -> R"
FT CONFLICT 8
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..33
FT /note="RK -> KR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="E -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..79
FT /note="EAV -> DAI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="V -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..281
FT /note="PVV -> AVI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..314
FT /note="NE -> KD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1NDY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:1VFL"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:1VFL"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:1VFL"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1QXL"
FT HELIX 337..351
FT /evidence="ECO:0007829|PDB:1VFL"
SQ SEQUENCE 363 AA; 40919 MW; 69F6D25ACFF2A3E5 CRC64;
MAQTPAFNKP KVELHVHLDG AIKPETILYY GRKRGIALPA DTPEELQNII GMDKPLSLPE
FLAKFDYYMP AIAGCREAVK RIAYEFVEMK AKDGVVYVEV RYSPHLLANS KVEPIPWNQA
EGDLTPDEVV SLVNQGLQEG ERDFGVKVRS ILCCMRHQPS WSSEVVELCK KYREQTVVAI
DLAGDETIEG SSLFPGHVKA YAEAVKSGVH RTVHAGEVGS ANVVKEAVDT LKTERLGHGY
HTLEDATLYN RLRQENMHFE VCPWSSYLTG AWKPDTEHPV VRFKNDQVNY SLNTDDPLIF
KSTLDTDYQM TKNEMGFTEE EFKRLNINAA KSSFLPEDEK KELLDLLYKA YGMPSPASAE
QCL
