AL1A1_SHEEP
ID AL1A1_SHEEP Reviewed; 501 AA.
AC P51977;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Aldehyde dehydrogenase 1A1 {ECO:0000305|PubMed:26373694};
DE EC=1.2.1.19 {ECO:0000250|UniProtKB:P24549};
DE EC=1.2.1.28 {ECO:0000250|UniProtKB:P00352};
DE EC=1.2.1.3 {ECO:0000269|PubMed:26373694};
DE EC=1.2.1.36 {ECO:0000250|UniProtKB:P51647};
DE AltName: Full=3-deoxyglucosone dehydrogenase {ECO:0000250|UniProtKB:P00352};
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A1 {ECO:0000303|PubMed:9862807};
DE AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000303|PubMed:7484410};
DE AltName: Full=Retinal dehydrogenase 1 {ECO:0000305};
DE Short=RALDH 1 {ECO:0000305};
DE Short=RalDH1 {ECO:0000305};
GN Name=ALDH1A1 {ECO:0000303|PubMed:9862807};
GN Synonyms=ALDH1 {ECO:0000303|PubMed:9862807};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7484410; DOI=10.1007/978-1-4615-1965-2_8;
RA Stayner C.K., Tweedie J.W.;
RT "Cloning and characterisation of the cDNA for sheep liver cytosolic
RT aldehyde dehydrogenase.";
RL Adv. Exp. Med. Biol. 372:61-66(1995).
RN [2] {ECO:0007744|PDB:1BXS}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT, AND
RP ACTIVE SITE.
RX PubMed=9862807; DOI=10.1016/s0969-2126(98)00152-x;
RA Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M., Baker E.N.;
RT "Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the
RT basis for the retinal specificity of class 1 aldehyde dehydrogenases.";
RL Structure 6:1541-1551(1998).
RN [3] {ECO:0007744|PDB:5ABM, ECO:0007744|PDB:5AC0, ECO:0007744|PDB:5AC1}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-501 IN COMPLEX WITH DUOCARMYCIN
RP ANALOG AND NAD, SUBUNIT, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=26373694; DOI=10.1002/anie.201505749;
RA Koch M.F., Harteis S., Blank I.D., Pestel G., Tietze L.F., Ochsenfeld C.,
RA Schneider S., Sieber S.A.;
RT "Structural, biochemical, and computational studies reveal the mechanism of
RT selective aldehyde dehydrogenase 1A1 inhibition by cytotoxic duocarmycin
RT analogues.";
RL Angew. Chem. Int. Ed. Engl. 54:13550-13554(2015).
CC -!- FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible
CC oxidation of a wide range of aldehydes to their corresponding
CC carboxylic acid (PubMed:26373694). Functions downstream of retinol
CC dehydrogenases and catalyzes the oxidation of retinaldehyde into
CC retinoic acid, the second step in the oxidation of retinol/vitamin A
CC into retinoic acid. This pathway is crucial to control the levels of
CC retinol and retinoic acid, two important molecules which excess can be
CC teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes
CC resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE,
CC malonaldehyde and hexanal that form protein adducts and are highly
CC cytotoxic. By participating for instance to the clearance of (E)-4-
CC hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of
CC HNE-protein adducts and lens opacification. Functions also downstream
CC of fructosamine-3-kinase in the fructosamine degradation pathway by
CC catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product
CC of fructosamine 3-phosphate decomposition, which is itself a potent
CC glycating agent that may react with lysine and arginine side-chains of
CC proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase
CC activity and is probably part of an alternative pathway for the
CC biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a
CC role in GABAergic synaptic transmission (By similarity).
CC {ECO:0000250|UniProtKB:P00352, ECO:0000250|UniProtKB:P24549,
CC ECO:0000269|PubMed:26373694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000269|PubMed:26373694};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000305|PubMed:26373694};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:42084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78273,
CC ChEBI:CHEBI:78630; Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:47132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16066, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:87435; Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47133;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:169952; Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67333;
CC Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-
CC gluconate + 2 H(+) + NADH; Xref=Rhea:RHEA:67244, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:57990, ChEBI:CHEBI:60777;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67245;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:566274; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:26373694};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257;
CC Evidence={ECO:0000305|PubMed:26373694};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC -!- ACTIVITY REGULATION: Inhibited by duocarmycin analogs.
CC {ECO:0000269|PubMed:26373694}.
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:P51647}.
CC -!- SUBUNIT: Homotetramer (PubMed:26373694, PubMed:9862807). Interacts with
CC PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde
CC dehydrogenase activity and is independent of the methyltransferase
CC activity of PRMT3 (By similarity). {ECO:0000250|UniProtKB:P00352,
CC ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P00352}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P24549}.
CC -!- PTM: The N-terminus is blocked most probably by acetylation.
CC {ECO:0000250|UniProtKB:P15437}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U12761; AAA85435.1; -; mRNA.
DR PIR; S78582; S14752.
DR RefSeq; NP_001009778.1; NM_001009778.1.
DR PDB; 1BXS; X-ray; 2.35 A; A/B/C/D=1-501.
DR PDB; 5ABM; X-ray; 1.70 A; A/B/C/D=2-501.
DR PDB; 5AC0; X-ray; 1.90 A; A/B=1-501.
DR PDB; 5AC1; X-ray; 2.08 A; A/B/C/D=1-501.
DR PDBsum; 1BXS; -.
DR PDBsum; 5ABM; -.
DR PDBsum; 5AC0; -.
DR PDBsum; 5AC1; -.
DR AlphaFoldDB; P51977; -.
DR SMR; P51977; -.
DR STRING; 9940.ENSOARP00000013613; -.
DR PRIDE; P51977; -.
DR Ensembl; ENSOART00000013815; ENSOARP00000013613; ENSOARG00000012705.
DR GeneID; 443343; -.
DR KEGG; oas:443343; -.
DR CTD; 216; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR OMA; GDHTSYV; -.
DR OrthoDB; 153834at2759; -.
DR UniPathway; UPA00912; -.
DR EvolutionaryTrace; P51977; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000012705; Expressed in adrenal cortex and 52 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; ISS:UniProtKB.
DR GO; GO:0030392; P:fructosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Cytoplasm; Lipid metabolism;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15437"
FT CHAIN 2..501
FT /note="Aldehyde dehydrogenase 1A1"
FT /id="PRO_0000056420"
FT REGION 336..501
FT /note="Mediates interaction with PRMT3"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000303|PubMed:9862807"
FT BINDING 167..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS,
FT ECO:0007744|PDB:5AC0"
FT BINDING 193..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS,
FT ECO:0007744|PDB:5AC0"
FT BINDING 226..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS,
FT ECO:0007744|PDB:5AC0"
FT BINDING 246..247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS,
FT ECO:0007744|PDB:5AC0"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0007744|PDB:5AC0"
FT BINDING 349..353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS,
FT ECO:0007744|PDB:5AC0"
FT BINDING 400..402
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26373694,
FT ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS,
FT ECO:0007744|PDB:5AC0"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P15437"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 495
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5ABM"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1BXS"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:5ABM"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 348..364
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5ABM"
FT HELIX 479..484
FT /evidence="ECO:0007829|PDB:5ABM"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:5ABM"
SQ SEQUENCE 501 AA; 54825 MW; 58B897197D621AB1 CRC64;
MSSSAMPDVP APLTNLQFKY TKIFINNEWH SSVSGKKFPV FNPATEEKLC EVEEGDKEDV
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLIERDR LLLATMEAMN GGKLFSNAYL
MDLGGCIKTL RYCAGWADKI QGRTIPMDGN FFTYTRSEPV GVCGQIIPWN FPLLMFLWKI
GPALSCGNTV VVKPAEQTPL TALHMGSLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
KVAFTGSTEV GKLIKEAAGK SNLKRVSLEL GGKSPCIVFA DADLDNAVEF AHQGVFYHQG
QCCIAASRLF VEESIYDEFV RRSVERAKKY VLGNPLTPGV SQGPQIDKEQ YEKILDLIES
GKKEGAKLEC GGGPWGNKGY FIQPTVFSDV TDDMRIAKEE IFGPVQQIMK FKSLDDVIKR
ANNTFYGLSA GIFTNDIDKA ITVSSALQSG TVWVNCYSVV SAQCPFGGFK MSGNGRELGE
YGFHEYTEVK TVTIKISQKN S
