ADH4_MOUSE
ID ADH4_MOUSE Reviewed; 377 AA.
AC Q9QYY9; Q3V0P5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH4 {ECO:0000305};
DE EC=1.1.1.105 {ECO:0000250|UniProtKB:P08319};
DE AltName: Full=ADH2;
DE AltName: Full=Alcohol dehydrogenase 4;
DE AltName: Full=Alcohol dehydrogenase class II;
DE Short=Alcohol dehydrogenase II;
GN Name=Adh4 {ECO:0000312|MGI:MGI:1349472};
GN Synonyms=Adh2 {ECO:0000303|PubMed:10514444};
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], ZINC-BINDING, MUTAGENESIS OF PRO-48; ASN-52 AND
RP SER-183, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC TISSUE=Liver;
RX PubMed=10514444; DOI=10.1074/jbc.274.42.29712;
RA Svensson S., Stroemberg P., Hoeoeg J.-O.;
RT "A novel subtype of class II alcohol dehydrogenase in rodents. Unique
RT Pro(47) and Ser(182) modulates hydride transfer in the mouse enzyme.";
RL J. Biol. Chem. 274:29712-29719(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=16081420; DOI=10.1074/jbc.m504055200;
RA Collins X.H., Harmon S.D., Kaduce T.L., Berst K.B., Fang X., Moore S.A.,
RA Raju T.V., Falck J.R., Weintraub N.L., Duester G., Plapp B.V.,
RA Spector A.A.;
RT "Omega-oxidation of 20-hydroxyeicosatetraenoic acid (20-HETE) in cerebral
RT microvascular smooth muscle and endothelium by alcohol dehydrogenase 4.";
RL J. Biol. Chem. 280:33157-33164(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH NADH AND
RP INHIBITOR AND OF MUTANT HIS-48 IN COMPLEX WITH NADH.
RX PubMed=10970744; DOI=10.1006/jmbi.2000.4039;
RA Svensson S., Hoeoeg J.-O., Schneider G., Sandalova T.;
RT "Crystal structures of mouse class II alcohol dehydrogenase reveal
RT determinants of substrate specificity and catalytic efficiency.";
RL J. Mol. Biol. 302:441-453(2000).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of either all-trans-
CC retinol or 9-cis-retinol (By similarity). Also oxidizes long chain
CC omega-hydroxy fatty acids, such as 20-HETE, producing both the
CC intermediate aldehyde, 20-oxoarachidonate and the end product, a
CC dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate
CC (PubMed:16081420). Also catalyzes the reduction of benzoquinones (By
CC similarity). {ECO:0000250|UniProtKB:P08319,
CC ECO:0000269|PubMed:16081420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:P08319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20-
CC oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645;
CC Evidence={ECO:0000269|PubMed:16081420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800;
CC Evidence={ECO:0000269|PubMed:16081420};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) =
CC (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645,
CC ChEBI:CHEBI:76647; Evidence={ECO:0000269|PubMed:16081420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804;
CC Evidence={ECO:0000269|PubMed:16081420};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42053;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-benzoquinone + H(+) + NADH = hydroquinone + NAD(+);
CC Xref=Rhea:RHEA:60660, ChEBI:CHEBI:15378, ChEBI:CHEBI:16509,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60661;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- ACTIVITY REGULATION: Oxidation of 20-HETE is inhibited by low
CC concentrations of N-heptylformamide (PubMed:16081420). Oxidation of 20-
CC HETE is a decreased by 55-65% by either all-trans-retinol or all-trans-
CC retinoic acid (PubMed:16081420). Strongly inhibited by omega-hydroxy
CC fatty acids (PubMed:10514444). {ECO:0000269|PubMed:10514444,
CC ECO:0000269|PubMed:16081420}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for 20-HETE {ECO:0000269|PubMed:16081420};
CC KM=0.24 mM for 1,4-benzoquinone {ECO:0000269|PubMed:10514444};
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:10970744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:10514444}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-II subfamily. {ECO:0000305}.
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DR EMBL; AJ245750; CAB57455.1; -; mRNA.
DR EMBL; AK132994; BAE21459.1; -; mRNA.
DR CCDS; CCDS38653.1; -.
DR RefSeq; NP_036126.2; NM_011996.2.
DR PDB; 1E3E; X-ray; 2.12 A; A/B=2-377.
DR PDB; 1E3I; X-ray; 2.08 A; A/B=2-377.
DR PDB; 1E3L; X-ray; 2.50 A; A/B=2-377.
DR PDBsum; 1E3E; -.
DR PDBsum; 1E3I; -.
DR PDBsum; 1E3L; -.
DR AlphaFoldDB; Q9QYY9; -.
DR SMR; Q9QYY9; -.
DR BioGRID; 205034; 1.
DR STRING; 10090.ENSMUSP00000013458; -.
DR SwissLipids; SLP:000000496; -.
DR iPTMnet; Q9QYY9; -.
DR PhosphoSitePlus; Q9QYY9; -.
DR SwissPalm; Q9QYY9; -.
DR jPOST; Q9QYY9; -.
DR MaxQB; Q9QYY9; -.
DR PaxDb; Q9QYY9; -.
DR PRIDE; Q9QYY9; -.
DR ProteomicsDB; 285618; -.
DR Antibodypedia; 14813; 281 antibodies from 30 providers.
DR DNASU; 26876; -.
DR Ensembl; ENSMUST00000013458; ENSMUSP00000013458; ENSMUSG00000037797.
DR GeneID; 26876; -.
DR KEGG; mmu:26876; -.
DR UCSC; uc008rnj.1; mouse.
DR CTD; 127; -.
DR MGI; MGI:1349472; Adh4.
DR VEuPathDB; HostDB:ENSMUSG00000037797; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000162645; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q9QYY9; -.
DR OMA; NGTCFGG; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; Q9QYY9; -.
DR TreeFam; TF300429; -.
DR BRENDA; 1.1.1.1; 3474.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR Reactome; R-MMU-71384; Ethanol oxidation.
DR SABIO-RK; Q9QYY9; -.
DR BioGRID-ORCS; 26876; 3 hits in 73 CRISPR screens.
DR EvolutionaryTrace; Q9QYY9; -.
DR PRO; PR:Q9QYY9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9QYY9; protein.
DR Bgee; ENSMUSG00000037797; Expressed in left lobe of liver and 49 other tissues.
DR ExpressionAtlas; Q9QYY9; baseline and differential.
DR Genevisible; Q9QYY9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:MGI.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI.
DR GO; GO:0005503; F:all-trans retinal binding; ISO:MGI.
DR GO; GO:0019115; F:benzaldehyde dehydrogenase [NAD(P)+] activity; ISO:MGI.
DR GO; GO:0035276; F:ethanol binding; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; ISO:MGI.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:MGI.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; ISO:MGI.
DR GO; GO:0019841; F:retinol binding; ISO:MGI.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0046164; P:alcohol catabolic process; IDA:MGI.
DR GO; GO:0006066; P:alcohol metabolic process; ISO:MGI.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:MGI.
DR GO; GO:0006067; P:ethanol metabolic process; IDA:MGI.
DR GO; GO:0006069; P:ethanol oxidation; ISO:MGI.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IDA:UniProtKB.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR GO; GO:1901661; P:quinone metabolic process; IDA:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; ISO:MGI.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028632; Zinc_ADH_II.
DR PANTHER; PTHR43880:SF14; PTHR43880:SF14; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid metabolism; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..377
FT /note="All-trans-retinol dehydrogenase [NAD(+)] ADH4"
FT /id="PRO_0000160682"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 204..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT BINDING 297..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT BINDING 320..322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT BINDING 372
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10970744"
FT MUTAGEN 48
FT /note="P->H: Strongly increases enzyme activity, serves as
FT proton acceptor."
FT /evidence="ECO:0000269|PubMed:10514444"
FT MUTAGEN 52
FT /note="N->H: No effect."
FT /evidence="ECO:0000269|PubMed:10514444"
FT MUTAGEN 183
FT /note="S->T: Strongly increases activity towards ethanol,
FT increases KM for benzoquinone 10-fold."
FT /evidence="ECO:0000269|PubMed:10514444"
FT CONFLICT 197
FT /note="S -> G (in Ref. 1; CAB57455)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="K -> E (in Ref. 1; CAB57455)"
FT /evidence="ECO:0000305"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1E3I"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:1E3I"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1E3E"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:1E3I"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1E3I"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:1E3I"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:1E3I"
SQ SEQUENCE 377 AA; 40211 MW; 5B527E48BB745E14 CRC64;
MGTQGKVIKC KAAIAWKTGS PLCIEEIEVS PPKACEVRIQ VIATCVCPTD INATDPKKKA
LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKR CKLCLSPLTN LCGKLRNFKY
PTIDQELMED RTSRFTCKGR SIYHFMGVSS FSQYTVVSEA NLARVDDEAN LERVCLIGCG
FSSGYGAAIN TAKVTPSSTC AVFGLGCVGL SAIIGCKIAG ASRIIAIDIN GEKFPKAKAL
GATDCLNPRE LDKPVQDVIT ELTAGGVDYS LDCAGTAQTL KAAVDCTVLG WGSCTVVGAK
VDKMTIPTVD VILGRSINGT FFGGWKSVDS VPNLVSDYKN KKFDLDLLVT HALPFESIND
AIDLMKEGKS IRTILTF
