ARK72_HUMAN
ID ARK72_HUMAN Reviewed; 359 AA.
AC O43488; O75749; Q5TG63;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Aflatoxin B1 aldehyde reductase member 2;
DE EC=1.1.1.n11;
DE AltName: Full=AFB1 aldehyde reductase 1;
DE Short=AFB1-AR 1;
DE AltName: Full=Aldoketoreductase 7;
DE AltName: Full=Succinic semialdehyde reductase;
DE Short=SSA reductase;
GN Name=AKR7A2; Synonyms=AFAR, AFAR1, AKR7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-359.
RC TISSUE=Pancreas, Skin, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-359, PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT THR-142.
RC TISSUE=Liver;
RX PubMed=9576847; DOI=10.1042/bj3320021;
RA Ireland L.S., Harrison D.J., Neal G.E., Hayes J.D.;
RT "Molecular cloning, expression and catalytic activity of a human AKR7
RT member of the aldo-keto reductase superfamily: evidence that the major 2-
RT carboxybenzaldehyde reductase from human liver is a homologue of rat
RT aflatoxin B1-aldehyde reductase.";
RL Biochem. J. 332:21-34(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-359.
RC TISSUE=Brain;
RX PubMed=9823300;
RA Praml C., Savelyeva L., Perri P., Schwab M.;
RT "Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1
RT in a region frequently altered in human tumor cells.";
RL Cancer Res. 58:5014-5018(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-359.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 222-236; 251-261 AND 279-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=10510318; DOI=10.1042/bj3430487;
RA O'Connor T., Ireland L.S., Harrison D.J., Hayes J.D.;
RT "Major differences exist in the function and tissue-specific expression of
RT human aflatoxin B1 aldehyde reductase and the principal human aldo-keto
RT reductase AKR1 family members.";
RL Biochem. J. 343:487-504(1999).
RN [8]
RP GENE STRUCTURE.
RX PubMed=12071861; DOI=10.1042/bj20020342;
RA Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D.;
RT "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases
RT that associate with the Golgi apparatus define a distinct subclass of aldo-
RT keto reductase 7 family proteins.";
RL Biochem. J. 366:847-861(2002).
RN [9]
RP FUNCTION.
RX PubMed=17591773; DOI=10.1074/jbc.m702465200;
RA Lyon R.C., Johnston S.M., Watson D.G., McGarvie G., Ellis E.M.;
RT "Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human
RT neuroblastoma cells: role of the aldo-keto reductase AKR7A2.";
RL J. Biol. Chem. 282:25986-25992(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.
RG Structural genomics consortium (SGC);
RT "Structure of the aflatoxin aldehyde reductase in complex with NADPH.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [15]
RP VARIANTS THR-142 AND HIS-157.
RX PubMed=18752886; DOI=10.1016/j.canlet.2008.07.013;
RA Praml C., Schulz W., Claas A., Mollenhauer J., Poustka A., Ackermann R.,
RA Schwab M., Henrich K.-O.;
RT "Genetic variation of aflatoxin B1 aldehyde reductase genes (AFAR) in human
RT tumour cells.";
RL Cancer Lett. 272:160-166(2008).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of succinic
CC semialdehyde to gamma-hydroxybutyrate. May have an important role in
CC producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad
CC substrate specificity. Has NADPH-dependent aldehyde reductase activity
CC towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-
CC aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-
CC phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-
CC binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol.
CC May be involved in protection of liver against the toxic and
CC carcinogenic effects of AFB1, a potent hepatocarcinogen.
CC {ECO:0000269|PubMed:17591773, ECO:0000269|PubMed:9576847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate
CC semialdehyde; Xref=Rhea:RHEA:26381, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16724, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.n11;
CC Evidence={ECO:0000269|PubMed:10510318};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for succinic semialdehyde {ECO:0000269|PubMed:10510318};
CC KM=17 uM for 2-carboxybenzaldehyde {ECO:0000269|PubMed:10510318};
CC KM=8 uM for 9,10-phenanthrenequinone {ECO:0000269|PubMed:10510318};
CC KM=102 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:10510318};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9576847, ECO:0000269|Ref.14}.
CC -!- INTERACTION:
CC O43488; O95154: AKR7A3; NbExp=6; IntAct=EBI-748855, EBI-748869;
CC O43488; Q92870-2: APBB2; NbExp=3; IntAct=EBI-748855, EBI-21535880;
CC O43488; P54252: ATXN3; NbExp=3; IntAct=EBI-748855, EBI-946046;
CC O43488; Q8WWM9: CYGB; NbExp=3; IntAct=EBI-748855, EBI-6309037;
CC O43488; Q9Y2K1: ZBTB1; NbExp=4; IntAct=EBI-748855, EBI-2682961;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:9576847}.
CC -!- TISSUE SPECIFICITY: Detected in brain, liver, small intestine and
CC testis, and at lower levels in heart, prostate, skeletal muscle and
CC spleen. Detected in kidney proximal and distal tubules, endothelial
CC cells lining the Bowman's capsules and some cysts. Detected at low
CC levels in lung and pancreas (at protein level). Widely expressed.
CC {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:9576847}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-30 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH04111.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH10852.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH11586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH12171.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH13996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP36011.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA76347.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL035413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004111; AAH04111.3; ALT_INIT; mRNA.
DR EMBL; BC007352; AAH07352.2; -; mRNA.
DR EMBL; BC010852; AAH10852.1; ALT_INIT; mRNA.
DR EMBL; BC011586; AAH11586.1; ALT_INIT; mRNA.
DR EMBL; BC012171; AAH12171.1; ALT_INIT; mRNA.
DR EMBL; BC013996; AAH13996.1; ALT_INIT; mRNA.
DR EMBL; AF026947; AAC52104.1; ALT_INIT; mRNA.
DR EMBL; Y16675; CAA76347.1; ALT_INIT; mRNA.
DR EMBL; BT007347; AAP36011.1; ALT_INIT; mRNA.
DR EMBL; BK000395; DAA00088.1; -; mRNA.
DR CCDS; CCDS194.1; -.
DR RefSeq; NP_003680.2; NM_003689.3.
DR PDB; 2BP1; X-ray; 2.40 A; A/B/C/D=1-359.
DR PDBsum; 2BP1; -.
DR AlphaFoldDB; O43488; -.
DR SMR; O43488; -.
DR BioGRID; 114142; 64.
DR IntAct; O43488; 46.
DR STRING; 9606.ENSP00000235835; -.
DR iPTMnet; O43488; -.
DR MetOSite; O43488; -.
DR PhosphoSitePlus; O43488; -.
DR SwissPalm; O43488; -.
DR BioMuta; AKR7A2; -.
DR REPRODUCTION-2DPAGE; IPI00305978; -.
DR REPRODUCTION-2DPAGE; O43488; -.
DR UCD-2DPAGE; O43488; -.
DR EPD; O43488; -.
DR jPOST; O43488; -.
DR MassIVE; O43488; -.
DR PaxDb; O43488; -.
DR PeptideAtlas; O43488; -.
DR PRIDE; O43488; -.
DR ProteomicsDB; 48966; -.
DR Antibodypedia; 29614; 283 antibodies from 31 providers.
DR DNASU; 8574; -.
DR Ensembl; ENST00000235835.8; ENSP00000235835.3; ENSG00000053371.13.
DR GeneID; 8574; -.
DR KEGG; hsa:8574; -.
DR MANE-Select; ENST00000235835.8; ENSP00000235835.3; NM_003689.4; NP_003680.2.
DR CTD; 8574; -.
DR DisGeNET; 8574; -.
DR GeneCards; AKR7A2; -.
DR HGNC; HGNC:389; AKR7A2.
DR HPA; ENSG00000053371; Low tissue specificity.
DR MIM; 603418; gene.
DR neXtProt; NX_O43488; -.
DR OpenTargets; ENSG00000053371; -.
DR PharmGKB; PA24682; -.
DR VEuPathDB; HostDB:ENSG00000053371; -.
DR eggNOG; ENOG502QU2T; Eukaryota.
DR GeneTree; ENSGT00940000164191; -.
DR HOGENOM; CLU_023205_1_1_1; -.
DR InParanoid; O43488; -.
DR OMA; TARMYVG; -.
DR OrthoDB; 1226539at2759; -.
DR PhylomeDB; O43488; -.
DR TreeFam; TF329173; -.
DR BioCyc; MetaCyc:ENSG00000053371-MON; -.
DR PathwayCommons; O43488; -.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR SABIO-RK; O43488; -.
DR SignaLink; O43488; -.
DR BioGRID-ORCS; 8574; 9 hits in 1085 CRISPR screens.
DR ChiTaRS; AKR7A2; human.
DR EvolutionaryTrace; O43488; -.
DR GeneWiki; AKR7A2; -.
DR GenomeRNAi; 8574; -.
DR Pharos; O43488; Tbio.
DR PRO; PR:O43488; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43488; protein.
DR Bgee; ENSG00000053371; Expressed in mucosa of transverse colon and 199 other tissues.
DR ExpressionAtlas; O43488; baseline and differential.
DR Genevisible; O43488; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; TAS:ProtInc.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0019119; F:phenanthrene-9,10-epoxide hydrolase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; TAS:ProtInc.
DR GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
DR GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Golgi apparatus; Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..359
FT /note="Aflatoxin B1 aldehyde reductase member 2"
FT /id="PRO_0000070375"
FT ACT_SITE 77
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171..172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 226..236
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 250
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318..326
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 105
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT MOD_RES 236
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 135
FT /note="V -> M (in dbSNP:rs6670759)"
FT /id="VAR_048209"
FT VARIANT 142
FT /note="A -> T (in dbSNP:rs1043657)"
FT /evidence="ECO:0000269|PubMed:18752886,
FT ECO:0000269|PubMed:9576847"
FT /id="VAR_017413"
FT VARIANT 157
FT /note="Q -> H (in dbSNP:rs859208)"
FT /evidence="ECO:0000269|PubMed:18752886"
FT /id="VAR_017414"
FT VARIANT 180
FT /note="E -> K (in dbSNP:rs859210)"
FT /id="VAR_060222"
FT VARIANT 198
FT /note="G -> S (in dbSNP:rs2231200)"
FT /id="VAR_048210"
FT VARIANT 214
FT /note="C -> Y (in dbSNP:rs2235794)"
FT /id="VAR_017415"
FT VARIANT 255
FT /note="S -> N (in dbSNP:rs2231203)"
FT /id="VAR_048211"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2BP1"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2BP1"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 267..284
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2BP1"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:2BP1"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2BP1"
SQ SEQUENCE 359 AA; 39589 MW; 2C9775FE4B977D2A CRC64;
MLSAASRVVS RAAVHCALRS PPPEARALAM SRPPPPRVAS VLGTMEMGRR MDAPASAAAV
RAFLERGHTE LDTAFMYSDG QSETILGGLG LGLGGGDCRV KIATKANPWD GKSLKPDSVR
SQLETSLKRL QCPQVDLFYL HAPDHGTPVE ETLHACQRLH QEGKFVELGL SNYASWEVAE
ICTLCKSNGW ILPTVYQGMY NATTRQVETE LFPCLRHFGL RFYAYNPLAG GLLTGKYKYE
DKDGKQPVGR FFGNSWAETY RNRFWKEHHF EAIALVEKAL QAAYGASAPS VTSAALRWMY
HHSQLQGAHG DAVILGMSSL EQLEQNLAAT EEGPLEPAVV DAFNQAWHLV AHECPNYFR
