ID ARK72_MOUSE Reviewed; 367 AA. AC Q8CG76; A2AMV3; Q3UPU2; Q8CG77; Q8JZQ8; Q9D157; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 24-JAN-2024, entry version 166. DE RecName: Full=Aflatoxin B1 aldehyde reductase member 2; DE EC=1.1.1.n11; DE AltName: Full=Succinic semialdehyde reductase; DE Short=SSA reductase; DE Flags: Precursor; GN Name=Akr7a2 {ECO:0000250|UniProtKB:O43488}; GN Synonyms=Afar {ECO:0000312|MGI:MGI:107796}, Akr7a5 GN {ECO:0000312|MGI:MGI:107796}; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Eye; 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 [2] 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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH31857.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-367. RC STRAIN=FVB/N; TISSUE=Liver {ECO:0000312|EMBL:AAH31857.1}; 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 [4] {ECO:0000305, ECO:0000312|EMBL:CAC81078.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-367. RC STRAIN=BALB/cJ {ECO:0000312|EMBL:CAC81078.1}; RX PubMed=12879023; DOI=10.1038/sj.onc.1206684; RA Praml C., Savelyeva L., Schwab M.; RT "Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a RT region frequently altered in human tumour cells."; RL Oncogene 22:4765-4773(2003). RN [5] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-367, AND TISSUE SPECIFICITY. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=12123834; DOI=10.1016/s0014-5793(02)02982-4; RA Hinshelwood A., McGarvie G., Ellis E.; RT "Characterisation of a novel mouse liver aldo-keto reductase AKR7A5."; RL FEBS Lett. 523:213-218(2002). RN [6] {ECO:0000305} RP SEQUENCE REVISION TO 127 AND 162. RA Ellis E.M., Hinshelwood A., McGarvie G.; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000305, ECO:0000312|EMBL:DAA00087.1} 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND THR-48, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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 [10] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-244, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-367 IN COMPLEX WITH NADP AND RP THE INHIBITOR TARTRATE, ACTIVITY REGULATION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBUNIT. RX PubMed=16460003; DOI=10.1021/bi051610k; RA Zhu X., Lapthorn A.J., Ellis E.M.; RT "Crystal structure of mouse succinic semialdehyde reductase AKR7A5: RT structural basis for substrate specificity."; RL Biochemistry 45:1562-1570(2006). 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. Can reduce the dialdehyde protein-binding form CC of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be CC involved in protection of liver against the toxic and carcinogenic CC effects of AFB1, a potent hepatocarcinogen (By similarity). CC {ECO:0000250, ECO:0000269|PubMed:16460003}. 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:16460003}; CC -!- ACTIVITY REGULATION: Inhibited by citrate, succinate and tartrate. CC {ECO:0000269|PubMed:16460003}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=19.8 uM for succinic semialdehyde {ECO:0000269|PubMed:16460003}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16460003}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. Golgi apparatus CC {ECO:0000250|UniProtKB:Q8CG45}. Cytoplasm CC {ECO:0000250|UniProtKB:O43488}. CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, testis and brain with CC low levels in skeletal muscle, spleen, heart and lung. CC {ECO:0000269|PubMed:12123834}. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto CC reductase 2 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH31857.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAC81077.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAC81078.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK143203; BAE25302.1; -; mRNA. DR EMBL; AL807811; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC031857; AAH31857.1; ALT_INIT; mRNA. DR EMBL; AJ271800; CAC81077.1; ALT_INIT; mRNA. DR EMBL; AJ271801; CAC81078.1; ALT_INIT; mRNA. DR EMBL; AF525358; AAO38437.2; -; mRNA. DR EMBL; BK000393; DAA00087.1; -; mRNA. DR CCDS; CCDS18844.1; -. DR RefSeq; NP_079613.3; NM_025337.3. DR PDB; 2C91; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=30-367. DR PDBsum; 2C91; -. DR AlphaFoldDB; Q8CG76; -. DR SMR; Q8CG76; -. DR BioGRID; 225379; 5. DR IntAct; Q8CG76; 1. DR STRING; 10090.ENSMUSP00000073459; -. DR iPTMnet; Q8CG76; -. DR PhosphoSitePlus; Q8CG76; -. DR SwissPalm; Q8CG76; -. DR REPRODUCTION-2DPAGE; Q8CG76; -. DR EPD; Q8CG76; -. DR jPOST; Q8CG76; -. DR MaxQB; Q8CG76; -. DR PaxDb; 10090-ENSMUSP00000073459; -. DR PeptideAtlas; Q8CG76; -. DR ProteomicsDB; 265100; -. DR Pumba; Q8CG76; -. DR DNASU; 110198; -. DR Ensembl; ENSMUST00000073787.7; ENSMUSP00000073459.7; ENSMUSG00000028743.8. DR GeneID; 110198; -. DR KEGG; mmu:110198; -. DR UCSC; uc008vmc.2; mouse. DR AGR; MGI:107796; -. DR CTD; 110198; -. DR MGI; MGI:107796; Akr7a5. DR VEuPathDB; HostDB:ENSMUSG00000028743; -. DR eggNOG; ENOG502QU2T; Eukaryota. DR GeneTree; ENSGT00940000158496; -. DR HOGENOM; CLU_023205_1_1_1; -. DR InParanoid; Q8CG76; -. DR OMA; APNYWHL; -. DR OrthoDB; 1379250at2759; -. DR PhylomeDB; Q8CG76; -. DR TreeFam; TF329173; -. DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification. DR SABIO-RK; Q8CG76; -. DR BioGRID-ORCS; 110198; 3 hits in 80 CRISPR screens. DR ChiTaRS; Akr7a5; mouse. DR EvolutionaryTrace; Q8CG76; -. DR PRO; PR:Q8CG76; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q8CG76; Protein. DR Bgee; ENSMUSG00000028743; Expressed in right kidney and 259 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005635; C:nuclear envelope; ISO:MGI. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; ISO:MGI. DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0019119; F:phenanthrene-9,10-epoxide hydrolase activity; ISO:MGI. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR CDD; cd19075; AKR_AKR7A1-5; 1. DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR InterPro; IPR036812; NADP_OxRdtase_dom_sf. DR PANTHER; PTHR43364:SF4; NAD(P)-LINKED OXIDOREDUCTASE SUPERFAMILY PROTEIN; 1. DR PANTHER; PTHR43364; NADH-SPECIFIC METHYLGLYOXAL REDUCTASE-RELATED; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1. DR Genevisible; Q8CG76; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Golgi apparatus; Lipid metabolism; KW Mitochondrion; NADP; Oxidoreductase; Phosphoprotein; Reference proteome; KW Transit peptide. FT TRANSIT 1..46 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 47..367 FT /note="Aflatoxin B1 aldehyde reductase member 2" FT /id="PRO_0000070376" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 85 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 80 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 179..180 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 205 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 234..244 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 258 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 326..334 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16460003" FT BINDING 367 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16460003" FT SITE 113 FT /note="Lowers pKa of active site Tyr" FT /evidence="ECO:0000250|UniProtKB:O43488" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 48 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 136 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 244 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT CONFLICT 5 FT /note="A -> G (in Ref. 1; BAE25302)" FT /evidence="ECO:0000305" FT CONFLICT 9 FT /note="V -> G (in Ref. 1; BAE25302)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="A -> V (in Ref. 1; BAE25302)" FT /evidence="ECO:0000305" FT CONFLICT 17 FT /note="A -> G (in Ref. 1; BAE25302)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="I -> V (in Ref. 3; AAH31857 and 4; CAC81078)" FT /evidence="ECO:0000305" FT CONFLICT 162 FT /note="R -> C (in Ref. 5; AAO38437)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="A -> G (in Ref. 3; AAH31857)" FT /evidence="ECO:0000305" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:2C91" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 61..73 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 89..95 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:2C91" FT TURN 117..120 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 124..137 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 157..169 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 172..180 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 183..196 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 201..207 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 219..226 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 237..242 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 247..250 FT /evidence="ECO:0007829|PDB:2C91" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 265..272 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 275..292 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 299..309 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:2C91" FT STRAND 320..323 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 328..337 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 345..358 FT /evidence="ECO:0007829|PDB:2C91" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:2C91" SQ SEQUENCE 367 AA; 40612 MW; 1123BD7028D3FBDF CRC64; MLRAASRAVG RAAVRSAQRS GTSVGRPLAM SRPPPPRAAS GAPLRPATVL GTMEMGRRMD ASASAASVRA FLERGHSELD TAFMYCDGQS ENILGGLGLG LGSGDCTVKI ATKANPWEGK SLKPDSIRSQ LETSLKRLQC PRVDLFYLHA PDHSTPVEET LRACHQLHQE GKFVELGLSN YASWEVAEIC TLCKSNGWIL PTVYQGMYNA TTRQVEAELL PCLRHFGLRF YAYNPLAGGL LTGKYKYEDK DGKQPVGRFF GNNWAETYRN RFWKEHHFEA IALVEKALQT TYGTNAPRMT SAALRWMYHH SQLQGTRGDA VILGMSSLEQ LEQNLAATEE GPLEPAVVEA FDQAWNMVAH ECPNYFR //