AL3A2_MOUSE
ID AL3A2_MOUSE Reviewed; 484 AA.
AC P47740; Q99L64;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Aldehyde dehydrogenase family 3 member A2;
DE EC=1.2.1.3 {ECO:0000269|PubMed:25286108};
DE EC=1.2.1.94 {ECO:0000250|UniProtKB:P51648};
DE AltName: Full=Aldehyde dehydrogenase 3;
DE AltName: Full=Fatty aldehyde dehydrogenase;
GN Name=Aldh3a2; Synonyms=Ahd-3, Ahd3, Aldh3, Aldh4;
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].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=8634152; DOI=10.1089/dna.1996.15.235;
RA Vasiliou V., Kozak C.A., Lindahl R., Nebert D.W.;
RT "Mouse microsomal class 3 aldehyde dehydrogenase: AHD3 cDNA sequence,
RT inducibility by dioxin and clofibrate, and genetic mapping.";
RL DNA Cell Biol. 15:235-245(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Spinal cord, Stomach, and Thymus;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=25286108; DOI=10.1042/bj20140624;
RA Kitamura T., Takagi S., Naganuma T., Kihara A.;
RT "Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via
RT two C-terminal tryptophan residues and lipid modification.";
RL Biochem. J. 465:79-87(2015).
CC -!- FUNCTION: Catalyzes the oxidation of medium and long-chain aliphatic
CC aldehydes to fatty acids. Active on a variety of saturated and
CC unsaturated aliphatic aldehydes between 6 and 24 carbons in length
CC (PubMed:25286108). Responsible for conversion of the sphingosine 1-
CC phosphate (S1P) degradation product hexadecenal to hexadecenoic acid
CC (PubMed:25286108). {ECO:0000269|PubMed:25286108}.
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:25286108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+);
CC Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:72745;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298,
CC ChEBI:CHEBI:76299; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14-
CC tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate;
CC Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+);
CC Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate;
CC Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84067; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH;
CC Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+)
CC + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:83276; EC=1.2.1.94;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51648}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:25286108}. Microsome
CC membrane {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P51648}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P51648}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P30839}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {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; U14390; AAB06232.1; -; mRNA.
DR EMBL; AK079639; BAC37712.1; -; mRNA.
DR EMBL; AK140932; BAE24523.1; -; mRNA.
DR EMBL; AK159246; BAE34928.1; -; mRNA.
DR EMBL; AK163040; BAE37166.1; -; mRNA.
DR EMBL; AK169157; BAE40936.1; -; mRNA.
DR EMBL; AK170195; BAE41628.1; -; mRNA.
DR EMBL; AL672172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003797; AAH03797.1; -; mRNA.
DR CCDS; CCDS24809.1; -.
DR RefSeq; NP_031463.2; NM_007437.5.
DR AlphaFoldDB; P47740; -.
DR SMR; P47740; -.
DR BioGRID; 198066; 5.
DR STRING; 10090.ENSMUSP00000073764; -.
DR SwissLipids; SLP:000001741; -.
DR iPTMnet; P47740; -.
DR PhosphoSitePlus; P47740; -.
DR SwissPalm; P47740; -.
DR EPD; P47740; -.
DR jPOST; P47740; -.
DR MaxQB; P47740; -.
DR PaxDb; P47740; -.
DR PRIDE; P47740; -.
DR ProteomicsDB; 282068; -.
DR Antibodypedia; 2232; 473 antibodies from 32 providers.
DR DNASU; 11671; -.
DR Ensembl; ENSMUST00000074127; ENSMUSP00000073764; ENSMUSG00000010025.
DR GeneID; 11671; -.
DR KEGG; mmu:11671; -.
DR UCSC; uc007jhf.2; mouse.
DR CTD; 224; -.
DR MGI; MGI:1353452; Aldh3a2.
DR VEuPathDB; HostDB:ENSMUSG00000010025; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000157944; -.
DR HOGENOM; CLU_005391_3_0_1; -.
DR InParanoid; P47740; -.
DR OMA; RRITWAA; -.
DR OrthoDB; 646662at2759; -.
DR TreeFam; TF314264; -.
DR BRENDA; 1.2.1.3; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-MMU-389599; Alpha-oxidation of phytanate.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 11671; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Aldh3a2; mouse.
DR PRO; PR:P47740; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P47740; protein.
DR Bgee; ENSMUSG00000010025; Expressed in prostate gland ventral lobe and 251 other tissues.
DR ExpressionAtlas; P47740; baseline and differential.
DR Genevisible; P47740; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISO:MGI.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; ISO:MGI.
DR GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; ISO:MGI.
DR GO; GO:0008544; P:epidermis development; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046292; P:formaldehyde metabolic process; ISO:MGI.
DR GO; GO:0046458; P:hexadecanal metabolic process; ISS:UniProtKB.
DR GO; GO:0007422; P:peripheral nervous system development; ISO:MGI.
DR GO; GO:0033306; P:phytol metabolic process; ISO:MGI.
DR GO; GO:0000302; P:response to reactive oxygen species; ISO:MGI.
DR GO; GO:0006714; P:sesquiterpenoid metabolic process; ISO:MGI.
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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 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 Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Microsome; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..484
FT /note="Aldehyde dehydrogenase family 3 member A2"
FT /id="PRO_0000056475"
FT TOPO_DOM 1..463
FT /note="Cytoplasmic"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 481..484
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT ACT_SITE 207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 185..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51648"
FT CONFLICT 19
FT /note="P -> L (in Ref. 1; AAB06232)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="I -> V (in Ref. 1; AAB06232)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="T -> A (in Ref. 1; AAB06232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53971 MW; DFC67C96C757832A CRC64;
MERQVLRLRQ AFRSGRSRPL RFRLQQLEAL RRMVQEREKE ILAAIAADLS KSELNAYSHE
VITILGEIDF MLGNLPELAS ARPAKKNLLT MMDEAYVQPE PLGVVLIIGA WNYPFVLTMQ
PLVGAIAAGN AAIVKPSELS ENTAKILAEL LPQYLDQDLY AIVNGGIPET TELLKQRFDH
ILYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDRDC DLDVACRRIA WGKYMNCGQT
CIAPDYILCE ASLQNQIVQK IKETVKDFYG ENIKASPDYE RIINLRHFKR LQSLLKGQKI
AFGGEMDEAT RYLAPTILTD VDPNSKVMQE EIFGPILPIV SVKNVDEAIN FINDREKPLA
LYVFSRNNKL IKRVIDETSS GGVTGNDVIM HFTVNSLPFG GVGASGMGAY HGKYSFDTFS
HQRPCLLKGL KGESVNKLRY PPNSESKVSW AKFFLLKQFN KGRLGMLLFV CLVAVAAVIV
KDQL
