ACDSB_MOUSE
ID ACDSB_MOUSE Reviewed; 432 AA.
AC Q9DBL1;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000250|UniProtKB:P70584};
DE Short=SBCAD {ECO:0000250|UniProtKB:P70584};
DE EC=1.3.8.5 {ECO:0000250|UniProtKB:P70584};
DE AltName: Full=2-methyl branched chain acyl-CoA dehydrogenase;
DE Short=2-MEBCAD;
DE AltName: Full=2-methylbutyryl-coenzyme A dehydrogenase;
DE Short=2-methylbutyryl-CoA dehydrogenase;
DE Flags: Precursor;
GN Name=Acadsb {ECO:0000312|MGI:MGI:1914135};
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=Liver;
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 PROTEIN SEQUENCE OF 348-355, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
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 [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-278 AND LYS-284, AND
RP IDENTIFICATION BY MASS 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-284 AND LYS-426, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Short and branched chain specific acyl-CoA dehydrogenase that
CC catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty
CC acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA.
CC Among the different mitochondrial acyl-CoA dehydrogenases, acts
CC specifically on short and branched chain acyl-CoA derivatives such as
CC (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such
CC as butyryl-CoA (By similarity). Plays an important role in the
CC metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-
CC methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic
CC pathway (By similarity). Can also act on valproyl-CoA, a metabolite of
CC the valproic acid drug (By similarity). {ECO:0000250|UniProtKB:P45954,
CC ECO:0000250|UniProtKB:P70584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57336,
CC ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.5;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43781;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:48256, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57337,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:88166;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48257;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = ethylacryloyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:65296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:156439, ChEBI:CHEBI:156440;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65297;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylpropenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:44180, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62500;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44181;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + valproyl-
CC CoA = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:65344, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:156457, ChEBI:CHEBI:156458;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65345;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P45954};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P45954}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AK004889; BAB23646.1; -; mRNA.
DR CCDS; CCDS21916.1; -.
DR RefSeq; NP_080102.1; NM_025826.4.
DR AlphaFoldDB; Q9DBL1; -.
DR SMR; Q9DBL1; -.
DR IntAct; Q9DBL1; 2.
DR MINT; Q9DBL1; -.
DR STRING; 10090.ENSMUSP00000015829; -.
DR iPTMnet; Q9DBL1; -.
DR PhosphoSitePlus; Q9DBL1; -.
DR SwissPalm; Q9DBL1; -.
DR EPD; Q9DBL1; -.
DR jPOST; Q9DBL1; -.
DR MaxQB; Q9DBL1; -.
DR PaxDb; Q9DBL1; -.
DR PeptideAtlas; Q9DBL1; -.
DR PRIDE; Q9DBL1; -.
DR ProteomicsDB; 285970; -.
DR Antibodypedia; 19074; 161 antibodies from 31 providers.
DR DNASU; 66885; -.
DR Ensembl; ENSMUST00000015829; ENSMUSP00000015829; ENSMUSG00000030861.
DR GeneID; 66885; -.
DR KEGG; mmu:66885; -.
DR UCSC; uc009kbm.2; mouse.
DR CTD; 36; -.
DR MGI; MGI:1914135; Acadsb.
DR VEuPathDB; HostDB:ENSMUSG00000030861; -.
DR eggNOG; KOG0139; Eukaryota.
DR GeneTree; ENSGT00940000156525; -.
DR HOGENOM; CLU_018204_0_0_1; -.
DR InParanoid; Q9DBL1; -.
DR OMA; LYREAPM; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; Q9DBL1; -.
DR TreeFam; TF105055; -.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00364; -.
DR UniPathway; UPA00660; -.
DR BioGRID-ORCS; 66885; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q9DBL1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DBL1; protein.
DR Bgee; ENSMUSG00000030861; Expressed in hindlimb stylopod muscle and 257 other tissues.
DR ExpressionAtlas; Q9DBL1; baseline and differential.
DR Genevisible; Q9DBL1; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0047119; F:2-methyl-branched-chain-enoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003853; F:2-methylacyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0102035; F:isobutyryl-CoA:FAD oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016937; F:short-branched-chain-acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006550; P:isoleucine catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT CHAIN 34..432
FT /note="Short/branched chain specific acyl-CoA
FT dehydrogenase, mitochondrial"
FT /id="PRO_0000000520"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 174..183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 207..209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 291..294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 387..391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 416..418
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT MOD_RES 278
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 284
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 284
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 432 AA; 47874 MW; 0272723CE36BCC46 CRC64;
MAVSALQLWR MGGLLRRRFP TCLSPWKIPP RVLKSSQPEA LVSLTNNAVA FAPLQTLTDE
EIMMKQTVKK FAQEHVAPLV SSMDENSKME KSVIQGLFQQ GLMGIEVEAQ YGGTEASFFC
SVLVIEELAK VDASVALLCD IQNTIINNLF RKHASEEQKA TYLPKLVTEK LGSFCLSEAG
AGSDSFAMKT RADKSGNYYV LNGSKMWISH AEHAELFLVF ANVDPSSGYR GITCFLVDRD
TEGFQIGKRE NKMGIRASST CQLTFENVKV PETNILGKIG HGYKYAIGSL NEGRIGIAAQ
MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAQVA TQLEATRLLT YNAARLVEAG
RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGASNIQ
LNTIAKHIDA EY
