ACD11_MOUSE
ID ACD11_MOUSE Reviewed; 779 AA.
AC Q80XL6; Q8BK19;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11;
DE Short=ACAD-11;
DE EC=1.3.8.- {ECO:0000250|UniProtKB:Q709F0};
GN Name=Acad11;
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=Embryo, and Placenta;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=17768142; DOI=10.1074/mcp.m700169-mcp200;
RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A.,
RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T.,
RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., Just W.,
RA Azevedo J.E., Wanders R.J., Warscheid B.;
RT "Proteomics characterization of mouse kidney peroxisomes by tandem mass
RT spectrometry and protein correlation profiling.";
RL Mol. Cell. Proteomics 6:2045-2057(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND TYR-323, AND
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Pancreas;
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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-368 AND LYS-390, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-166; LYS-175 AND
RP LYS-765, AND 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: Acyl-CoA dehydrogenase, that exhibits maximal activity
CC towards saturated C22-CoA. Probably participates in beta-oxydation and
CC energy production but could also play a role in the metabolism of
CC specific fatty acids to control fatty acids composition of cellular
CC lipids in brain. {ECO:0000250|UniProtKB:Q709F0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:44704, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexacosanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexacosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48216, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:64868, ChEBI:CHEBI:74281;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tricosanoyl-CoA = (2E)-tricosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48220, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:90118, ChEBI:CHEBI:90119;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:Q709F0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q709F0}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17768142}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:Q709F0}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AK077531; BAC36849.2; -; mRNA.
DR EMBL; AK145561; BAE26511.1; -; mRNA.
DR EMBL; AK145834; BAE26684.1; -; mRNA.
DR EMBL; BC045199; AAH45199.1; -; mRNA.
DR CCDS; CCDS23458.1; -.
DR RefSeq; NP_780533.2; NM_175324.3.
DR AlphaFoldDB; Q80XL6; -.
DR SMR; Q80XL6; -.
DR BioGRID; 221913; 16.
DR STRING; 10090.ENSMUSP00000043424; -.
DR iPTMnet; Q80XL6; -.
DR PhosphoSitePlus; Q80XL6; -.
DR SwissPalm; Q80XL6; -.
DR EPD; Q80XL6; -.
DR jPOST; Q80XL6; -.
DR MaxQB; Q80XL6; -.
DR PaxDb; Q80XL6; -.
DR PeptideAtlas; Q80XL6; -.
DR PRIDE; Q80XL6; -.
DR ProteomicsDB; 285536; -.
DR GeneID; 102632; -.
DR KEGG; mmu:102632; -.
DR UCSC; uc009rhg.1; mouse.
DR CTD; 84129; -.
DR MGI; MGI:2143169; Acad11.
DR eggNOG; KOG1469; Eukaryota.
DR InParanoid; Q80XL6; -.
DR OrthoDB; 1028522at2759; -.
DR PhylomeDB; Q80XL6; -.
DR TreeFam; TF333953; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 102632; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Acad11; mouse.
DR PRO; PR:Q80XL6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80XL6; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISS:HGNC.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISO:MGI.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR041726; ACAD10_11_N.
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 InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 Pfam; PF01636; APH; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Membrane; Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..779
FT /note="Acyl-CoA dehydrogenase family member 11"
FT /id="PRO_0000254146"
FT BINDING 503..513
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"
FT BINDING 511..513
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"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 537..539
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"
FT BINDING 539
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"
FT BINDING 628..631
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 726..730
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 726
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"
FT BINDING 754
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 755..757
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"
FT BINDING 757
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"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 368
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 390
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 765
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 426
FT /note="M -> I (in Ref. 1; BAC36849/BAE26511/BAE26684)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="T -> M (in Ref. 2; AAH45199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 87366 MW; ABE9D1919D23426E CRC64;
METDVTSDTV EVLPQHKFDL RSLEAYLNQH LPGFGSDSRA VLTVTQYRSG QSNPTFFLQK
GSQAYVLRKK PPGSLLPKAH KIDREFKIQK ALFSIGFPVA KPLLYCRDAS VIGTEFYVME
HVQGRIFRDF SIPGVSSAER AAIYVSVAET LAWLHSLDIR SLKLDKYGTG VGYCKRQVST
WTKQYQASAH QSIPAMDQLS TWLMKNLPDS DSEECLVHGD FKLDNIVFHP KECRVIAVLD
WELSTFGHPL TDLAHLSLFY YWPRTLPMIN RGSHIPENTG IPLMEELISI YCHRRGIDPN
LPNWNFFMAL SFFKLAGISQ GVYRRYLMGN NSSEDSFLTA NTVQPLAETG LQLSKRTLRT
TPPQADAKSQ LFAQSRRGQE VLTRVKQFMK QHVFPAEKEV AEYYAQSGNS AEKWGHPLVI
EKLKEMAKAE GLWNLFLPAV SGLSQVDYAL IAEETGKCFF APDVFNCQAP DTGNMEVLHL
YGSEQQKKQW LEPLLRGDIT SVFCMTEPNV SSSDATNIEC TIQRDGGGYI VNGKKWWSSG
AGNPKCKIAI VLGRTESPSA SRHRQHSMIL VPMDTPGVEL IRPLSVFGYM DNMHGGHWEV
HFNHVRVPAS NLILGEGRGF EISQGRLGPG RIHHCMRTVG LAERILQIMC DRAVQREAFK
KKLYEHEVVA HWIAKSRIAI EEIRLLTLKA AHSIDTLGSA SARKEIAMIK VAAPKAVCKI
ADWAIQVHGG AGVSQDYPLA NMYAIIRTLR LADGPDEVHL SAIAKMELQD QARRLTARM
