APOA2_MOUSE
ID APOA2_MOUSE Reviewed; 102 AA.
AC P09813; Q3UKX6; Q61317;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Apolipoprotein A-II;
DE Short=Apo-AII;
DE Short=ApoA-II;
DE AltName: Full=Apolipoprotein A2;
DE Contains:
DE RecName: Full=Proapolipoprotein A-II;
DE Short=ProapoA-II;
DE Flags: Precursor;
GN Name=Apoa2;
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], AND INVOLVEMENT IN SAM.
RX PubMed=2426658; DOI=10.1093/nar/14.14.5729;
RA Kunisada T., Higuchi K., Aota S., Takeda T., Yamagishi H.;
RT "Molecular cloning and nucleotide sequence of cDNA for murine senile
RT amyloid protein: nucleotide substitutions found in apolipoprotein A-II cDNA
RT of senescence accelerated mouse (SAM).";
RL Nucleic Acids Res. 14:5729-5740(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN SAM, AND VARIANT SAM
RP GLN-28.
RX PubMed=2514123; DOI=10.1016/0378-1119(89)90154-6;
RA Yonezu T., Toda M., Yamagishi H., Higuchi K., Takeda T.;
RT "Structural organization of the gene encoding apolipoprotein A-II in an
RT amyloidotic strain of senescence-accelerated mouse.";
RL Gene 84:187-191(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ, C3H/HeJ, C57BL/6J, and DBA/2J; TISSUE=Liver;
RX PubMed=2118905; DOI=10.1016/s0021-9258(17)46234-x;
RA Doolittle M.H., Leboeuf R.C., Warden C.H., Bee L.M., Lusis A.J.;
RT "A polymorphism affecting apolipoprotein A-II translational efficiency
RT determines high density lipoprotein size and composition.";
RL J. Biol. Chem. 265:16380-16388(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=1683229; DOI=10.1042/bj2790427;
RA Higuchi K., Kitagawa K., Naiki H., Hanada K., Hosakawa M., Takeda T.;
RT "Polymorphism of apolipoprotein A-II (apoA-II) among inbred strains of
RT mice. Relationship between the molecular type of apoA-II and mouse senile
RT amyloidosis.";
RL Biochem. J. 279:427-433(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP PROTEIN SEQUENCE OF 24-102.
RX PubMed=3095143; DOI=10.1016/0014-5793(86)80006-0;
RA Higuchi K., Yonezu T., Tsunasawa S., Sakiyama F., Takeda T.;
RT "The single proline-glutamine substitution at position 5 enhances the
RT potency of amyloid fibril formation of murine apo A-II.";
RL FEBS Lett. 207:23-27(1986).
RN [10]
RP PROTEIN SEQUENCE OF 24-102.
RX PubMed=3089836; DOI=10.1016/0014-5793(86)80732-3;
RA Yonezu T., Higuchi K., Tsunasawa S., Takagi S., Sakiyama F., Takeda T.;
RT "High homology is present in the primary structures between murine senile
RT amyloid protein (ASSAM) and human apolipoprotein A-II.";
RL FEBS Lett. 203:149-152(1986).
RN [11]
RP PROTEIN SEQUENCE OF 54-62 AND 68-77, MASS SPECTROMETRY, AND OXIDATION.
RX PubMed=16876491; DOI=10.1016/j.bbapap.2006.06.001;
RA Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W.,
RA Schumaker V.N., Whitelegge J.P.;
RT "Mass spectral analysis of the apolipoproteins on mouse high density
RT lipoproteins. Detection of post-translational modifications.";
RL Biochim. Biophys. Acta 1764:1363-1371(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, 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).
CC -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC association with lipids, and affect the HDL metabolism.
CC -!- SUBUNIT: Monomer. Interacts with NAXE and NDRG1 (By similarity).
CC {ECO:0000250|UniProtKB:P02652}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8709.2;
CC Mass_error=0.071; Method=Electrospray; Note=Strain C57BL/6. Without
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8719.5;
CC Method=Electrospray; Note=Strain BALB/c. Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8725.3;
CC Mass_error=0.283; Method=Electrospray; Note=Strain C57BL/6. With 1
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8742;
CC Method=Electrospray; Note=Strain C57BL/6. With 2 methionine
CC sulfoxides.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8735.2;
CC Method=Electrospray; Note=Strain BALB/c. With 1 methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Proapolipoprotein A-II]: Mass=9294;
CC Mass_error=0.707; Method=Electrospray; Note=Strain C57BL/6. Without
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Proapolipoprotein A-II]: Mass=9304;
CC Method=Electrospray; Note=Strain BALB/c. Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- DISEASE: Note=Defects in Apoa2 are the cause of senescence accelerated
CC mouse (SAM), the senile amyloid is a mutated apolipoprotein A-II.
CC {ECO:0000269|PubMed:2426658, ECO:0000269|PubMed:2514123}.
CC -!- MISCELLANEOUS: The apo A-II stoichiometry in HDL molecules varies among
CC inbred mice strains, because of structural polymorphisms affecting the
CC apo A-II gene, which influence its translational efficiency.
CC -!- MISCELLANEOUS: The sequence presented here is that of strain BALB/c and
CC C3H/HeJ.
CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR EMBL; X04119; CAA27731.1; -; mRNA.
DR EMBL; M32360; AAA37248.1; -; Genomic_DNA.
DR EMBL; M79361; AAA37249.1; -; mRNA.
DR EMBL; M79362; AAA37250.1; -; mRNA.
DR EMBL; X62772; CAA44616.1; -; mRNA.
DR EMBL; AK145823; BAE26675.1; -; mRNA.
DR EMBL; AC084821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39118.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL39119.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL39120.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL39121.1; -; Genomic_DNA.
DR EMBL; BC031786; AAH31786.1; -; mRNA.
DR CCDS; CCDS35773.1; -.
DR PIR; A37887; A37887.
DR PIR; B37887; B23594.
DR PIR; I48250; I48250.
DR PIR; JS0392; A23594.
DR RefSeq; NP_001292478.1; NM_001305549.1.
DR RefSeq; NP_001292479.1; NM_001305550.1.
DR RefSeq; NP_001292514.1; NM_001305585.1.
DR RefSeq; NP_038502.2; NM_013474.2.
DR AlphaFoldDB; P09813; -.
DR SMR; P09813; -.
DR BioGRID; 198156; 13.
DR IntAct; P09813; 1.
DR MINT; P09813; -.
DR STRING; 10090.ENSMUSP00000005824; -.
DR iPTMnet; P09813; -.
DR PhosphoSitePlus; P09813; -.
DR CPTAC; non-CPTAC-3414; -.
DR jPOST; P09813; -.
DR PaxDb; P09813; -.
DR PeptideAtlas; P09813; -.
DR PRIDE; P09813; -.
DR ProteomicsDB; 296334; -.
DR Antibodypedia; 20506; 512 antibodies from 39 providers.
DR DNASU; 11807; -.
DR Ensembl; ENSMUST00000005824; ENSMUSP00000005824; ENSMUSG00000005681.
DR Ensembl; ENSMUST00000111319; ENSMUSP00000106951; ENSMUSG00000005681.
DR Ensembl; ENSMUST00000111320; ENSMUSP00000106952; ENSMUSG00000005681.
DR Ensembl; ENSMUST00000111321; ENSMUSP00000106953; ENSMUSG00000005681.
DR GeneID; 11807; -.
DR KEGG; mmu:11807; -.
DR UCSC; uc007dnk.2; mouse.
DR CTD; 336; -.
DR MGI; MGI:88050; Apoa2.
DR VEuPathDB; HostDB:ENSMUSG00000005681; -.
DR eggNOG; ENOG502SVYZ; Eukaryota.
DR GeneTree; ENSGT00390000003306; -.
DR HOGENOM; CLU_157351_0_0_1; -.
DR InParanoid; P09813; -.
DR OMA; LTICSFE; -.
DR OrthoDB; 1612564at2759; -.
DR TreeFam; TF338165; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 11807; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Apoa2; mouse.
DR PRO; PR:P09813; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P09813; protein.
DR Bgee; ENSMUSG00000005681; Expressed in left lobe of liver and 100 other tissues.
DR Genevisible; P09813; MM.
DR GO; GO:0042627; C:chylomicron; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034190; F:apolipoprotein receptor binding; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IMP:MGI.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0005319; F:lipid transporter activity; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR GO; GO:0033344; P:cholesterol efflux; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR GO; GO:0030301; P:cholesterol transport; ISO:MGI.
DR GO; GO:0046340; P:diacylglycerol catabolic process; ISO:MGI.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:MGI.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IMP:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IDA:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0060621; P:negative regulation of cholesterol import; ISO:MGI.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; ISO:MGI.
DR GO; GO:0060695; P:negative regulation of cholesterol transporter activity; ISO:MGI.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; ISO:MGI.
DR GO; GO:0060192; P:negative regulation of lipase activity; IMP:MGI.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISO:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:MGI.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0018158; P:protein oxidation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; ISO:MGI.
DR InterPro; IPR006801; ApoA-II.
DR InterPro; IPR036172; ApoA-II_sf.
DR PANTHER; PTHR11027; PTHR11027; 1.
DR Pfam; PF04711; ApoA-II; 1.
DR SUPFAM; SSF82936; SSF82936; 1.
PE 1: Evidence at protein level;
KW Amyloid; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disease variant; HDL; Lipid transport; Oxidation; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT CHAIN 19..102
FT /note="Proapolipoprotein A-II"
FT /id="PRO_0000425354"
FT CHAIN 24..102
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000269|PubMed:3089836,
FT ECO:0000269|PubMed:3095143"
FT /id="PRO_0000002008"
FT MOD_RES 49
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT VARIANT 28
FT /note="P -> Q (in SAM)"
FT /evidence="ECO:0000269|PubMed:2514123"
FT CONFLICT 43
FT /note="D -> E (in Ref. 1; CAA27731, 2; AAA37248, 3;
FT AAA37250 and 8; AAH31786)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> F (in Ref. 4; CAA44616)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="M -> V (in Ref. 1; CAA27731, 2; AAA37248, 3;
FT AAA37250 and 8; AAH31786)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="A -> V (in Ref. 1; CAA27731, 3; AAA37250 and 8;
FT AAH31786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 102 AA; 11309 MW; F50142E0D118665B CRC64;
MKLLAMVALL VTICSLEGAL VKRQADGPDM QSLFTQYFQS MTDYGKDLME KAKTSEIQSQ
AKAYFEKTHE QLTPLVRSAG TSLVNFFSSL MNLEEKPAPA AK
