ABC8A_MOUSE
ID ABC8A_MOUSE Reviewed; 1620 AA.
AC Q8K442; A2AB96; Q6PAV3; Q8C0A9; Q8R0R4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ABC-type organic anion transporter ABCA8A {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O94911};
DE AltName: Full=ATP-binding cassette sub-family A member 8A {ECO:0000305};
GN Name=Abca8a {ECO:0000312|MGI:MGI:2386846};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=12532264; DOI=10.1007/s00335-002-2229-9;
RA Annilo T., Chen Z.-Q., Shulenin S., Dean M.;
RT "Evolutionary analysis of a cluster of ATP-binding cassette (ABC) genes.";
RL Mamm. Genome 14:7-20(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
RA Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
RT "Acute digoxin loading reduces ABCA8A mRNA expression in the mouse liver.";
RL Clin. Exp. Pharmacol. Physiol. 32:1034-1041(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] OF 811-1620.
RC STRAIN=C57BL/6J; TISSUE=Eye, and Retina;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 898-1620.
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, 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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=28882873; DOI=10.1161/atvbaha.117.309574;
RA Trigueros-Motos L., van Capelleveen J.C., Torta F., Castano D., Zhang L.H.,
RA Chai E.C., Kang M., Dimova L.G., Schimmel A.W.M., Tietjen I., Radomski C.,
RA Tan L.J., Thiam C.H., Narayanaswamy P., Wu D.H., Dorninger F., Yakala G.K.,
RA Barhdadi A., Angeli V., Dube M.P., Berger J., Dallinga-Thie G.M.,
RA Tietge U.J.F., Wenk M.R., Hayden M.R., Hovingh G.K., Singaraja R.R.;
RT "ABCA8 Regulates Cholesterol Efflux and High-Density Lipoprotein
RT Cholesterol Levels.";
RL Arterioscler. Thromb. Vasc. Biol. 37:2147-2155(2017).
RN [8]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29300488; DOI=10.1021/acs.molpharmaceut.7b00679;
RA Sasaki K., Tachikawa M., Uchida Y., Hirano S., Kadowaki F., Watanabe M.,
RA Ohtsuki S., Terasaki T.;
RT "ATP-Binding Cassette Transporter A Subfamily 8 Is a Sinusoidal Efflux
RT Transporter for Cholesterol and Taurocholate in Mouse and Human Liver.";
RL Mol. Pharm. 15:343-355(2018).
CC -!- FUNCTION: Mediates cholesterol and taurocholate efflux. Through the
CC interaction with ABCA1 potentiates the cholesterol efflux to lipid-free
CC APOA1, in turn regulates high-density lipoprotein cholesterol levels.
CC {ECO:0000250|UniProtKB:O94911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O94911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000250|UniProtKB:O94911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O94911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:O94911};
CC -!- ACTIVITY REGULATION: Cholesterol efflux is increased by extracellularly
CC applied taurocholate. {ECO:0000250|UniProtKB:O94911}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O94911};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O94911}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:Q8K440}. Note=Predominantly
CC expressed on the sinusoidal plasma membrane.
CC {ECO:0000250|UniProtKB:Q8K440}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, heart, liver, skeletal muscle
CC and testis (PubMed:12532264, PubMed:16445568). Highly expressed in the
CC liver, and is also abundant in heart and skeletal muscle
CC (PubMed:28882873). Highly expressed in heart (PubMed:29300488).
CC {ECO:0000269|PubMed:12532264, ECO:0000269|PubMed:16445568,
CC ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at 17 dpc.
CC {ECO:0000269|PubMed:12532264}.
CC -!- INDUCTION: Down-regulated by digoxin. {ECO:0000269|PubMed:16445568}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27576.1; Type=Frameshift; 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; AF498360; AAM90906.1; -; mRNA.
DR EMBL; AY732492; AAU81985.1; -; mRNA.
DR EMBL; AL603792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026496; AAH26496.1; -; mRNA.
DR EMBL; BC060032; AAH60032.1; -; mRNA.
DR EMBL; AK031843; BAC27576.1; ALT_FRAME; mRNA.
DR RefSeq; NP_694785.3; NM_153145.4.
DR AlphaFoldDB; Q8K442; -.
DR SMR; Q8K442; -.
DR BioGRID; 229875; 5.
DR STRING; 10090.ENSMUSP00000097860; -.
DR GlyGen; Q8K442; 3 sites.
DR iPTMnet; Q8K442; -.
DR PhosphoSitePlus; Q8K442; -.
DR SwissPalm; Q8K442; -.
DR MaxQB; Q8K442; -.
DR PaxDb; Q8K442; -.
DR PRIDE; Q8K442; -.
DR ProteomicsDB; 285948; -.
DR DNASU; 217258; -.
DR Ensembl; ENSMUST00000100287; ENSMUSP00000097860; ENSMUSG00000041828.
DR Ensembl; ENSMUST00000106664; ENSMUSP00000102275; ENSMUSG00000041828.
DR GeneID; 217258; -.
DR KEGG; mmu:217258; -.
DR CTD; 217258; -.
DR MGI; MGI:2386846; Abca8a.
DR VEuPathDB; HostDB:ENSMUSG00000041828; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162012; -.
DR InParanoid; Q8K442; -.
DR OMA; SDQGIMN; -.
DR PhylomeDB; Q8K442; -.
DR TreeFam; TF105192; -.
DR BioGRID-ORCS; 217258; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Abca8a; mouse.
DR PRO; PR:Q8K442; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K442; protein.
DR Bgee; ENSMUSG00000041828; Expressed in sciatic nerve and 159 other tissues.
DR ExpressionAtlas; Q8K442; baseline and differential.
DR Genevisible; Q8K442; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042908; P:xenobiotic transport; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR030372; ABCA8.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF186; PTHR19229:SF186; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1620
FT /note="ABC-type organic anion transporter ABCA8A"
FT /id="PRO_0000250678"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1068..1088
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1133..1153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1159..1179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1196..1216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 478..713
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1284..1517
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1322..1329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 449
FT /note="R -> S (in Ref. 1; AAM90906 and 2; AAU81985)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="T -> A (in Ref. 4; BAC27576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1620 AA; 184180 MW; ED455820ACB6D7B6 CRC64;
MVKREINVCQ QTWALLCKNL LRKKRLKRDT FLEFLYTALI LLSLILFLQL HEVYDFSSLP
DVDLGRIDSF NDSTFMIVYT PITPTTQRIM DRVSLVSYMT GRKILASPNE ENMTELISMR
FSDVVGVIFT NAYSYNLKFI KGARIPTIKE HQDHTAHCHS YGEIIYCGLS EFWRDGFVAL
QAAINAAIIE VTTNHSVMEE MMSLTGKYIK IDSFVGQEGT TTDCFLFFCI IRFSPLTYYI
SAGVTRERKK MKGLMAVMGL RDSAFWLSWG LLYGVIVFVV TLLSTTIVKL VQFVFLTGFM
VIFSLFFFYG LSLISLSFLM SVLLKKSFLT DLVVFLLTVS CGSLGFTALY RYLPVSLEWL
LSLLSPFAFM LGMVQLLRLD YDVNSNADPM GNPNEVIGTI FMLFFDGVFY LLLTFYFEKV
LPSKSFHDKT YWHACKSHFF LIDYSFYIRT ALDNETDYEF SDDSFEPVSM EFHGKEAIRI
RNLTKDYIQK SKRTEALKDL TLDVYKGQIT AILGHSGAGK STLLNVLSGL CVPTKGWVTI
HNNKLSEMTD LENISKLTGV CPQCNVQFDF LTVRENLRLF AKIKGIQAHE VDNEVQRVLL
ELDMKNTQNI LVQNLSGGQK RKLTFGIAIL GDPQIFLLDE PTAGLDPFSR HRVWNFLKER
RADRVVLFST QFMDEADILA DRKVFISKGK LKCAGSSLFL KKKWGIGYHL SLQLSETCVH
ERITSLVKQH IPDSKLSAES EGKLSYILPL ERTNKFPDLY RDLERSPDLG IENYGVSITT
LTEVFLKLEG KSSIDQSDIG MTEDVQAGGA RSPERFAEVE QLVSLLNGRC KMKGGMALWW
QQLCAVTRLR FLKLKHERKS IVILILVLGI GLLHILSANI YRMVRQSDYC WELAPHMYFL
TPGQQPQPPL TNLLIVNKTG AKIDDFIHSL EQQNIALEVD AFGTRNGTED SQYNGAIILS
GDEKNYNFTL ACNTKRLNCF PVLVDIVSNG LLGLFAPSAH IQTDRSTFPE ENDHRKFDYL
AYFFLWVLLM ACVPPYISMT SIDDYKNRAQ FQLWISGLSP SAYWFGQALF EVPVYCALIL
SIFIAFYASA PPESKFTVGD LFIQILYVGG YAMSVIFMTY VISFIYRKGR KNSGLWSLCF
YIVSFFSMCF MLIDYFRDIS LFVLIALVPP ATLGGCTLLH FENREFSEII FEPEREYSYL
FFLAPLLHFA IFVVILRCME RKFGMKTMRT DPVFRISPRS DRVFNNPEDP DGEDEDVSQE
RVWTANALTS ADFQEKPAII ASCLRKEYKG KKKCFVLKSK KKIATRNISF CVRKGEVVGL
LGHNGAGKST SIKMITGETK PSAGQVLLKG SSTGDTPGFL GYCPQENALW LNLTVREHLE
IFAAIKGMRK SDANVAIERL ADALKLQDQL KSPVKTLSEG VKRKLCFVLS ILGNPSVVLL
DEPSTGMDPE GQQQMWQAIQ ATFSNTERGA LLTTHYMAEA EAVCDRVAIM VSGRLRCIGS
IQHLKSKFGK EYLLEMKVKT PSQVEPLNTE IMRLFPQAAR QERYSSLMVY KLPREDVQPL
SQAFFKLETV KQSFDLEEYS LSQSTLEQVF LELSKEQELD GFEEELDPSV KWKLLPQEEA
