ABC8B_MOUSE
ID ABC8B_MOUSE Reviewed; 1620 AA.
AC Q8K440; A2AM55; Q69ZY4; Q8BRQ1; Q9JL38;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ABC-type organic anion transporter ABCA8B {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O94911};
DE AltName: Full=ATP-binding cassette sub-family A member 8B {ECO:0000305};
GN Name=Abca8b {ECO:0000312|MGI:MGI:1351668}; Synonyms=Abca8, Kiaa0822;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP 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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
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 1415-1620 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1433-1620 (ISOFORMS 1/2).
RX PubMed=10708515; DOI=10.1006/geno.1999.6102;
RA Schriml L.M., Dean M.;
RT "Identification of 18 mouse ABC genes and characterization of the ABC
RT superfamily in Mus musculus.";
RL Genomics 64:24-31(2000).
RN [6]
RP INDUCTION.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, and Lung;
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 [8]
RP FUNCTION, AND 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 [9]
RP TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
RP LOCATION.
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
CC (PubMed:28882873). Through the interaction with ABCA1 potentiates the
CC cholesterol efflux to lipid-free APOA1, in turn regulates high-density
CC lipoprotein cholesterol levels (By similarity).
CC {ECO:0000250|UniProtKB:O94911, ECO:0000269|PubMed:28882873}.
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:0000269|PubMed:29300488}. Note=Predominantly
CC expressed on the sinusoidal plasma membrane in hepatocytes.
CC {ECO:0000269|PubMed:29300488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K440-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K440-2; Sequence=VSP_020704;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver and skeletal
CC muscle (PubMed:12532264). Highly expressed in the liver, and is also
CC abundant in heart and skeletal muscle (PubMed:28882873). Highly
CC expressed in liver (PubMed:29300488). {ECO:0000269|PubMed:12532264,
CC ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
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=BAD32312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF498362; AAM90908.1; -; mRNA.
DR EMBL; AK173034; BAD32312.1; ALT_INIT; mRNA.
DR EMBL; AL807245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK043744; BAC31640.1; -; mRNA.
DR EMBL; AF213393; AAF31432.1; -; mRNA.
DR CCDS; CCDS25587.1; -. [Q8K440-1]
DR CCDS; CCDS88278.1; -. [Q8K440-2]
DR RefSeq; NP_038879.2; NM_013851.2. [Q8K440-1]
DR RefSeq; XP_006533522.1; XM_006533459.3. [Q8K440-1]
DR RefSeq; XP_006533525.1; XM_006533462.3.
DR RefSeq; XP_006533526.1; XM_006533463.3. [Q8K440-2]
DR AlphaFoldDB; Q8K440; -.
DR BioGRID; 205211; 8.
DR IntAct; Q8K440; 1.
DR MINT; Q8K440; -.
DR STRING; 10090.ENSMUSP00000020948; -.
DR GlyGen; Q8K440; 1 site.
DR iPTMnet; Q8K440; -.
DR PhosphoSitePlus; Q8K440; -.
DR SwissPalm; Q8K440; -.
DR jPOST; Q8K440; -.
DR MaxQB; Q8K440; -.
DR PaxDb; Q8K440; -.
DR PRIDE; Q8K440; -.
DR ProteomicsDB; 285897; -. [Q8K440-1]
DR ProteomicsDB; 285898; -. [Q8K440-2]
DR Antibodypedia; 31802; 139 antibodies from 27 providers.
DR DNASU; 27404; -.
DR Ensembl; ENSMUST00000020948; ENSMUSP00000020948; ENSMUSG00000020620. [Q8K440-1]
DR Ensembl; ENSMUST00000106669; ENSMUSP00000102280; ENSMUSG00000020620. [Q8K440-2]
DR GeneID; 27404; -.
DR KEGG; mmu:27404; -.
DR UCSC; uc007mdb.2; mouse. [Q8K440-1]
DR UCSC; uc007mdc.2; mouse. [Q8K440-2]
DR CTD; 27404; -.
DR MGI; MGI:1351668; Abca8b.
DR VEuPathDB; HostDB:ENSMUSG00000020620; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162012; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8K440; -.
DR OMA; IMTTHFL; -.
DR PhylomeDB; Q8K440; -.
DR TreeFam; TF105192; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 27404; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8K440; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K440; protein.
DR Bgee; ENSMUSG00000020620; Expressed in lumbar dorsal root ganglion and 86 other tissues.
DR ExpressionAtlas; Q8K440; baseline and differential.
DR Genevisible; Q8K440; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA: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:0005743; C:mitochondrial inner membrane; HDA:MGI.
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; ISO:MGI.
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:SF148; PTHR19229:SF148; 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW Lipid transport; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1620
FT /note="ABC-type organic anion transporter ABCA8B"
FT /id="PRO_0000250679"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1023..1043
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1069..1089
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1164..1184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 479..714
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1283..1516
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 515..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1321..1328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 313..374
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_020704"
FT CONFLICT 985
FT /note="D -> G (in Ref. 1; AAM90908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1447
FT /note="D -> V (in Ref. 5; AAF31432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1620 AA; 183039 MW; 4330378E6D820B62 CRC64;
MIKREISVRQ QTCALLQKNL LKKWRLKRES LMEWVSSLLL LLFLYWYPHG HGATDLSSVP
TKDLGRVDSF RQSGFMIGYT PVTSMTQQIM EKVAATPFMA DKKVLGLLDE ENIKELTESH
AEIIRVIFSD TFSYHLKFQF DQRIPTSREL RDHNAHCDGL YEDVNCLIAI FWKEGFVALQ
AAINAAIIET TTNHSVMEEL LSVSGKFMKI HPFVRQEGIL TDFFIFTCII SFSPITYYVS
INVARERKRM KGLMMMMGLR DPAFWLSWGL LYAGFVFIMA LSLALVIKSV QFFILTSFMV
VFSLFLLYGL SMITLAFLMS ALVRKSVLTG LSVFLLTIFW GSLGFTSLYR YLPAPVEWTL
SLFSPFAFTL GMAQLLRVDY DLNSNAPPDP ASGSNLIIAT NFMLVFDAFL YLALMMYFEK
VLPNEYGHQH SPLFFLKSSF WLQTRKPAHV ILEDGIDPVP SSGDSFEPVS PEFHGKESIR
IRNISKEYKG KPNKIEALKD LTLDIYEGQI TAVLGHSGAG KSTLLNILSG LSVPTKGSVT
IYNNNLSEMA DLENILRIAG VCPQANVQFD FLTVRENLRL FAKIRGIPPQ DVEKEVQRVL
LELEMKNIQN ILAQNLSGGQ KRKLTFGIAI LGDSQIFLLD EPTAGLDPFS RHRVWNLLKE
RRADRVVLFS TQFMDEADIL ADRKVFISNG RLKCAGSSLF LKKKWGVGYH LSLQLKEVCV
PENITSLVKQ HIPAAKLSAE GEGKLLYTLP LETTYRFPEL CQSLDSCPGL GIENYGVSMT
TLNEVFLKLE GKASIDEPEV DIVGEGQTER SGDTERLMEM EQTLSSLRET EKTDGMALWR
QQTCAIAKVR LLKLKHERKT LLSVLLILVV GICPFLFENI STKIRQSSYT WELSPHDYFL
APGQQPQGML TQLLIINKTE ASIDDFIHSV ERQNIALEVD ASGTRDGTDD PSYNGALIVS
GNEKNHSFSF ACNTKRLNCF PVLMDILSNG LLGMVKPSAR IQTDRSTYLM DETIHPLEDL
WKTAFWLILT SACPPYIAMS SVTDYKNRAW FQLRVSGLFP SAYWVGQAMV DIPLYCFVFL
FMSLMDYLFR FPDTMFSIIS HVIQIPCSVG YAISLIFLTY VISFISRKGK KNSGIWSLSF
YIITVFSVAV ILLAFDVDGT QYYIIFLIPP STLVGCLILS LHLFIGQIFE EGQVIEPFLV
FLIPFLHVFI FIFTLRCLEW KFGKKTMRKD PIFRISPRNN DVYQNPEEPE DEDEDVQMER
MRTANALVST SFDEKPVIIA SCLRKEYAGK QKHCLSKKKA KIATRNVSFC VRKGEILGLL
GHNGAGKSTS LKMISGDTKV TAGQVLLKGS REGDTPGFLG YCPQENALWP NLTVKEHLEI
FAAVRGLRKS HAAVAITRLA DALKLQDQLK SPVKTLSEGV KRKLCFVLSI LGNPSILLLD
EPSTGLDPEG QQQIWQAIRA IIKNTDRGAL LTTHYMAEAE ALCDRVAILV SGRLRCIGSI
QHLKSKFGKD YLLEMKVKTL EQVEPLNTEI LRLFPQASRQ ERYSSLMAYK LPVEAVQPLS
QAFFKLEKVK QTFDLEEYSL SQSTLEQVFL ELSKEQELDG LELEELDSSI KWKLLPQEEA
