ABCA2_RAT
ID ABCA2_RAT Reviewed; 2434 AA.
AC Q9ESR9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP-binding cassette sub-family A member 2 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q9BZC7};
DE AltName: Full=ATP-binding cassette transporter 2;
DE Short=ATP-binding cassette 2;
GN Name=Abca2 {ECO:0000312|RGD:620238};
GN Synonyms=Abc2 {ECO:0000312|RGD:620238};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB16596.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Brain {ECO:0000312|EMBL:BAB16596.1};
RX PubMed=10970803; DOI=10.1042/bj3500865;
RA Zhao L.-X., Zhou C.-J., Tanaka A., Nakata M., Hirabayashi T., Amachi T.,
RA Shioda S., Ueda K., Inagaki N.;
RT "Cloning, characterization and tissue distribution of the rat ATP-binding
RT cassette (ABC) transporter ABC2/ABCA2.";
RL Biochem. J. 350:865-872(2000).
RN [2]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11157071; DOI=10.1523/jneurosci.21-03-00849.2001;
RA Zhou C., Zhao L., Inagaki N., Guan J., Nakajo S., Hirabayashi T.,
RA Kikuyama S., Shioda S.;
RT "Atp-binding cassette transporter ABC2/ABCA2 in the rat brain: a novel
RT mammalian lysosome-associated membrane protein and a specific marker for
RT oligodendrocytes but not for myelin sheaths.";
RL J. Neurosci. 21:849-857(2001).
RN [3]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12210128; DOI=10.1002/cne.10354;
RA Zhou C.J., Inagaki N., Pleasure S.J., Zhao L.X., Kikuyama S., Shioda S.;
RT "ATP-binding cassette transporter ABCA2 (ABC2) expression in the developing
RT spinal cord and PNS during myelination.";
RL J. Comp. Neurol. 451:334-345(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17240058; DOI=10.1016/j.neulet.2006.12.028;
RA Saito T., Yamada K., Wang Y., Tanaka Y., Ohtomo K., Ishikawa K.,
RA Inagaki N.;
RT "Expression of ABCA2 protein in both non-myelin-forming and myelin-forming
RT Schwann cells in the rodent peripheral nerve.";
RL Neurosci. Lett. 414:35-40(2007).
RN [5]
RP FUNCTION.
RX PubMed=22086926; DOI=10.1074/jbc.m111.288258;
RA Michaki V., Guix F.X., Vennekens K., Munck S., Dingwall C., Davis J.B.,
RA Townsend D.M., Tew K.D., Feiguin F., De Strooper B., Dotti C.G., Wahle T.;
RT "Down-regulation of the ATP-binding cassette transporter 2 (Abca2) reduces
RT amyloid-beta production by altering Nicastrin maturation and intracellular
RT localization.";
RL J. Biol. Chem. 287:1100-1111(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1327; SER-1331 AND THR-2411,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [8]
RP FUNCTION.
RX PubMed=24201375; DOI=10.1016/j.bbalip.2013.10.019;
RA Davis W. Jr.;
RT "The ATP-binding cassette transporter-2 (ABCA2) regulates esterification of
RT plasma membrane cholesterol by modulation of sphingolipid metabolism.";
RL Biochim. Biophys. Acta 1841:168-179(2014).
CC -!- FUNCTION: Probable transporter, its natural substrate has not been
CC found yet. May have a role in macrophage lipid metabolism and neural
CC development. May play a role in myelination, perhaps as a transporter
CC for certain kinds of myelin chemical components (PubMed:12210128). May
CC play an important role in gamma-secretase processing of APP and thus in
CC amyloid-beta peptide generation (PubMed:22086926). Regulates
CC esterification of plasma membrane cholesterol by modulation of
CC sphingolipid metabolism (PubMed:24201375).
CC {ECO:0000269|PubMed:12210128, ECO:0000269|PubMed:22086926,
CC ECO:0000269|PubMed:24201375, ECO:0000305}.
CC -!- FUNCTION: Probable lipid transporter that modulates cholesterol
CC sequestration in the late endosome/lysosome by regulating the
CC intracellular sphingolipid metabolism, in turn participates in
CC cholesterol homeostasis (PubMed:24201375). May alter the transbilayer
CC distribution of ceramide in the intraluminal membrane lipid bilayer,
CC favoring its retention in the outer leaflet that results in increased
CC acid ceramidase activity in the late endosome/lysosome, facilitating
CC ceramide deacylation to sphingosine leading to the sequestration of
CC free cholesterol in lysosomes (By similarity). In addition regulates
CC amyloid-beta production either by activating a signaling pathway that
CC regulates amyloid precursor protein transcription through the
CC modulation of sphingolipid metabolism or through its role in gamma-
CC secretase processing of APP (PubMed:22086926). May play a role in
CC myelin formation (PubMed:12210128). {ECO:0000250|UniProtKB:Q9BZC7,
CC ECO:0000269|PubMed:12210128, ECO:0000269|PubMed:22086926,
CC ECO:0000269|PubMed:24201375}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9BZC7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BZC7}. Lysosome
CC membrane {ECO:0000269|PubMed:11157071, ECO:0000269|PubMed:12210128};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BZC7}. Note=Forms
CC discrete, punctate intracellular vesicles.
CC {ECO:0000250|UniProtKB:Q9BZC7}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, at moderate
CC levels in heart, kidney and lung, and at low levels in skeletal muscle,
CC stomach, spleen, colon and pancreas (PubMed:10970803). Not detected in
CC the liver or small intestine (PubMed:10970803). In brain, highly
CC expressed in white matter and detected in oligodendrocytes
CC (PubMed:10970803, PubMed:11157071). Expressed in cerebellum as well as
CC the anterior commissure (PubMed:11157071). Expressed mainly in the
CC white matter but is also scattered in gray matter throughout the whole
CC brain (PubMed:11157071). Expressed in myelinating cells of both ventral
CC and dorsal restricted regions in newborn spinal cord (PubMed:12210128).
CC Expressed in non-myelin-forming as well as in myelin-forming Schwann
CC cells in the sciatic nerve (PubMed:17240058).
CC {ECO:0000269|PubMed:10970803, ECO:0000269|PubMed:11157071,
CC ECO:0000269|PubMed:12210128, ECO:0000269|PubMed:17240058}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10970803}.
CC -!- PTM: Methylated at Gln-271 by N6AMT1. {ECO:0000250|UniProtKB:Q9BZC7}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AB037937; BAB16596.1; -; mRNA.
DR RefSeq; NP_077372.1; NM_024396.1.
DR AlphaFoldDB; Q9ESR9; -.
DR SMR; Q9ESR9; -.
DR BioGRID; 249446; 1.
DR STRING; 10116.ENSRNOP00000020339; -.
DR GlyGen; Q9ESR9; 25 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9ESR9; -.
DR PhosphoSitePlus; Q9ESR9; -.
DR jPOST; Q9ESR9; -.
DR PaxDb; Q9ESR9; -.
DR PRIDE; Q9ESR9; -.
DR GeneID; 79248; -.
DR KEGG; rno:79248; -.
DR UCSC; RGD:620238; rat.
DR CTD; 20; -.
DR RGD; 620238; Abca2.
DR eggNOG; KOG0059; Eukaryota.
DR InParanoid; Q9ESR9; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q9ESR9; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR PRO; PR:Q9ESR9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0099038; F:ceramide floppase activity; ISO:RGD.
DR GO; GO:0061135; F:endopeptidase regulator activity; ISO:RGD.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; ISO:RGD.
DR GO; GO:0032289; P:central nervous system myelin formation; IDA:UniProtKB.
DR GO; GO:0099040; P:ceramide translocation; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0001573; P:ganglioside metabolic process; ISS:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0090370; P:negative regulation of cholesterol efflux; ISO:RGD.
DR GO; GO:0150110; P:negative regulation of cholesterol esterification; ISO:RGD.
DR GO; GO:0032384; P:negative regulation of intracellular cholesterol transport; ISO:RGD.
DR GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; IDA:ARUK-UCL.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:1905601; P:negative regulation of receptor-mediated endocytosis involved in cholesterol transport; ISO:RGD.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0045939; P:negative regulation of steroid metabolic process; IMP:ARUK-UCL.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; ISO:RGD.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:ARUK-UCL.
DR GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; ISO:RGD.
DR GO; GO:0010872; P:regulation of cholesterol esterification; ISS:UniProtKB.
DR GO; GO:0032383; P:regulation of intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:1901873; P:regulation of post-translational protein modification; ISO:RGD.
DR GO; GO:0060049; P:regulation of protein glycosylation; ISO:RGD.
DR GO; GO:1904375; P:regulation of protein localization to cell periphery; ISO:RGD.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0070723; P:response to cholesterol; ISO:RGD.
DR GO; GO:0048545; P:response to steroid hormone; ISS:UniProtKB.
DR GO; GO:0006684; P:sphingomyelin metabolic process; ISS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; NAS: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; IPR030366; ABCA2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF225; PTHR19229:SF225; 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; Endosome; Glycoprotein; Lysosome; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2434
FT /note="ATP-binding cassette sub-family A member 2"
FT /id="PRO_0000093292"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1461..1481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1793..1813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1842..1862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1873..1893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1906..1926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1992..2012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 990..1221
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 2051..2286
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 354..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1024..1031
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 2088..2095
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 271
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZC7"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZC7"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2055
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2434 AA; 270928 MW; CD424A9C4F63513F CRC64;
MGFLHQLQLL LWKNVTLKRR SPWVLAFEIF IPLVLFFILL GLRQKKPTIS VKEAFYTAAP
LTSAGILPVM QSLCPDGQRD EFGFLQYANS TVTQLLERLN RVVEESNLFD PERPSLGSEL
EALHQRLEAL SSGPGTWESH SARPAVSSFS LDSVARDKRE LWRFLMQNLS LPNSTAQALL
AARVDPSEVY RLLFGPLPDL DGKLGFLRKQ EPWSHLGSNP LFQMEELLLA PALLEQLTCA
PGSGELGRIL TMPEGHQVDL QGYRDAVCSG QATARAQHFS DLATELRNQL DIAKIAQQLG
FNVPNGSDPQ PQAPSPQSLQ ALLGDLLDVQ KVLQDVDVLS ALALLLPQGA CAGRAPAPQA
GSPSGPANST GVGANTGPNT TVEEGTQSPV TPASPDTLQG QCSAFVQLWA GLQPILCGNN
RTIEPEALRR GNMSSLGFTS KEQRNLGLLV HLMTSNPKIL YAPAGSEADH VILKANETFA
FVGNVTHYAQ VWLNISAEIR SFLEQGRLQQ HLHWLQQYVA DLRLHPEAMN LSLDELPPAL
RLDYFSLPNG TALLQQLDTI DNAACGWIQF MSKVSVDIFK GFPDEESIVN YTLNQAYQDN
VTVFASVIFQ TRKDGSLPPH VHYKIRQNSS FTEKTNEIRR AYWRPGPNTG GRFYFLYGFV
WIQDMIERAI INTFVGHDVV EPGNYVQMFP YPCYTRDDFL FVIEHMMPLC MVISWVYSVA
MTIQHIVAEK EHRLKEVMKT MGLNNAVHWV AWFITGFVQL SISVTALTAI LKYGQVLMHS
HVLIIWLFLA VYAVATIMFC FLVSVLYSKA KLASACGGII YFLSYVPYMY VAIREEVAHD
KITAFEKCIA SLMSTTAFGL GSKYFALYEV AGVGIQWHTF SQSPVEGDDF NLLLAVTMLM
VDTVVYGVLT WYIEAVHPGM YGLPRPWYFP LQKSYWLGSG RTETWEWSWP WAHAPRLSVM
EEDQACAMES RHFEETRGME EEPTHLPLVV CVDKLTKVYK NDKKLALNKL SLNLYENQVV
SFLGHNGAGK TTTMSILTGL FPPTSGSATI YGHDIRTEMD EIRKNLGMCP QHNVLFDQLT
VEEHLWFYSR LKSMAQEEIR KEMDKMIEDL ELSNKRHSLV QTLSGGMKRK LSVAIAFVGG
SRAIILDEPT AGVDPYARRA IWDLILKYKP GRTILLSTHH MDEADLLGDR IAIISHGKLK
CCGSPLFLKG AYGDGYRLTL VKRPAEPGTS QEPGMASSPS GRPQLSNCSE MQVSQFIRKH
VASSLLVSDT STELSYILPS EAVKKGAFER LFQQLEHSLD ALHLSSFGLM DTTLEEVFLK
VSEEDQSLEN SEADVKESRK DALPGAEGLT AVESQAGNLA RCSELAQSQA SLQSASSVGS
ARGDEGAGYT DGYGDYRPLF DNLQDPDSVS LQEAEMEALA RVGQGSRKLE GWWLKMRQFH
GLLVKRFHCA RRNSKALCSQ ILLPAFFVCV AMTVALSVPE IGDLPPLVLS PSQYHNYTQP
RGNFIPYANE ERREYRLRLS PDASPQQLVS TFRLPSGVGA TCVLKSPANG SLGPMLNLSS
GESRLLAARF FDSMCLESFT QGLPLSNFVP PPPSPAPSDS PLSPDEDSLL AWNTSLPPTA
GPETWTWAPS LPRLVHEPVR CTCSAQGTGF SCPSSVGGHP PQMRVVTGDI LTDITGHNVS
EYLLFTSDRF RLHRYGAITF GNIQKSIPAP IGTRTPLMVR KIAVRRVAQV LYNNKGYHSM
PTYLNSLNNA ILRANLPKSK GNPAAYGITV TNHPMNKTSA SLSLDYLLQG TDVVIAIFII
VAMSFVPASF VVFLVAEKST KAKHLQFVSG CNPVIYWLAN YVWDMLNYLV PATCCIIILF
VFDLPAYTSP TNFPAVLSLF LLYGWSITPI MYPASFWFEV PSSAYVFLIV INLFIGITAT
VATFLLQLFE HDKDLKVVNS YLKSCFLIFP NYNLGHGLME IAYNEYINEY YAKIGQFDKM
KSPFEWDIVT RGLVAMTVEG FVGFFLTIMC QYNFLRQPQR LPVSTKPVED DVDVASERQR
VLRGDADNDM VKIENLTKVY KSRKIGRILA VDRLCLGVRP GECFGLLGVN GAGKTSTFKM
LTGDESTTGG EAFVNGHSVL KDLLQVQQSL GYCPQFDALF DELTAREHLQ LYTRLRGIPW
KDEAQVVRWA LEKLELTKCA DKPAGSYSGG NKRKLSTAIA LIGYPAFIFL DEPTTGMDPK
ARRFLWNLIL DLIKTGRSVV LTSHSMEECE AVCTRLAIMV NGRLRCLGSI QHLKNRFGDG
YMITVRTKSS QNVKDVVRFF NRNFPEAMLK ERHHTKVQYQ LKSEHISLAQ VFSKMEHVVG
VLGIEDYSVS QTTLDNVFVN FAKKQSDNVE QQEAEPSTLP SPLGLLSLLR PRPAPTELRA
LVADEPEDLD TEDEGLISFE EERAQLSFNT DTLC
