ABCA2_MOUSE
ID ABCA2_MOUSE Reviewed; 2434 AA.
AC P41234;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 4.
DT 03-AUG-2022, entry version 160.
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|MGI:MGI:99606}; Synonyms=Abc2;
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].
RC STRAIN=DBA/2J;
RA Chimini G.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 964-2434.
RC STRAIN=DBA/2J; TISSUE=Macrophage;
RX PubMed=8088782; DOI=10.1006/geno.1994.1237;
RA Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
RT "Cloning of two novel ABC transporters mapping on human chromosome 9.";
RL Genomics 21:150-159(1994).
RN [3]
RP 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 [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17488728; DOI=10.1074/jbc.m611056200;
RA Sakai H., Tanaka Y., Tanaka M., Ban N., Yamada K., Matsumura Y.,
RA Watanabe D., Sasaki M., Kita T., Inagaki N.;
RT "ABCA2 deficiency results in abnormal sphingolipid metabolism in mouse
RT brain.";
RL J. Biol. Chem. 282:19692-19699(2007).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17060448; DOI=10.1128/mcb.01824-06;
RA Mack J.T., Beljanski V., Soulika A.M., Townsend D.M., Brown C.B., Davis W.,
RA Tew K.D.;
RT "'Skittish' Abca2 knockout mice display tremor, hyperactivity, and abnormal
RT myelin ultrastructure in the central nervous system.";
RL Mol. Cell. Biol. 27:44-53(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1327 AND SER-1331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1327; SER-1331 AND THR-2411,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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).
RN [8]
RP FUNCTION.
RX PubMed=22748276; DOI=10.1016/j.atherosclerosis.2012.05.039;
RA Calpe-Berdiel L., Zhao Y., de Graauw M., Ye D., van Santbrink P.J.,
RA Mommaas A.M., Foks A., Bot M., Meurs I., Kuiper J., Mack J.T., Van Eck M.,
RA Tew K.D., van Berkel T.J.;
RT "Macrophage ABCA2 deletion modulates intracellular cholesterol deposition,
RT affects macrophage apoptosis, and decreases early atherosclerosis in LDL
RT receptor knockout mice.";
RL Atherosclerosis 223:332-341(2012).
RN [9]
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).
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:17488728, PubMed:22748276). May alter
CC the transbilayer distribution of ceramide in the intraluminal membrane
CC lipid bilayer, favoring its retention in the outer leaflet that results
CC in increased acid ceramidase activity in the late endosome/lysosome,
CC facilitating ceramide deacylation to sphingosine leading to the
CC sequestration of free cholesterol in lysosomes (By similarity). In
CC addition regulates amyloid-beta production either by activating a
CC signaling pathway that regulates amyloid precursor protein
CC transcription through the modulation of sphingolipid metabolism or
CC through its role in gamma-secretase processing of APP
CC (PubMed:22086926). May play a role in myelin formation
CC (PubMed:17060448). {ECO:0000250|UniProtKB:Q9BZC7,
CC ECO:0000269|PubMed:17060448, ECO:0000269|PubMed:17488728,
CC ECO:0000269|PubMed:22086926, ECO:0000269|PubMed:22748276}.
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}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9BZC7}. Note=Forms discrete, punctate
CC intracellular vesicles. {ECO:0000250|UniProtKB:Q9BZC7}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest levels
CC are found in brain and pregnant uterus. Higly expressed in
CC oligodendrocytes and weakly in the cerebral cortex. Highly expressed in
CC some large pyramidal cells in layer V (PubMed:17488728).
CC {ECO:0000269|PubMed:17488728}.
CC -!- PTM: Methylated at Gln-271 by N6AMT1. {ECO:0000250|UniProtKB:Q9BZC7}.
CC -!- DISRUPTION PHENOTYPE: Homozygote knockout mice for the ABCA2 gene are
CC viable and fertile (PubMed:17488728, PubMed:17060448). Mice are born at
CC the expected Mendelian ratio and exhibit a phenotype including lower
CC pregnancy rate and body weight, shorter latency period on the balance
CC beam, and sensitization to environmental stress compared with wild type
CC mice (PubMed:17488728). Homozygote knockout males and females are
CC viable and fertile. However, a non-Mendelian inheritance pattern is
CC found among male progeny of heterozygous crosses. Mice display a tremor
CC without ataxia, hyperactivity, and reduced body weight; the latter two
CC phenotypes are more marked in females than in males (PubMed:17060448).
CC {ECO:0000269|PubMed:17060448, ECO:0000269|PubMed:17488728}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; X75927; CAA53531.2; -; mRNA.
DR PIR; B54774; B54774.
DR AlphaFoldDB; P41234; -.
DR SMR; P41234; -.
DR STRING; 10090.ENSMUSP00000099983; -.
DR GlyConnect; 2140; 5 N-Linked glycans (4 sites).
DR GlyGen; P41234; 25 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; P41234; -.
DR PhosphoSitePlus; P41234; -.
DR EPD; P41234; -.
DR MaxQB; P41234; -.
DR PaxDb; P41234; -.
DR PRIDE; P41234; -.
DR ProteomicsDB; 285950; -.
DR MGI; MGI:99606; Abca2.
DR eggNOG; KOG0059; Eukaryota.
DR InParanoid; P41234; -.
DR PhylomeDB; P41234; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR ChiTaRS; Abca2; mouse.
DR PRO; PR:P41234; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P41234; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0099038; F:ceramide floppase activity; ISO:MGI.
DR GO; GO:0061135; F:endopeptidase regulator activity; ISO:MGI.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; ISO:MGI.
DR GO; GO:0032289; P:central nervous system myelin formation; IMP:ARUK-UCL.
DR GO; GO:0099040; P:ceramide translocation; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0001573; P:ganglioside metabolic process; IMP:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:ARUK-UCL.
DR GO; GO:0090370; P:negative regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0150110; P:negative regulation of cholesterol esterification; ISO:MGI.
DR GO; GO:0032384; P:negative regulation of intracellular cholesterol transport; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1905601; P:negative regulation of receptor-mediated endocytosis involved in cholesterol transport; ISO:MGI.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; ISO:MGI.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; ISO:MGI.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
DR GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; ISO:MGI.
DR GO; GO:0010872; P:regulation of cholesterol esterification; ISS:UniProtKB.
DR GO; GO:0032383; P:regulation of intracellular cholesterol transport; IMP:UniProtKB.
DR GO; GO:1901873; P:regulation of post-translational protein modification; ISO:MGI.
DR GO; GO:0060049; P:regulation of protein glycosylation; IMP:ARUK-UCL.
DR GO; GO:1904375; P:regulation of protein localization to cell periphery; IMP:ARUK-UCL.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:ARUK-UCL.
DR GO; GO:0019218; P:regulation of steroid metabolic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048545; P:response to steroid hormone; ISS:UniProtKB.
DR GO; GO:0006684; P:sphingomyelin metabolic process; IMP:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; ISO:MGI.
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_0000093291"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..832
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 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1600
FT /note="Pro 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:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000255"
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 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1408
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; 270509 MW; 38564C2989F0CFCC CRC64;
MGFLHQLQLL LWKNVTLKRR SPWVLAFEIF IPLVLFFILL GLRQKKPTIS VKEAFYTAAP
LTSAGILPVM QSLCPDGQRD EFGFLQYANS TVTQLLERLH RVVEEGNLFD PVRPSLGSEL
EALRQRLEAL SSGPGTWESH SARPAVSSFS LDSVARDQRE LWRFLMQNLS LPNSTAQALL
AARVDPSEVY RLLFGPLPDL DGKLGFLRKQ EPWSRLGSNP LLQMEELLLA PALLEQLTCA
PGSGELGRIL TMPEGHQVDL QGYRDAVCSG QATARAQRFS DLAAELRNQL DTAKIAQQLG
FDVPNGSDPQ PQAPSPQSLP ALLGDLLDAQ KLLQDVDVLS ALALLLPQGA CAGQASAPQA
SSLNGLANST GIGANSGSNT TVEEGTQSPV SPASPDTLQG QCSAFVQLWA GLQPILCGNN
RTIEPEALRR GNMSSLGFTS KEQRNLGLLV HLMTSNPKIL YAPVGSEADR VILKANETFA
FVGNVTHYAQ VWLNISTEIR SFLEQGRLQQ HLQWLQQYVA DLQLHPEAMN LSLEELPPAL
RQDFSLPNGT ALLQQLDTID NAACGWIQFM SKVSVDIFKG FPDEESIVNY TLNQAYQDNV
TVFASVIFQT RKDGSLPPHV HYKIRQNSSF TEKTNEIRRA YWRPGPNTGG RFYFLYGLRL
DQDMMERAII NTFVGHDVVE PGNYVQMFPY PCYTRDDFLF VIEHMMPLCM VISWVYSVAM
TIQHIVAEKE HRLKEVMKTM GLNNAVHWVA WFITGFVQLS ISVTALTAIL KYCQVLMHSH
VLIIWLFLAV YAVATIMFCF LVSVLYSKAK LASACGGIIY FLSYVPYMYV AIREEVAHDK
ITAFEKCIAS RCPQQPLAWV PSTLHCMKWQ EWASIQWHTF SQSPVEGDDF NLLLAVTMLM
VDTVVYGVLT WYIEAVHPGM YGLPRPWYSR YRSPIGWAVG GQKPGSGAGH GHTHRASALW
RRIQACAMES RHFEETRGME EEPTHLPLVV CVDKLTKVYK NDKKLALNKL SLNLYENQVV
SFLGHNGAGK TTTMSILTGL FPPTSGSATI YGHDIRTEMD EIRKNLGMCP QHNVLFDRLT
VEEHLWFYSR LKSMAQEEIR KETDKMIEDL ELSNKRHSLV QTLSGGMKRK LSVAIAFVGG
SRAIILDEPT AGVDPYARRA IWDLILKYKP GRTILLSTHH MDEADLLGDR IAIISHGKLK
CCGSPLFLKG AYGDGYRLTL VKQPAEPGTS QEPGLASSPS GCPRLSSCSE PQVSQFIRKH
VASSLLVSDT STELSYILPS EAVKKGAFER LFQQLEHSLD ALHLSSFGLM DTTLEEVFLK
VSEEDQSLEN SEADVKESRK DVLPGAEGLT AVGGQAGNLA RCSELAQSQA SLQSASSVGS
ARGEEGTGYS DGYGDYRPLF DNLQDPDNVS LQEAEMEALA QVGQGSRKLE GWWLKMRQFH
GLLVKRFHCA RRNSKALCSQ ILLPAFFVCV AMTVALSVPE IGDLPPLVLS PSQYHNYTQP
RGNFIPYANE ERQEYRLRLS PDASPQQLVS TFRLPSGVGA TCVLKSPANG SLGPMLNLSS
GESRLLAARF FDSMCLESFT QGLPLSNFVP PPPSPAPSDS PVSPDEDSLQ AWNMSLPPTA
GPETWTSAPS LPRLVHEPVR CTCSAQGTGF SCPSSVGGHP PQMRVVTGDI LTDITGHNVS
EYLLFTSDRF RLHRYGAITF GNVQKSIPAS FGARVPPMVR KIAVRRVAQV LYNNKGYHSM
PTYLNSLNNA ILRANLPKSK GNPAAYGITV TNHPMNKTSA SLSLDYLLQG TDVVIAIFII
VAMSFVPASF VVFLVAEKST KAKHLQFVSG CNPVIYWLAN YVWDMLNYLV PATCCVIILF
VFDLPAYTSP TNFPAVLSLF LLYGWSITPI MYPASFWFEV PSSAYVFLIV INLFIGITAT
VATFLLQLFE HDKDLKVVNS YLKSCFLIFP NYNLGHGLME MAYNEYINEY YAKIGQFDKM
KSPFEWDIVT RGLVAMTVEG FVGFFLTIMC QYNFLRQPQR LPVSTKPVED DVDVASERQR
VLRGDADNDM VKIENLTKVY KSRKIGRILA VDRLCLGVRP GECFGLLGVN GAGKTSTFKM
LTGDESTTGG EAFVNGHSVL KDLLQVQQSL GYCPQFDALF DELTAREHLQ LYTRLRGIPW
KDEAQVVKWA LEKLELTKYA DKPAGTYSGG NKRKLSTAIA LIGYPAFIFL DEPTTGMDPK
ARRFLWNLIL DLIKTGRSVV LTSHSMEECE ALCTRLAIMV NGRLRCLGSI QHLKNRFGDG
YMITVRTKSS QNVKDVVRFF NRNFPEAMLK ERHHTKVQYQ LKSEHISLAQ VFSKMEQVVG
VLGIEDYSVS QTTLDNVFVN FAKKQSDNVE QQEAEPSSLP SPLGLLSLLR PRPAPTELRA
LVADEPEDLD TEDEGLISFE EERAQLSFNT DTLC
