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ATP-binding cassette sub-family A member 7

 ABCA7_MOUSE             Reviewed;        2159 AA.
Q91V24; Q9JL36;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
13-FEB-2019, entry version 132.
RecName: Full=ATP-binding cassette sub-family A member 7;
Name=Abca7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=DBA/2J; TISSUE=Lymphoma;
PubMed=11435699;
Broccardo C., Osorio J., Luciani M.-F., Schriml L.M., Prades C.,
Shulenin S., Arnould I., Naudin L., Lafargue C., Rosier M., Jordan B.,
Mattei M.-G., Dean M., Denefle P., Chimini G.;
"Comparative analysis of the promoter structure and genomic
organization of the human and mouse ABCA7 gene encoding a novel ABCA
transporter.";
Cytogenet. Cell Genet. 92:264-270(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1920-2159.
STRAIN=C57BL/6J;
PubMed=10708515; DOI=10.1006/geno.1999.6102;
Schriml L.M., Dean M.;
"Identification of 18 mouse ABC genes and characterization of the ABC
superfamily in Mus musculus.";
Genomics 64:24-31(2000).
[3]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12917409; DOI=10.1074/jbc.M307831200;
Wang N., Lan D., Gerbod-Giannone M., Linsel-Nitschke P., Jehle A.W.,
Chen W., Martinez L.O., Tall A.R.;
"ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I
and mediates cellular phospholipid but not cholesterol efflux.";
J. Biol. Chem. 278:42906-42912(2003).
[4]
INDUCTION.
PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
"Acute digoxin loading reduces ABCA8A mRNA expression in the mouse
liver.";
Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
[5]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15550377; DOI=10.1074/jbc.M412602200;
Kim W.S., Fitzgerald M.L., Kang K., Okuhira K., Bell S.A.,
Manning J.J., Koehn S.L., Lu N., Moore K.J., Freeman M.W.;
"Abca7 null mice retain normal macrophage phosphatidylcholine and
cholesterol efflux activity despite alterations in adipose mass and
serum cholesterol levels.";
J. Biol. Chem. 280:3989-3995(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=16908670; DOI=10.1083/jcb.200601030;
Jehle A.W., Gardai S.J., Li S., Linsel-Nitschke P., Morimoto K.,
Janssen W.J., Vandivier R.W., Wang N., Greenberg S., Dale B.M.,
Qin C., Henson P.M., Tall A.R.;
"ATP-binding cassette transporter A7 enhances phagocytosis of
apoptotic cells and associated ERK signaling in macrophages.";
J. Cell Biol. 174:547-556(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND DISRUPTION
PHENOTYPE.
PubMed=20495215; DOI=10.1194/jlr.M006049;
Tanaka N., Abe-Dohmae S., Iwamoto N., Fitzgerald M.L., Yokoyama S.;
"Helical apolipoproteins of high-density lipoprotein enhance
phagocytosis by stabilizing ATP-binding cassette transporter A7.";
J. Lipid Res. 51:2591-2599(2010).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=26260791; DOI=10.1074/jbc.M115.655076;
Satoh K., Abe-Dohmae S., Yokoyama S., St George-Hyslop P.,
Fraser P.E.;
"ATP-binding cassette transporter A7 (ABCA7) loss of function alters
Alzheimer amyloid processing.";
J. Biol. Chem. 290:24152-24165(2015).
[11]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
DISRUPTION PHENOTYPE.
PubMed=27472885; DOI=10.3233/JAD-160456;
Fu Y., Hsiao J.H., Paxinos G., Halliday G.M., Kim W.S.;
"ABCA7 Mediates Phagocytic Clearance of Amyloid-beta in the Brain.";
J. Alzheimers Dis. 54:569-584(2016).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27030769; DOI=10.1523/JNEUROSCI.3757-15.2016;
Sakae N., Liu C.C., Shinohara M., Frisch-Daiello J., Ma L.,
Yamazaki Y., Tachibana M., Younkin L., Kurti A., Carrasquillo M.M.,
Zou F., Sevlever D., Bisceglio G., Gan M., Fol R., Knight P., Wang M.,
Han X., Fryer J.D., Fitzgerald M.L., Ohyagi Y., Younkin S.G., Bu G.,
Kanekiyo T.;
"ABCA7 Deficiency Accelerates Amyloid-beta Generation and Alzheimer's
Neuronal Pathology.";
J. Neurosci. 36:3848-3859(2016).
[13]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=28091533; DOI=10.1038/srep40273;
Nowyhed H.N., Chandra S., Kiosses W., Marcovecchio P., Andary F.,
Zhao M., Fitzgerald M.L., Kronenberg M., Hedrick C.C.;
"ATP Binding Cassette Transporter ABCA7 Regulates NKT Cell Development
and Function by Controlling CD1d Expression and Lipid Raft Content.";
Sci. Rep. 7:40273-40273(2017).
-!- FUNCTION: Probable ATP-binding cassette (ABC) transporter that
plays a role in lipid homeostasis and macrophage-mediated
phagocytosis (PubMed:12917409, PubMed:15550377, PubMed:16908670,
PubMed:27472885, PubMed:27030769, PubMed:20495215). Binds APOA1
and may function in apolipoprotein-mediated phospholipid efflux
from cells (PubMed:12917409). May also mediate cholesterol efflux
(By similarity). May regulate cellular ceramide homeostasis during
keratinocyte differentiation (By similarity). Involved in lipid
raft organization and CD1D localization on thymocytes and antigen-
presenting cells, which plays an important role in natural killer
T-cell development and activation (PubMed:28091533). Plays a role
in phagocytosis of apoptotic cells by macrophages
(PubMed:16908670). Macrophage phagocytosis is stimulated by APOA1
or APOA2, probably by stabilization of ABCA7 (PubMed:20495215).
Also involved in phagocytic clearance of amyloid-beta by microglia
cells and macrophages (PubMed:27472885). Further limits amyloid-
beta production by playing a role in the regulation of amyloid-
beta A4 precursor protein (APP) endocytosis and/or processing
(PubMed:26260791, PubMed:27030769). {ECO:0000250|UniProtKB:Q8IZY2,
ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:15550377,
ECO:0000269|PubMed:16908670, ECO:0000269|PubMed:20495215,
ECO:0000269|PubMed:26260791, ECO:0000269|PubMed:27030769,
ECO:0000269|PubMed:27472885, ECO:0000269|PubMed:28091533}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12917409,
ECO:0000269|PubMed:20495215, ECO:0000269|PubMed:26260791}; Multi-
pass membrane protein {ECO:0000255}. Golgi apparatus membrane
{ECO:0000269|PubMed:16908670}; Multi-pass membrane protein
{ECO:0000255}. Early endosome membrane
{ECO:0000269|PubMed:16908670}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:27472885}. Cell
projection, ruffle membrane {ECO:0000269|PubMed:16908670}. Cell
projection, phagocytic cup {ECO:0000269|PubMed:16908670}.
Note=Localizes to cell membrane ruffles and phagocytic cups of
macrophages stimulated with C1q or apoptotic cells. Localizes to
the cytoplasm of resting macrophages, probably in Golgi and
endosomes (PubMed:16908670). Localizes to the apical brush border
of cells in the proximal tubules of kidney (Probable).
{ECO:0000269|PubMed:16908670, ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
brain, lung, adrenal gland, spleen and hematopoietic tissues (at
protein level) (PubMed:12917409, PubMed:15550377,
PubMed:27472885). In the brain, expressed in cortex, cerebellum,
hippocampus, olfactory bulb, neurons, astrocytes and microglia (at
protein level) (PubMed:26260791). Also expressed in adipocytes and
macrophages (at protein level) (PubMed:15550377, PubMed:27472885).
Expressed in thymocytes (at protein level) (PubMed:28091533).
Highly expressed in spleen and hematopoietic tissues
(PubMed:11435699). Expressed in brain, lung, macrophages,
microglia, oligodendrocytes and neurons (PubMed:27472885).
{ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:12917409,
ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:26260791,
ECO:0000269|PubMed:27472885, ECO:0000269|PubMed:28091533}.
-!- DEVELOPMENTAL STAGE: Widely expressed during embryogenesis
(PubMed:11435699). Expressed in newborn mice with increasing
expression from 4 to 24 weeks of age (PubMed:26260791).
{ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:26260791}.
-!- INDUCTION: Up-regulated during differentiation from monocytes to
macrophages (PubMed:27472885). Down-regulated by digoxin.
{ECO:0000269|PubMed:16445568, ECO:0000269|PubMed:27472885}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:20495215}.
-!- DISRUPTION PHENOTYPE: According to one study, knockout mice are
not viable and heterozygous knockout mice display impaired
phagocytosis of apoptotic cells (PubMed:16908670). However,
another study shows that knockout mice are viable and females have
less visceral fat and lower total serum and high density
lipoprotein cholesterol level (PubMed:15550377). Knockout mice
exhibit altered lipid profile in mouse brains, compromised spatial
memory and increased BACE1 activity (PubMed:27030769). Display an
increase in amyloid-beta protein 42 (Abeta42) from 4 to 24 weeks
of age, whereas amyloid-beta protein 40 (Abeta40) is increased at
4 weeks and decreased at 24 weeks of age (PubMed:26260791).
Increased endocytotic uptake of APP into endosomes in primary
microglia cells (PubMed:26260791). Reduced phagocytic uptake of
Abeta42 and Abeta40 by microglia cells and phagocytes
(PubMed:27472885). Decreased macrophage phagocytosis in the
peritoneal cavity (PubMed:20495215). Decreased surface CD1D
expression on double positive thymocytes, on antigen-presenting
thymocytes, on peripheral antigen-presenting cells in the spleen
and on peritoneal macrophages (PubMed:28091533). Increased
accumulation of CD1D to late endosomes (PubMed:28091533). Impaired
natural killer T (NKT) cell development with a 2-fold decrease in
frequencies and total numbers of NKT cells in the thymus and a
reduction of peripheral NKT cells in spleen and liver
(PubMed:28091533). Reduced proliferation during early stages of
NKT development and reduced expression of Egr2 in NKT cells
(PubMed:28091533). Decreased number of plasma membrane lipid rafts
on thymocytes and a reduction of CAV1 and CD1D clusters in
macrophages (PubMed:28091533). RNAi-mediated knockdown reduces
phagocytosis of apoptotic cells by macrophages (PubMed:16908670).
{ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:16908670,
ECO:0000269|PubMed:20495215, ECO:0000269|PubMed:26260791,
ECO:0000269|PubMed:27030769, ECO:0000269|PubMed:27472885,
ECO:0000269|PubMed:28091533}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- CAUTION: There are conflicting results concerning the role of
ABCA7 in lipid transport. ABCA7 was described to play a role in
apolipoprotein-mediated phospholipid and cholesterol efflux when
expressed in HEK293 cells (PubMed:12917409, PubMed:27472885).
However, another report shows that ABCA7 deficiency does not
influence cholesterol and phospholipid efflux in mouse primary
macrophages, but leads to lower serum HDL cholesterol levels and a
reduction in fat mass in female mice (PubMed:15550377).
{ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:15550377,
ECO:0000269|PubMed:27472885}.
-!- SEQUENCE CAUTION:
Sequence=AAF31434.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AF287141; AAK56862.1; -; mRNA.
EMBL; AF287142; AAK56863.1; -; Genomic_DNA.
EMBL; AF213395; AAF31434.1; ALT_FRAME; mRNA.
CCDS; CCDS24004.1; -.
RefSeq; NP_038878.1; NM_013850.1.
RefSeq; XP_017169446.1; XM_017313957.1.
UniGene; Mm.103351; -.
ProteinModelPortal; Q91V24; -.
SMR; Q91V24; -.
IntAct; Q91V24; 1.
STRING; 10090.ENSMUSP00000043090; -.
iPTMnet; Q91V24; -.
PhosphoSitePlus; Q91V24; -.
SwissPalm; Q91V24; -.
EPD; Q91V24; -.
MaxQB; Q91V24; -.
PaxDb; Q91V24; -.
PRIDE; Q91V24; -.
Ensembl; ENSMUST00000043866; ENSMUSP00000043090; ENSMUSG00000035722.
Ensembl; ENSMUST00000132517; ENSMUSP00000115111; ENSMUSG00000035722.
GeneID; 27403; -.
KEGG; mmu:27403; -.
UCSC; uc007gba.1; mouse.
CTD; 10347; -.
MGI; MGI:1351646; Abca7.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00940000161439; -.
HOVERGEN; HBG050436; -.
InParanoid; Q91V24; -.
KO; K05645; -.
OrthoDB; 131191at2759; -.
Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
PRO; PR:Q91V24; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000035722; Expressed in 215 organ(s), highest expression level in dorsal pancreas.
ExpressionAtlas; Q91V24; baseline and differential.
Genevisible; Q91V24; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0097386; C:glial cell projection; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0001891; C:phagocytic cup; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005886; C:plasma membrane; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032587; C:ruffle membrane; IDA:Alzheimers_University_of_Toronto.
GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; ISO:MGI.
GO; GO:0090556; F:phosphatidylserine-translocating ATPase activity; ISO:MGI.
GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IMP:UniProtKB.
GO; GO:0034205; P:amyloid-beta formation; IMP:UniProtKB.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IDA:Alzheimers_University_of_Toronto.
GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:Alzheimers_University_of_Toronto.
GO; GO:0006869; P:lipid transport; IBA:GO_Central.
GO; GO:0007613; P:memory; IMP:Alzheimers_University_of_Toronto.
GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0045806; P:negative regulation of endocytosis; IMP:UniProtKB.
GO; GO:0018149; P:peptide cross-linking; IDA:Alzheimers_University_of_Toronto.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
GO; GO:0044857; P:plasma membrane raft organization; IMP:UniProtKB.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IMP:Alzheimers_University_of_Toronto.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:Alzheimers_University_of_Toronto.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:Alzheimers_University_of_Toronto.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
GO; GO:1902995; P:positive regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:UniProtKB.
GO; GO:0034504; P:protein localization to nucleus; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISO:MGI.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR026082; ABCA.
InterPro; IPR030369; ABCA7.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
PANTHER; PTHR19229:SF49; PTHR19229:SF49; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Disulfide bond; Endosome; Glycoprotein; Golgi apparatus;
Membrane; Nucleotide-binding; Phagocytosis; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 2159 ATP-binding cassette sub-family A member
7.
/FTId=PRO_0000250675.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 546 Extracellular. {ECO:0000250}.
TRANSMEM 547 567 Helical. {ECO:0000255}.
TRANSMEM 590 610 Helical. {ECO:0000255}.
TRANSMEM 623 643 Helical. {ECO:0000255}.
TRANSMEM 652 672 Helical. {ECO:0000255}.
TRANSMEM 678 698 Helical. {ECO:0000255}.
TRANSMEM 732 752 Helical. {ECO:0000255}.
TRANSMEM 846 866 Helical. {ECO:0000255}.
TRANSMEM 1246 1266 Helical. {ECO:0000255}.
TOPO_DOM 1267 1551 Extracellular. {ECO:0000250}.
TRANSMEM 1552 1572 Helical. {ECO:0000255}.
TRANSMEM 1598 1618 Helical. {ECO:0000255}.
TRANSMEM 1635 1655 Helical. {ECO:0000255}.
TRANSMEM 1663 1683 Helical. {ECO:0000255}.
TRANSMEM 1743 1763 Helical. {ECO:0000255}.
DOMAIN 804 1035 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1807 2039 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 838 845 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1841 1848 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 222 {ECO:0000250}.
DISULFID 1359 1373 {ECO:0000250}.
CONFLICT 1944 1944 N -> D (in Ref. 2; AAF31434).
{ECO:0000305}.
CONFLICT 2004 2004 A -> R (in Ref. 2; AAF31434).
{ECO:0000305}.
CONFLICT 2069 2069 L -> M (in Ref. 2; AAF31434).
{ECO:0000305}.
SEQUENCE 2159 AA; 236884 MW; CD2BE3FE0D8B822B CRC64;
MALGTQLMLL LWKNYTYRRR QPIQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP
LPSAGTVPWL QGLVCNVNNS CFQHPTPGEK PGVLSNFKDS LISRLLADTR TVLGGHSIQD
MLDALGKLIP VLRAVGGGAR PQESDQPTSQ GSVTKLLEKI LQRASLDPVL GQAQDSMRKF
SDAIRDLAQE LLTLPSLMEL RALLRRPRGS AGSLELVSEA LCSTKGPSSP GGLSLNWYEA
NQLNEFMGPE VAPALPDNSL SPACSEFVGT LDDHPVSRLL WRRLKPLILG KILFAPDTNF
TRKLMAQVNQ TFEELALLRD LHELWGVLGP QIFNFMNDST NVAMLQRLLD VGGTGQRQQT
PRAQKKLEAI KDFLDPSRGG YSWREAHADM GRLAGILGQM MECVSLDKLE AVPSEEALVS
RALELLGERR LWAGIVFLSP EHPLDPSELS SPALSPGHLR FKIRMDIDDV TRTNKIRDKF
WDPGPSADPF MDLRYVWGGF VYLQDLLEQA AVRVLGGGNS RTGLYLQQMP HPCYVDDVFL
RVLSRSLPLF LTLAWIYSVA LTVKAVVREK ETRLRETMRA MGLSRAVLWL GWFLSCLGPF
LVSAALLVLV LKLGNILPYS HPVVIFLFLA AFAVATVAQS FLLSAFFSRA NLAAACGGLA
YFALYLPYVL CVAWRERLHL GGLLAASLLS PVAFGFGCES LALLEEQGDG AQWHNLGTGP
AEDVFSLAQV SAFLLLDAVI YGLALWYLEA VCPGQYGIPE PWNFPFRRSY WCGPGPPKSS
VLAPAPQDPK VLVEEPPLGL VPGVSIRGLK KHFRGCPQPA LQGLNLDFYE GHITAFLGHN
GAGKTTTLSI LSGLFPPSSG SASILGHDVQ TNMAAIRPHL GICPQYNVLF DMLTVEEHVW
FYGRLKGVSA AAMGPERERL IRDVGLTLKR DTQTRHLSGG MQRKLSVAIA FVGGSRVVIM
DEPTAGVDPA SRRGIWELLL KYREGRTLIL STHHLDEAEL LGDRVAMVAG GSLCCCGSPL
FLRRHLGCGY YLTLVKSSQS LVTHDAKGDS EDPRREKKSD GNGRTSDTAF TRGTSDKSNQ
APAPGAVPIT PSTARILELV QQHVPGAQLV EDLPHELLLV LPYAGALDGS FAMVFQELDQ
QLELLGLTGY GISDTNLEEI FLKVVEDAHR EGGDSRPQLH LRTCTPQPPT GPEASVLENG
ELAPQGLAPN AAQVQGWTLT CQQLRALLHK RFLLARRSRR GLFAQVVLPA LFVGLALFFS
LIVPPFGQYP PLQLSPAMYG PQVSFFSEDA PGDPNRMKLL EALLGEAGLQ EPSMQDKDAR
GSECTHSLAC YFTVPEVPPD VASILASGNW TPESPSPACQ CSQPGARRLL PDCPAGAGGP
PPPQAVAGLG EVVQNLTGRN VSDFLVKTYP SLVRRGLKTK KWVDEVRYGG FSLGGRDPDL
PTGHEVVRTL AEIRALLSPQ PGNALDRILN NLTQWALGLD ARNSLKIWFN NKGWHAMVAF
VNRANNGLLH ALLPSGPVRH AHSITTLNHP LNLTKEQLSE ATLIASSVDV LVSICVVFAM
SFVPASFTLV LIEERITRAK HLQLVSGLPQ TLYWLGNFLW DMCNYLVAVC IVVFIFLAFQ
QRAYVAPENL PALLLLLLLY GWSITPLMYP ASFFFSVPST AYVVLTCINL FIGINSSMAT
FVLELLSDQN LQEVSRILKQ VFLIFPHFCL GRGLIDMVRN QAMADAFERL GDKQFQSPLR
WDIIGKNLLA MMAQGPLFLL ITLLLQHRNR LLPQSKPRLL PPLGEEDEDV AQERERVTKG
ATQGDVLVLR DLTKVYRGQR NPAVDRLCLG IPPGECFGLL GVNGAGKTST FRMVTGDTLP
SSGEAVLAGH NVAQERSAAH RSMGYCPQSD AIFDLLTGRE HLELFARLRG VPEAQVAQTA
LSGLVRLGLP SYADRPAGTY SGGNKRKLAT ALALVGDPAV VFLDEPTTGM DPSARRFLWN
SLLSVVREGR SVVLTSHSME ECEALCTRLA IMVNGRFRCL GSSQHLKGRF GAGHTLTLRV
PPDQPEPAIA FIRITFPGAE LREVHGSRLR FQLPPGGRCT LTRVFRELAA QGRAHGVEDF
SVSQTTLEEV FLYFSKDQGE EEESSRQEAE EEEVSKPGRQ HPKRVSRFLE DPSSVETMI


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