GENTAUR Molecular Products.

 ABCA1_MOUSE             Reviewed;        2261 AA.
 P41233; B1AWZ8;
 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
 27-JUL-2011, sequence version 4.
 18-JUL-2018, entry version 175.
 RecName: Full=ATP-binding cassette sub-family A member 1;
 AltName: Full=ATP-binding cassette transporter 1;
          Short=ABC-1;
          Short=ATP-binding cassette 1;
 Name=Abca1; Synonyms=Abc1;
 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 [MRNA].
 STRAIN=DBA/2J; TISSUE=Macrophage;
 PubMed=8088782; DOI=10.1006/geno.1994.1237;
 Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
 "Cloning of two novel ABC transporters mapping on human chromosome
 9.";
 Genomics 21:150-159(1994).
 [2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=C57BL/6J;
 PubMed=11352567; DOI=10.1006/geno.2000.6467;
 Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
 "Human and mouse ABCA1 comparative sequencing and transgenesis studies
 revealing novel regulatory sequences.";
 Genomics 73:66-76(2001).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=C57BL/6J;
 PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
 Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
 She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
 Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
 Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
 Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
 Lindblad-Toh K., Eichler E.E., Ponting C.P.;
 "Lineage-specific biology revealed by a finished genome assembly of
 the mouse.";
 PLoS Biol. 7:E1000112-E1000112(2009).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [5]
 INDUCTION BY LIPOPOLYSACCHARIDE.
 PubMed=12032171;
 Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
 "Bacterial lipopolysaccharide induces expression of ABCA1 but not
 ABCG1 via an LXR-independent pathway.";
 J. Lipid Res. 43:952-959(2002).
 [6]
 DOWN-REGULATION BY ENDOTOXIN.
 PubMed=12777468; DOI=10.1194/jlr.M300100-JLR200;
 Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C.,
 Feingold K.R.;
 "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
 ABCG1 in J774 murine macrophages: differential role of LXR.";
 J. Lipid Res. 44:1728-1736(2003).
 [7]
 INTERACTION WITH MEGF10.
 PubMed=17205124; DOI=10.1371/journal.pone.0000120;
 Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
 Zhou Z., Chimini G.;
 "Cooperation between engulfment receptors: the case of ABCA1 and
 MEGF10.";
 PLoS ONE 1:E120-E120(2006).
 [8]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=17242355; DOI=10.1073/pnas.0609836104;
 Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
 "Large-scale phosphorylation analysis of mouse liver.";
 Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
 [9]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489.
 PubMed=19349973; DOI=10.1038/nbt.1532;
 Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
 Schiess R., Aebersold R., Watts J.D.;
 "Mass-spectrometric identification and relative quantification of N-
 linked cell surface glycoproteins.";
 Nat. Biotechnol. 27:378-386(2009).
 [10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
 Spleen, and Testis;
 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).
 -!- FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion
     transporter. Key gatekeeper influencing intracellular cholesterol
     transport (By similarity). {ECO:0000250}.
 -!- SUBUNIT: Interacts with MEGF10. {ECO:0000269|PubMed:17205124}.
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
     protein {ECO:0000305}.
 -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest
     levels are found in pregnant uterus and uterus.
 -!- INDUCTION: Down-regulated by endotoxins (LPS) or cytokines (TNF
     and IL-1) in J774 macrophages. The down-regulation by endotoxin in
     macrophages is not likely to be mediated by the liver X
     receptor/retinoic X receptor (LXR/RXR).
     {ECO:0000269|PubMed:12032171}.
 -!- DOMAIN: Multifunctional polypeptide with two homologous halves,
     each containing a hydrophobic membrane-anchoring domain and an ATP
     binding cassette (ABC) domain.
 -!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux.
     {ECO:0000250}.
 -!- PTM: Palmitoylation by DHHC8 is essential for membrane
     localization. {ECO:0000250}.
 -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
     family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAG39073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
     Sequence=CAA53530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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 EMBL; X75926; CAA53530.1; ALT_INIT; mRNA.
 EMBL; AF287263; AAG39073.1; ALT_INIT; Genomic_DNA.
 EMBL; AL807243; CAM18883.1; -; Genomic_DNA.
 EMBL; AL772397; CAM18883.1; JOINED; Genomic_DNA.
 EMBL; AL772397; CAM27437.1; -; Genomic_DNA.
 EMBL; AL807243; CAM27437.1; JOINED; Genomic_DNA.
 EMBL; CH466565; EDL02285.1; -; Genomic_DNA.
 CCDS; CCDS18187.1; -.
 PIR; A54774; A54774.
 RefSeq; NP_038482.3; NM_013454.3.
 UniGene; Mm.277376; -.
 ProteinModelPortal; P41233; -.
 SMR; P41233; -.
 BioGrid; 197900; 1.
 IntAct; P41233; 2.
 STRING; 10090.ENSMUSP00000030010; -.
 BindingDB; P41233; -.
 ChEMBL; CHEMBL1641361; -.
 SwissLipids; SLP:000000484; -.
 TCDB; 3.A.1.211.1; the atp-binding cassette (abc) superfamily.
 iPTMnet; P41233; -.
 PhosphoSitePlus; P41233; -.
 SwissPalm; P41233; -.
 MaxQB; P41233; -.
 PaxDb; P41233; -.
 PeptideAtlas; P41233; -.
 PRIDE; P41233; -.
 Ensembl; ENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
 GeneID; 11303; -.
 KEGG; mmu:11303; -.
 UCSC; uc008swu.1; mouse.
 CTD; 19; -.
 MGI; MGI:99607; Abca1.
 eggNOG; KOG0059; Eukaryota.
 eggNOG; COG1131; LUCA.
 GeneTree; ENSGT00760000118965; -.
 HOGENOM; HOG000231547; -.
 HOVERGEN; HBG050436; -.
 InParanoid; P41233; -.
 KO; K05641; -.
 OMA; IQTISRF; -.
 OrthoDB; EOG091G007E; -.
 TreeFam; TF105191; -.
 Reactome; R-MMU-8963896; HDL assembly.
 PMAP-CutDB; B1AWZ8; -.
 PRO; PR:P41233; -.
 Proteomes; UP000000589; Chromosome 4.
 Bgee; ENSMUSG00000015243; -.
 Genevisible; P41233; MM.
 GO; GO:0009986; C:cell surface; ISO:MGI.
 GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
 GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
 GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
 GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
 GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
 GO; GO:0045121; C:membrane raft; ISO:MGI.
 GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
 GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
 GO; GO:0005886; C:plasma membrane; IDA:MGI.
 GO; GO:0008509; F:anion transmembrane transporter activity; IDA:BHF-UCL.
 GO; GO:0034186; F:apolipoprotein A-I binding; ISO:MGI.
 GO; GO:0034188; F:apolipoprotein A-I receptor activity; ISO:MGI.
 GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
 GO; GO:0005524; F:ATP binding; ISO:MGI.
 GO; GO:0016887; F:ATPase activity; ISO:MGI.
 GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; ISO:MGI.
 GO; GO:0051117; F:ATPase binding; ISO:MGI.
 GO; GO:0017127; F:cholesterol transporter activity; IDA:MGI.
 GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
 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:0005102; F:signaling receptor binding; ISO:MGI.
 GO; GO:0031267; F:small GTPase binding; ISO:MGI.
 GO; GO:0019905; F:syntaxin binding; ISO:MGI.
 GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISO:MGI.
 GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
 GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
 GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
 GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
 GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
 GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
 GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
 GO; GO:0030301; P:cholesterol transport; ISO:MGI.
 GO; GO:0016197; P:endosomal transport; ISO:MGI.
 GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
 GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:MGI.
 GO; GO:0050702; P:interleukin-1 beta secretion; ISO:MGI.
 GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
 GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:MGI.
 GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
 GO; GO:0007040; P:lysosome organization; ISO:MGI.
 GO; GO:0002790; P:peptide secretion; IMP:MGI.
 GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
 GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
 GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
 GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
 GO; GO:0015914; P:phospholipid transport; ISO:MGI.
 GO; GO:0060155; P:platelet dense granule organization; ISO:MGI.
 GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
 GO; GO:0006497; P:protein lipidation; IMP:MGI.
 GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
 GO; GO:0042493; P:response to drug; IEA:Ensembl.
 GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
 GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
 GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
 InterPro; IPR003593; AAA+_ATPase.
 InterPro; IPR003439; ABC_transporter-like.
 InterPro; IPR017871; ABC_transporter_CS.
 InterPro; IPR026082; ABCA.
 InterPro; IPR027417; P-loop_NTPase.
 PANTHER; PTHR19229; PTHR19229; 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; Complete proteome; Disulfide bond; Glycoprotein;
 Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
 Reference proteome; Repeat; Transmembrane; Transmembrane helix;
 Transport.
 CHAIN         1   2261       ATP-binding cassette sub-family A member
                              1.
                              /FTId=PRO_0000093289.
 TRANSMEM     22     42       Helical. {ECO:0000255}.
 TOPO_DOM     43    639       Extracellular. {ECO:0000250}.
 TRANSMEM    640    660       Helical. {ECO:0000255}.
 TRANSMEM    683    703       Helical. {ECO:0000255}.
 TRANSMEM    716    736       Helical. {ECO:0000255}.
 TRANSMEM    745    765       Helical. {ECO:0000255}.
 TRANSMEM    777    797       Helical. {ECO:0000255}.
 TRANSMEM    827    847       Helical. {ECO:0000255}.
 TRANSMEM    941    961       Helical. {ECO:0000255}.
 TRANSMEM   1351   1371       Helical. {ECO:0000255}.
 TOPO_DOM   1372   1656       Extracellular. {ECO:0000250}.
 TRANSMEM   1657   1677       Helical. {ECO:0000255}.
 TRANSMEM   1703   1723       Helical. {ECO:0000255}.
 TRANSMEM   1735   1755       Helical. {ECO:0000255}.
 TRANSMEM   1768   1788       Helical. {ECO:0000255}.
 TRANSMEM   1802   1822       Helical. {ECO:0000255}.
 TRANSMEM   1852   1872       Helical. {ECO:0000255}.
 DOMAIN      899   1131       ABC transporter 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00434}.
 DOMAIN     1912   2144       ABC transporter 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00434}.
 NP_BIND     933    940       ATP 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00434}.
 NP_BIND    1946   1953       ATP 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00434}.
 MOD_RES    1042   1042       Phosphoserine; by PKA.
                              {ECO:0000250|UniProtKB:O95477}.
 MOD_RES    1296   1296       Phosphoserine.
                              {ECO:0000244|PubMed:17242355,
                              ECO:0000244|PubMed:21183079}.
 MOD_RES    2054   2054       Phosphoserine; by PKA.
                              {ECO:0000250|UniProtKB:O95477}.
 LIPID         3      3       S-palmitoyl cysteine. {ECO:0000250}.
 LIPID        23     23       S-palmitoyl cysteine. {ECO:0000250}.
 LIPID      1110   1110       S-palmitoyl cysteine. {ECO:0000250}.
 LIPID      1111   1111       S-palmitoyl cysteine. {ECO:0000250}.
 CARBOHYD     14     14       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD     98     98       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    161    161       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    196    196       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    244    244       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    292    292       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    337    337       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    349    349       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    400    400       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    478    478       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    489    489       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19349973}.
 CARBOHYD    521    521       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    820    820       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1144   1144       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1294   1294       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1453   1453       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1499   1499       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1504   1504       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1637   1637       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   2044   2044       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   2238   2238       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID     75    309       {ECO:0000250}.
 DISULFID   1463   1477       {ECO:0000250}.
 CONFLICT   1567   1568       Missing (in Ref. 2; AAG39073).
                              {ECO:0000305}.
 CONFLICT   1568   1568       S -> T (in Ref. 1; CAA53530).
                              {ECO:0000305}.
 CONFLICT   2024   2024       V -> F (in Ref. 1; CAA53530).
                              {ECO:0000305}.
 CONFLICT   2024   2024       Missing (in Ref. 2; AAG39073).
                              {ECO:0000305}.
 SEQUENCE   2261 AA;  253912 MW;  E041DA4FA73C2660 CRC64;
 MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
 MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVSRLFSDAQ RLLLYSQRDT
 SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD NETFSGFLQH NLSLPRSTVD SLLQANVGLQ
 KVFLQGYQLH LASLCNGSKL EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV
 TKLNSTSHLP TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI
 YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS TTPYCNDLMK
 NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
 PQIWTFMENS QEMDLVRTLL DSRGNDQFWE QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS
 VYTWREAFNE TNQAIQTISR FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG
 ITPDSVELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
 EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKSIV
 YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
 FLSVFAMVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS
 LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW
 YIEAVFPGQY GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS
 IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
 GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
 LPPSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
 GRTIILSTHH MDEADILGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
 SCRNSSSTVS CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
 GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
 TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP ESRETDLLSG MDGKGSYQLK
 GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
 PWMYNEQYTF VSNDAPEDMG TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP
 VPQSIVDLFQ NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL
 TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE VNDAIKQMKK
 LLKLTKDSSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
 GENPSQYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
 VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
 LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN
 DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
 VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
 YRRKRKPAVD RICIGIPPGE CFGLLGVNGA GKSTTFKMLT GDTPVTRGDA FLNKNSILSN
 IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK
 YASNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT
 SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQEFFG
 LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
 AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V

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