ABCA6_HUMAN
ID ABCA6_HUMAN Reviewed; 1617 AA.
AC Q8N139; Q6NSH9; Q8N856; Q8WWZ6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP-binding cassette sub-family A member 6 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:10639163};
GN Name=ABCA6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), ALTERNATIVE SPLICING
RP (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Macrophage;
RX PubMed=11478798; DOI=10.1006/bbrc.2001.5326;
RA Kaminski W.E., Wenzel J.J., Piehler A., Langmann T., Schmitz G.;
RT "ABCA6, a novel A subclass ABC transporter.";
RL Biochem. Biophys. Res. Commun. 285:1295-1301(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND VARIANTS ILE-282; ILE-875 AND SER-1322.
RA Arnould I., Schriml L.M., Prades C., Lachtermacher-Triunfol M.,
RA Schneider T., Maintoux C., Lemoine C., Debono D., Devaud C., Naudin L.,
RA Bauche S., Annat M., Annilo T., Allikmets R., Gold B., Denefle P.,
RA Rosier M., Dean M.;
RT "Identifying and characterizing a five-gene cluster of ATP-binding cassette
RT transporters mapping to human chromosome 17q24: a new subgroup within the
RT ABCA subfamily.";
RL GeneScreen 1:157-164(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 801-1617 (ISOFORM 1), AND VARIANT
RP SER-1322.
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP INDUCTION, AND FUNCTION.
RX PubMed=10639163; DOI=10.1073/pnas.97.2.817;
RA Klucken J., Buechler C., Orso E., Kaminski W.E., Porsch-Oezcueruemez M.,
RA Liebisch G., Kapinsky M., Diederich W., Drobnik W., Dean M., Allikmets R.,
RA Schmitz G.;
RT "ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
RT regulator of macrophage cholesterol and phospholipid transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:817-822(2000).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-940.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24028821; DOI=10.1016/j.biocel.2013.08.020;
RA Gai J., Ji M., Shi C., Li W., Chen S., Wang Y., Li H.;
RT "FoxO regulates expression of ABCA6, an intracellular ATP-binding-cassette
RT transporter responsive to cholesterol.";
RL Int. J. Biochem. Cell Biol. 45:2651-2659(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Probable transporter which may play a role in macrophage
CC lipid transport and homeostasis. {ECO:0000305|PubMed:10639163}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:24028821}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N139-1; Sequence=Displayed;
CC Name=2; Synonyms=ABCA6delta-139;
CC IsoId=Q8N139-2; Sequence=VSP_020697, VSP_020698;
CC Name=3;
CC IsoId=Q8N139-3; Sequence=VSP_020695, VSP_020696;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in liver.
CC {ECO:0000269|PubMed:11478798, ECO:0000269|Ref.2}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal kidney, lung and liver.
CC {ECO:0000269|Ref.2}.
CC -!- INDUCTION: Up-regulated during monocyte differentiation into
CC macrophages (PubMed:10639163). Down-regulated by cholesterol loading of
CC macrophages (PubMed:10639163, PubMed:24028821).
CC {ECO:0000269|PubMed:10639163, ECO:0000269|PubMed:24028821}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM77557.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM77558.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC04994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AF373290; AAM77557.1; ALT_FRAME; mRNA.
DR EMBL; AF373328; AAM77558.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF373291; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373292; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373293; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373294; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373295; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373296; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373297; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373298; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373299; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373300; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373301; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373302; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373303; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373304; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373305; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373306; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373307; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373308; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373309; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373310; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373311; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373312; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373313; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373314; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373315; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373316; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373317; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373318; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373319; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373320; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373321; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373322; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373323; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373324; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373325; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373326; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AF373327; AAM77558.1; JOINED; Genomic_DNA.
DR EMBL; AY028898; AAK30023.1; -; mRNA.
DR EMBL; BC070125; AAH70125.1; -; mRNA.
DR EMBL; AK097296; BAC04994.1; ALT_INIT; mRNA.
DR CCDS; CCDS11683.1; -. [Q8N139-1]
DR RefSeq; NP_525023.2; NM_080284.2. [Q8N139-1]
DR RefSeq; XP_016879893.1; XM_017024404.1. [Q8N139-1]
DR RefSeq; XP_016879894.1; XM_017024405.1. [Q8N139-1]
DR AlphaFoldDB; Q8N139; -.
DR SMR; Q8N139; -.
DR BioGRID; 117023; 9.
DR IntAct; Q8N139; 1.
DR STRING; 9606.ENSP00000284425; -.
DR TCDB; 3.A.1.211.15; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q8N139; 3 sites.
DR iPTMnet; Q8N139; -.
DR PhosphoSitePlus; Q8N139; -.
DR BioMuta; ABCA6; -.
DR DMDM; 115503764; -.
DR EPD; Q8N139; -.
DR jPOST; Q8N139; -.
DR MassIVE; Q8N139; -.
DR PaxDb; Q8N139; -.
DR PeptideAtlas; Q8N139; -.
DR PRIDE; Q8N139; -.
DR ProteomicsDB; 71545; -. [Q8N139-1]
DR ProteomicsDB; 71546; -. [Q8N139-2]
DR ProteomicsDB; 71547; -. [Q8N139-3]
DR TopDownProteomics; Q8N139-3; -. [Q8N139-3]
DR Antibodypedia; 31832; 166 antibodies from 27 providers.
DR DNASU; 23460; -.
DR Ensembl; ENST00000284425.7; ENSP00000284425.1; ENSG00000154262.13. [Q8N139-1]
DR Ensembl; ENST00000590645.1; ENSP00000466862.1; ENSG00000154262.13. [Q8N139-3]
DR GeneID; 23460; -.
DR KEGG; hsa:23460; -.
DR MANE-Select; ENST00000284425.7; ENSP00000284425.1; NM_080284.3; NP_525023.2.
DR UCSC; uc002jhw.2; human. [Q8N139-1]
DR CTD; 23460; -.
DR DisGeNET; 23460; -.
DR GeneCards; ABCA6; -.
DR HGNC; HGNC:36; ABCA6.
DR HPA; ENSG00000154262; Tissue enhanced (liver).
DR MIM; 612504; gene.
DR neXtProt; NX_Q8N139; -.
DR OpenTargets; ENSG00000154262; -.
DR PharmGKB; PA24381; -.
DR VEuPathDB; HostDB:ENSG00000154262; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162244; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8N139; -.
DR OMA; ERRADHV; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q8N139; -.
DR TreeFam; TF105192; -.
DR PathwayCommons; Q8N139; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR SignaLink; Q8N139; -.
DR BioGRID-ORCS; 23460; 24 hits in 1072 CRISPR screens.
DR ChiTaRS; ABCA6; human.
DR GenomeRNAi; 23460; -.
DR Pharos; Q8N139; Tbio.
DR PRO; PR:Q8N139; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N139; protein.
DR Bgee; ENSG00000154262; Expressed in calcaneal tendon and 128 other tissues.
DR Genevisible; Q8N139; HS.
DR GO; GO:0000139; C:Golgi membrane; IDA: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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR030368; ABCA6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF13; PTHR19229:SF13; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Golgi apparatus; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1617
FT /note="ATP-binding cassette sub-family A member 6"
FT /id="PRO_0000250672"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1027
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1062..1082
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1094..1114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1127..1147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1150..1170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 478..713
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1288..1513
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1320..1327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 154..185
FT /note="AHCWDGYGEFSCTLTKYWNRGFVALQTAINTA -> GDFPYQISLWNFSCFQ
FT HKEQRRLGNRDAFNDT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020695"
FT VAR_SEQ 186..1617
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020696"
FT VAR_SEQ 636..637
FT /note="LL -> EK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020697"
FT VAR_SEQ 638..1617
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020698"
FT VARIANT 282
FT /note="V -> I (in dbSNP:rs4968839)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_027576"
FT VARIANT 610
FT /note="N -> Y (in dbSNP:rs9282554)"
FT /id="VAR_027577"
FT VARIANT 698
FT /note="M -> I (in dbSNP:rs9282553)"
FT /id="VAR_027578"
FT VARIANT 875
FT /note="M -> I (in dbSNP:rs7212506)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_027579"
FT VARIANT 1322
FT /note="N -> S (in dbSNP:rs2302134)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_027580"
FT CONFLICT 51
FT /note="M -> L (in Ref. 3; AAH70125)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="L -> R (in Ref. 3; AAH70125)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="E -> G (in Ref. 4; BAC04994)"
FT /evidence="ECO:0000305"
FT CONFLICT 875..876
FT /note="MY -> IH (in Ref. 4; BAC04994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1617 AA; 184286 MW; 73940D8050B0A3CA CRC64;
MNMKQKSVYQ QTKALLCKNF LKKWRMKRES LLEWGLSILL GLCIALFSSS MRNVQFPGMA
PQNLGRVDKF NSSSLMVVYT PISNLTQQIM NKTALAPLLK GTSVIGAPNK THMDEILLEN
LPYAMGIIFN ETFSYKLIFF QGYNSPLWKE DFSAHCWDGY GEFSCTLTKY WNRGFVALQT
AINTAIIEIT TNHPVMEELM SVTAITMKTL PFITKNLLHN EMFILFFLLH FSPLVYFISL
NVTKERKKSK NLMKMMGLQD SAFWLSWGLI YAGFIFIISI FVTIIITFTQ IIVMTGFMVI
FILFFLYGLS LVALVFLMSV LLKKAVLTNL VVFLLTLFWG CLGFTVFYEQ LPSSLEWILN
ICSPFAFTTG MIQIIKLDYN LNGVIFPDPS GDSYTMIATF SMLLLDGLIY LLLALYFDKI
LPYGDERHYS PLFFLNSSSC FQHQRTNAKV IEKEIDAEHP SDDYFEPVAP EFQGKEAIRI
RNVKKEYKGK SGKVEALKGL LFDIYEGQIT AILGHSGAGK SSLLNILNGL SVPTEGSVTI
YNKNLSEMQD LEEIRKITGV CPQFNVQFDI LTVKENLSLF AKIKGIHLKE VEQEVQRILL
ELDMQNIQDN LAKHLSEGQK RKLTFGITIL GDPQILLLDE PTTGLDPFSR DQVWSLLRER
RADHVILFST QSMDEADILA DRKVIMSNGR LKCAGSSMFL KRRWGLGYHL SLHRNEICNP
EQITSFITHH IPDAKLKTEN KEKLVYTLPL ERTNTFPDLF SDLDKCSDQG VTGYDISMST
LNEVFMKLEG QSTIEQDFEQ VEMIRDSESL NEMELAHSSF SEMQTAVSDM GLWRMQVFAM
ARLRFLKLKR QTKVLLTLLL VFGIAIFPLI VENIMYAMLN EKIDWEFKNE LYFLSPGQLP
QEPRTSLLII NNTESNIEDF IKSLKHQNIL LEVDDFENRN GTDGLSYNGA IIVSGKQKDY
RFSVVCNTKR LHCFPILMNI ISNGLLQMFN HTQHIRIESS PFPLSHIGLW TGLPDGSFFL
FLVLCSISPY ITMGSISDYK KNAKSQLWIS GLYTSAYWCG QALVDVSFFI LILLLMYLIF
YIENMQYLLI TSQIVFALVI VTPGYAASLV FFIYMISFIF RKRRKNSGLW SFYFFFASTI
MFSITLINHF DLSILITTMV LVPSYTLLGF KTFLEVRDQE HYREFPEANF ELSATDFLVC
FIPYFQTLLF VFVLRCMELK CGKKRMRKDP VFRISPQSRD AKPNPEEPID EDEDIQTERI
RTATALTTSI LDEKPVIIAS CLHKEYAGQK KSCFSKRKKK IAARNISFCV QEGEILGLLG
PNGAGKSSSI RMISGITKPT AGEVELKGCS SVLGHLGYCP QENVLWPMLT LREHLEVYAA
VKGLRKADAR LAIARLVSAF KLHEQLNVPV QKLTAGITRK LCFVLSLLGN SPVLLLDEPS
TGIDPTGQQQ MWQAIQAVVK NTERGVLLTT HNLAEAEALC DRVAIMVSGR LRCIGSIQHL
KNKLGKDYIL ELKVKETSQV TLVHTEILKL FPQAAGQERY SSLLTYKLPV ADVYPLSQTF
HKLEAVKHNF NLEEYSLSQC TLEKVFLELS KEQEVGNFDE EIDTTMRWKL LPHSDEP
