ABCA5_HUMAN
ID ABCA5_HUMAN Reviewed; 1642 AA.
AC Q8WWZ7; Q8IVJ2; Q96LJ1; Q96MS4; Q96PZ9; Q9NY14;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cholesterol transporter ABCA5 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:25125465};
DE AltName: Full=ATP-binding cassette sub-family A member 5 {ECO:0000305};
GN Name=ABCA5 {ECO:0000312|HGNC:HGNC:35}; Synonyms=KIAA1888;
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 [MRNA] (ISOFORM 1), VARIANT SER-832, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANTS THR-178; ARG-484 AND SER-832.
RC TISSUE=Hepatoma, and Testis;
RX PubMed=12504089; DOI=10.1016/s0006-291x(02)02827-9;
RA Petry F., Kotthaus A., Hirsch-Ernst K.I.;
RT "Cloning of human and rat ABCA5/Abca5 and detection of a human splice
RT variant.";
RL Biochem. Biophys. Res. Commun. 300:343-350(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1187-1642 (ISOFORM 1), AND VARIANT SER-832.
RC TISSUE=Teratocarcinoma, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 906-1642 (ISOFORM 1), AND VARIANT
RP VAL-960.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=24831815; DOI=10.1371/journal.pgen.1004333;
RA DeStefano G.M., Kurban M., Anyane-Yeboa K., Dall'Armi C., Di Paolo G.,
RA Feenstra H., Silverberg N., Rohena L., Lopez-Cepeda L.D., Jobanputra V.,
RA Fantauzzo K.A., Kiuru M., Tadin-Strapps M., Sobrino A., Vitebsky A.,
RA Warburton D., Levy B., Salas-Alanis J.C., Christiano A.M.;
RT "Mutations in the cholesterol transporter gene ABCA5 are associated with
RT excessive hair overgrowth.";
RL PLoS Genet. 10:e1004333-e1004333(2014).
RN [6]
RP TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25125465; DOI=10.3233/jad-141320;
RA Fu Y., Hsiao J.H., Paxinos G., Halliday G.M., Kim W.S.;
RT "ABCA5 regulates amyloid-beta peptide production and is associated with
RT Alzheimer's disease neuropathology.";
RL J. Alzheimers Dis. 43:857-869(2015).
CC -!- FUNCTION: Cholesterol efflux transporter in macrophages that is
CC responsible for APOAI/high-density lipoproteins (HDL) formation at the
CC plasma membrane under high cholesterol levels and participates in
CC reverse cholesterol transport (PubMed:25125465). May play a role in the
CC processing of autolysosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q8K448, ECO:0000269|PubMed:25125465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:25125465};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000305|PubMed:25125465};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8CF82}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8CF82}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q8K448}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8K448}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q8K448}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8K448}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8K448}. Note=Localized at cell membrane under
CC high cholesterol levels. {ECO:0000250|UniProtKB:Q8K448}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WWZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=V20+16;
CC IsoId=Q8WWZ7-2; Sequence=VSP_020691, VSP_020692;
CC Name=3;
CC IsoId=Q8WWZ7-3; Sequence=VSP_020690;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis,
CC skeletal muscle, kidney, liver and placenta. Expressed in both the
CC epithelial and mesenchymal compartments, present within the outer root
CC sheath (ORS) of the hair follicle as well as dermal sheath
CC (PubMed:24831815). Expressed in multiple regions of the brain,
CC including the hippocampus, superior frontal and inferior temporal
CC cortices (PubMed:25125465). Strongly expressed in neurons and
CC moderately in microglia, with only weak expression in astrocytes and
CC oligodendrocytes (PubMed:25125465). {ECO:0000269|PubMed:12504089,
CC ECO:0000269|PubMed:24831815, ECO:0000269|PubMed:25125465,
CC ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver, kidney and brain.
CC {ECO:0000269|Ref.1}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71700.1; 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; AY028897; AAK30022.1; -; mRNA.
DR EMBL; AJ275973; CAB93535.3; -; mRNA.
DR EMBL; AJ512612; CAD54757.1; -; mRNA.
DR EMBL; AK056533; BAB71208.1; -; mRNA.
DR EMBL; AK058170; BAB71700.1; ALT_INIT; mRNA.
DR EMBL; AB067475; BAB67781.1; -; mRNA.
DR CCDS; CCDS11685.1; -. [Q8WWZ7-1]
DR RefSeq; NP_061142.2; NM_018672.4. [Q8WWZ7-1]
DR RefSeq; NP_758424.1; NM_172232.3. [Q8WWZ7-1]
DR AlphaFoldDB; Q8WWZ7; -.
DR SMR; Q8WWZ7; -.
DR BioGRID; 117024; 4.
DR IntAct; Q8WWZ7; 3.
DR STRING; 9606.ENSP00000376443; -.
DR DrugBank; DB00864; Tacrolimus.
DR TCDB; 3.A.1.211.9; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q8WWZ7; 3 sites.
DR iPTMnet; Q8WWZ7; -.
DR PhosphoSitePlus; Q8WWZ7; -.
DR BioMuta; ABCA5; -.
DR DMDM; 115503762; -.
DR EPD; Q8WWZ7; -.
DR jPOST; Q8WWZ7; -.
DR MassIVE; Q8WWZ7; -.
DR MaxQB; Q8WWZ7; -.
DR PaxDb; Q8WWZ7; -.
DR PeptideAtlas; Q8WWZ7; -.
DR PRIDE; Q8WWZ7; -.
DR ProteomicsDB; 74970; -. [Q8WWZ7-1]
DR ProteomicsDB; 74971; -. [Q8WWZ7-2]
DR ProteomicsDB; 74972; -. [Q8WWZ7-3]
DR Antibodypedia; 19335; 181 antibodies from 28 providers.
DR DNASU; 23461; -.
DR Ensembl; ENST00000392676.8; ENSP00000376443.2; ENSG00000154265.16. [Q8WWZ7-1]
DR Ensembl; ENST00000588877.5; ENSP00000467882.1; ENSG00000154265.16. [Q8WWZ7-1]
DR GeneID; 23461; -.
DR KEGG; hsa:23461; -.
DR MANE-Select; ENST00000392676.8; ENSP00000376443.2; NM_172232.4; NP_758424.1.
DR UCSC; uc002jif.3; human. [Q8WWZ7-1]
DR CTD; 23461; -.
DR DisGeNET; 23461; -.
DR GeneCards; ABCA5; -.
DR HGNC; HGNC:35; ABCA5.
DR HPA; ENSG00000154265; Low tissue specificity.
DR MalaCards; ABCA5; -.
DR MIM; 612503; gene.
DR neXtProt; NX_Q8WWZ7; -.
DR OpenTargets; ENSG00000154265; -.
DR Orphanet; 2026; Gingival fibromatosis-hypertrichosis syndrome.
DR PharmGKB; PA24380; -.
DR VEuPathDB; HostDB:ENSG00000154265; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000158172; -.
DR InParanoid; Q8WWZ7; -.
DR OMA; HGLYFYA; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q8WWZ7; -.
DR TreeFam; TF105192; -.
DR PathwayCommons; Q8WWZ7; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR SignaLink; Q8WWZ7; -.
DR BioGRID-ORCS; 23461; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; ABCA5; human.
DR GenomeRNAi; 23461; -.
DR Pharos; Q8WWZ7; Tbio.
DR PRO; PR:Q8WWZ7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WWZ7; protein.
DR Bgee; ENSG00000154265; Expressed in adrenal tissue and 202 other tissues.
DR ExpressionAtlas; Q8WWZ7; baseline and differential.
DR Genevisible; Q8WWZ7; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0005770; C:late endosome; ISS:BHF-UCL.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0033344; P:cholesterol efflux; ISS:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:BHF-UCL.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISS:BHF-UCL.
DR GO; GO:1903064; P:positive regulation of reverse cholesterol transport; ISS:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
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; IPR030367; ABCA5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF100; PTHR19229:SF100; 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 Alternative splicing; ATP-binding; Cell membrane; Endosome; Glycoprotein;
KW Golgi apparatus; Lipid transport; Lysosome; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1642
FT /note="Cholesterol transporter ABCA5"
FT /id="PRO_0000250669"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1102..1122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1139..1159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1169..1189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1227
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 1290..1533
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1249..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1333..1340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..777
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020690"
FT VAR_SEQ 922..925
FT /note="DSDI -> GESV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12504089"
FT /id="VSP_020691"
FT VAR_SEQ 926..1642
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12504089"
FT /id="VSP_020692"
FT VARIANT 93
FT /note="Q -> K (in dbSNP:rs12383)"
FT /id="VAR_027571"
FT VARIANT 178
FT /note="A -> T (in dbSNP:rs11544715)"
FT /evidence="ECO:0000269|PubMed:12504089"
FT /id="VAR_048128"
FT VARIANT 484
FT /note="Q -> R (in dbSNP:rs17686569)"
FT /evidence="ECO:0000269|PubMed:12504089"
FT /id="VAR_027572"
FT VARIANT 753
FT /note="M -> V (in dbSNP:rs9898003)"
FT /id="VAR_027573"
FT VARIANT 832
FT /note="A -> S (in dbSNP:rs536009)"
FT /evidence="ECO:0000269|PubMed:12504089,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_027574"
FT VARIANT 960
FT /note="M -> V (in dbSNP:rs557491)"
FT /evidence="ECO:0000269|PubMed:11572484"
FT /id="VAR_027575"
FT VARIANT 1260
FT /note="D -> G (in dbSNP:rs11544716)"
FT /id="VAR_048129"
FT CONFLICT 1215
FT /note="Y -> H (in Ref. 3; BAB71208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1357
FT /note="V -> I (in Ref. 2; CAB93535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1366
FT /note="T -> S (in Ref. 2; CAB93535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="D -> G (in Ref. 3; BAB71208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1419
FT /note="A -> G (in Ref. 3; BAB71208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1523
FT /note="K -> R (in Ref. 3; BAB71208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1642 AA; 186508 MW; 608809E8539804BF CRC64;
MSTAIREVGV WRQTRTLLLK NYLIKCRTKK SSVQEILFPL FFLFWLILIS MMHPNKKYEE
VPNIELNPMD KFTLSNLILG YTPVTNITSS IMQKVSTDHL PDVIITEEYT NEKEMLTSSL
SKPSNFVGVV FKDSMSYELR FFPDMIPVSS IYMDSRAGCS KSCEAAQYWS SGFTVLQASI
DAAIIQLKTN VSLWKELEST KAVIMGETAV VEIDTFPRGV ILIYLVIAFS PFGYFLAIHI
VAEKEKKIKE FLKIMGLHDT AFWLSWVLLY TSLIFLMSLL MAVIATASLL FPQSSSIVIF
LLFFLYGLSS VFFALMLTPL FKKSKHVGIV EFFVTVAFGF IGLMIILIES FPKSLVWLFS
PFCHCTFVIG IAQVMHLEDF NEGASFSNLT AGPYPLIITI IMLTLNSIFY VLLAVYLDQV
IPGEFGLRRS SLYFLKPSYW SKSKRNYEEL SEGNVNGNIS FSEIIEPVSS EFVGKEAIRI
SGIQKTYRKK GENVEALRNL SFDIYEGQIT ALLGHSGTGK STLMNILCGL CPPSDGFASI
YGHRVSEIDE MFEARKMIGI CPQLDIHFDV LTVEENLSIL ASIKGIPANN IIQEVQKVLL
DLDMQTIKDN QAKKLSGGQK RKLSLGIAVL GNPKILLLDE PTAGMDPCSR HIVWNLLKYR
KANRVTVFST HFMDEADILA DRKAVISQGM LKCVGSSMFL KSKWGIGYRL SMYIDKYCAT
ESLSSLVKQH IPGATLLQQN DQQLVYSLPF KDMDKFSGLF SALDSHSNLG VISYGVSMTT
LEDVFLKLEV EAEIDQADYS VFTQQPLEEE MDSKSFDEME QSLLILSETK AALVSTMSLW
KQQMYTIAKF HFFTLKRESK SVRSVLLLLL IFFTVQIFMF LVHHSFKNAV VPIKLVPDLY
FLKPGDKPHK YKTSLLLQNS ADSDISDLIS FFTSQNIMVT MINDSDYVSV APHSAALNVM
HSEKDYVFAA VFNSTMVYSL PILVNIISNY YLYHLNVTET IQIWSTPFFQ EITDIVFKIE
LYFQAALLGI IVTAMPPYFA MENAENHKIK AYTQLKLSGL LPSAYWIGQA VVDIPLFFII
LILMLGSLLA FHYGLYFYTV KFLAVVFCLI GYVPSVILFT YIASFTFKKI LNTKEFWSFI
YSVAALACIA ITEITFFMGY TIATILHYAF CIIIPIYPLL GCLISFIKIS WKNVRKNVDT
YNPWDRLSVA VISPYLQCVL WIFLLQYYEK KYGGRSIRKD PFFRNLSTKS KNRKLPEPPD
NEDEDEDVKA ERLKVKELMG CQCCEEKPSI MVSNLHKEYD DKKDFLLSRK VKKVATKYIS
FCVKKGEILG LLGPNGAGKS TIINILVGDI EPTSGQVFLG DYSSETSEDD DSLKCMGYCP
QINPLWPDTT LQEHFEIYGA VKGMSASDMK EVISRITHAL DLKEHLQKTV KKLPAGIKRK
LCFALSMLGN PQITLLDEPS TGMDPKAKQH MWRAIRTAFK NRKRAAILTT HYMEEAEAVC
DRVAIMVSGQ LRCIGTVQHL KSKFGKGYFL EIKLKDWIEN LEVDRLQREI QYIFPNASRQ
ESFSSILAYK IPKEDVQSLS QSFFKLEEAK HAFAIEEYSF SQATLEQVFV ELTKEQEEED
NSCGTLNSTL WWERTQEDRV VF
