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   24-JAN-2024, entry version 155.
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; 5.
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   GlyCosmos; Q8WWZ7; 3 sites, No reported glycans.
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; 9606-ENSP00000376443; -.
DR   PeptideAtlas; Q8WWZ7; -.
DR   ProteomicsDB; 74970; -. [Q8WWZ7-1]
DR   ProteomicsDB; 74971; -. [Q8WWZ7-2]
DR   ProteomicsDB; 74972; -. [Q8WWZ7-3]
DR   Antibodypedia; 19335; 188 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   AGR; HGNC:35; -.
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; ITYFMGY; -.
DR   OrthoDB; 6951at2759; -.
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 1153 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 204 other cell types or tissues.
DR   ExpressionAtlas; Q8WWZ7; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd03263; ABC_subfamily_A; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR026082; ABCA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   PANTHER; PTHR19229:SF100; CHOLESTEROL TRANSPORTER ABCA5; 1.
DR   Pfam; PF12698; ABC2_membrane_3; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; Q8WWZ7; HS.
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
//