ABCA5_MOUSE
ID ABCA5_MOUSE Reviewed; 1642 AA.
AC Q8K448; Q3TE17; Q3UUB4; Q6P1Y0; Q6ZPG4; Q810C7; Q8BM46; Q8BXG7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cholesterol transporter ABCA5 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:25125465, ECO:0000305|PubMed:32687853};
DE AltName: Full=ATP-binding cassette sub-family A member 5 {ECO:0000305};
GN Name=Abca5 {ECO:0000312|MGI:MGI:2386607}; Synonyms=Kiaa1888;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=12532264; DOI=10.1007/s00335-002-2229-9;
RA Annilo T., Chen Z.-Q., Shulenin S., Dean M.;
RT "Evolutionary analysis of a cluster of ATP-binding cassette (ABC) genes.";
RL Mamm. Genome 14:7-20(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC TISSUE=Brain;
RX PubMed=15870284; DOI=10.1128/mcb.25.10.4138-4149.2005;
RA Kubo Y., Sekiya S., Ohigashi M., Takenaka C., Tamura K., Nada S., Nishi T.,
RA Yamamoto A., Yamaguchi A.;
RT "ABCA5 resides in lysosomes, and ABCA5 knockout mice develop lysosomal
RT disease-like symptoms.";
RL Mol. Cell. Biol. 25:4138-4149(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1589.
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Dendritic cell, Embryo, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1480.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1034-1642.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [6]
RP INDUCTION.
RX PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
RA Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
RT "Acute digoxin loading reduces ABCA8A mRNA expression in the mouse liver.";
RL Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION.
RX PubMed=20382126; DOI=10.1016/j.bbrc.2010.04.027;
RA Ye D., Meurs I., Ohigashi M., Calpe-Berdiel L., Habets K.L., Zhao Y.,
RA Kubo Y., Yamaguchi A., Van Berkel T.J., Nishi T., Van Eck M.;
RT "Macrophage ABCA5 deficiency influences cellular cholesterol efflux and
RT increases susceptibility to atherosclerosis in female LDLr knockout mice.";
RL Biochem. Biophys. Res. Commun. 395:387-394(2010).
RN [9]
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 [10]
RP TISSUE SPECIFICITY, AND FUNCTION.
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).
RN [11]
RP INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=32687853; DOI=10.1016/j.jmb.2020.07.006;
RA Ray A.G., Choudhury K.R., Chakraborty S., Chakravarty D., Chander V.,
RA Jana B., Siddiqui K.N., Bandyopadhyay A.;
RT "Novel Mechanism of Cholesterol Transport by ABCA5 in Macrophages and Its
RT Role in Dyslipidemia.";
RL J. Mol. Biol. 432:4922-4941(2020).
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, PubMed:32687853,
CC PubMed:20382126). May play a role in the processing of autolysosomes
CC (PubMed:15870284). {ECO:0000269|PubMed:15870284,
CC ECO:0000269|PubMed:20382126, ECO:0000269|PubMed:25125465,
CC ECO:0000269|PubMed:32687853}.
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, ECO:0000305|PubMed:32687853};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000305|PubMed:25125465, ECO:0000305|PubMed:32687853};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8CF82}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8CF82}. Lysosome membrane
CC {ECO:0000269|PubMed:15870284}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15870284}. Late endosome membrane
CC {ECO:0000269|PubMed:15870284}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15870284}. Cell membrane
CC {ECO:0000269|PubMed:32687853}. Note=Localized at cell membrane under
CC high cholesterol levels. {ECO:0000269|PubMed:32687853}.
CC -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes, oligodendrocytes and
CC astrocytes in brain, alveolar type 2 cells in lung and follicular cells
CC in the thyroid gland (at protein level). Detected in brain, testis,
CC lung, heart, liver, kidney, skeletal muscle and placenta. Strongly
CC expressed in the basal cells of the seminiferous tubules, interstitial
CC cells consisting of Leydig cells, as well as the tunica albuginea
CC (PubMed:24831815). In the epididymis, specificly and very strongly
CC expressed in the connective tissue outlining the cylindrical epithelium
CC in the corpus and cauda regions, including fibrocytes and smooth muscle
CC cells, as well as within the basal and tall columnar cells of the
CC corpus cylindrical epithelium (PubMed:24831815). Highly expressed in
CC the brain with high expression in cortical and hippocampal neurons and
CC moderately in the lung (PubMed:25125465). {ECO:0000269|PubMed:12532264,
CC ECO:0000269|PubMed:15870284, ECO:0000269|PubMed:24831815,
CC ECO:0000269|PubMed:25125465}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC {ECO:0000269|PubMed:12532264}.
CC -!- INDUCTION: Down-regulated by digoxin (PubMed:16445568). Up-regulated by
CC an excess cellular cholesterol level (PubMed:32687853). Up-regulated
CC when ABCA1 is down-regulated (PubMed:32687853).
CC {ECO:0000269|PubMed:16445568, ECO:0000269|PubMed:32687853}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15870284}.
CC -!- DISRUPTION PHENOTYPE: Mice display hypothyroidism and lethal heart
CC abnormalities that may be due to altered autolysosomes processing.
CC {ECO:0000269|PubMed:15870284}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28896.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF491842; AAM90895.1; -; mRNA.
DR EMBL; AB097675; BAC66658.1; -; mRNA.
DR EMBL; AK034961; BAC28896.2; ALT_INIT; mRNA.
DR EMBL; AK047188; BAC32984.1; -; mRNA.
DR EMBL; AK138604; BAE23713.1; -; mRNA.
DR EMBL; AK169879; BAE41431.1; -; mRNA.
DR EMBL; BC064823; AAH64823.1; ALT_SEQ; mRNA.
DR EMBL; AK129463; BAC98273.1; -; mRNA.
DR CCDS; CCDS25591.1; -.
DR RefSeq; NP_671752.2; NM_147219.2.
DR RefSeq; XP_006533128.1; XM_006533065.3.
DR AlphaFoldDB; Q8K448; -.
DR SMR; Q8K448; -.
DR BioGRID; 229877; 4.
DR STRING; 10090.ENSMUSP00000047927; -.
DR GlyGen; Q8K448; 5 sites.
DR iPTMnet; Q8K448; -.
DR PhosphoSitePlus; Q8K448; -.
DR MaxQB; Q8K448; -.
DR PaxDb; Q8K448; -.
DR PeptideAtlas; Q8K448; -.
DR PRIDE; Q8K448; -.
DR ProteomicsDB; 285952; -.
DR Antibodypedia; 19335; 181 antibodies from 28 providers.
DR DNASU; 217265; -.
DR Ensembl; ENSMUST00000043961; ENSMUSP00000047927; ENSMUSG00000018800.
DR GeneID; 217265; -.
DR KEGG; mmu:217265; -.
DR UCSC; uc007mdm.1; mouse.
DR CTD; 23461; -.
DR MGI; MGI:2386607; Abca5.
DR VEuPathDB; HostDB:ENSMUSG00000018800; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000158172; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8K448; -.
DR OMA; HGLYFYA; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q8K448; -.
DR TreeFam; TF105192; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR BioGRID-ORCS; 217265; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Abca5; mouse.
DR PRO; PR:Q8K448; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K448; protein.
DR Bgee; ENSMUSG00000018800; Expressed in otolith organ and 185 other tissues.
DR ExpressionAtlas; Q8K448; baseline and differential.
DR Genevisible; Q8K448; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; IDA:BHF-UCL.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA: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; IMP:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP: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; IMP:BHF-UCL.
DR GO; GO:1903064; P:positive regulation of reverse cholesterol transport; IMP: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 ATP-binding; Cell membrane; Endosome; Glycoprotein; Golgi apparatus;
KW 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_0000250670"
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 864..884
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 1138..1158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1164..1184
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 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 388
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 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 96
FT /note="S -> C (in Ref. 3; BAC32984)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="K -> E (in Ref. 3; BAE41431)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="K -> E (in Ref. 3; BAC32984)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="K -> E (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> V (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="A -> P (in Ref. 3; BAC32984)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="L -> P (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="M -> I (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="E -> G (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="L -> P (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="K -> N (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="F -> V (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 1231
FT /note="I -> K (in Ref. 4; AAH64823)"
FT /evidence="ECO:0000305"
FT CONFLICT 1503
FT /note="V -> G (in Ref. 1; AAM90895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1642 AA; 185895 MW; 177A5FC0B075DFC5 CRC64;
MATAIRDVGV WRQTRTLLLK NYLIKCRTKK SSVQEILFPL FFLFWLILVS MMHPNKKYEE
VSDIELSPMD KFSLSNVILG YTPVTNITSS IMQRVSTDHL PKVIVTEEYA NEKELVAASL
SKSSNFVGVV FKDTMSYELR FFPEMIPVSS IYMNSREGCS KTCDAAQYWS LGFTVLQASI
DAAIIQLKTN VSVWSELEST KAVIMGEAAV VEIDTFPRGV ILIYLVIAFS PFGYFLAIHI
VAEKEKKLKE FLKIMGLHDT AFWLSWVLLY ASLIFLMSLL MAVIATASSL FPQSSSIVIF
LLFFLYGLSS VFFALMLTPL FKKSKHVGVV EFFVTVVFGF VGLLIVLIES FPRSLVWLFS
PLCQCAFLIG IAQVMHLEDF NEGALFSNLT EGPYPLIITI IMLALDSVFY VLLAVYLDQV
IPGEFGLRRS SLYFLKPSYW SKNKRNYKEL SEGNINGNIS LNEIVEPVSS EFIGKEAIRI
SGIQKSYRKK TENVEALRNL SFDIYEGQIT ALLGHSGTGK STLMNILCGL CPPSDGFASI
YGHRVSEIDE MFEARKMIGI CPQSDINFDV LTVEENLSIL ASIKGIPANN IIQEVQKVLL
DLDMQAIKDN QAKKLSGGQK RKLSVGIAVL GNPKILLLDE PTAGMDPCSR HIVWNLLKYR
KANRVTVFST HFMDEADILA DRKAVISQGM LKCVGSSIFL KSKWGIGYRL SMYIDRYCAT
ESLSSLVRQH IPAAALLQQN DQQLVYSLPF KDMDKFSGLF SALDIHSNLG VISYGVSMTT
LEDVFLKLEV EAEIDQADYS VFTQQPREEE TDSKSFDEME QSLLILSETK ASSVSTMSLW
KQQVSTIAKF HFLSLKRESK SVRAVLLLLL IFFAVQIFMF FLHHSFKNAV VPIKLVPDLY
FLKPGDKPHK YKTSLLLQNS TDSDINGLIE FFAHQNIMVA MFNDSDYVSA APHSAALNVV
RSEKDYVFSA VFNSTMVYCL PVMMNIISNY YLYHLNVTEA IQTWSTPFIQ EITDIVFKIE
LYFQAALLGI IVTAMPPYFA MENAENHKIK AYTQLKLSGL LPSAYWVGQA VVDIPLFFVV
LILMLGSLFA FHHGLYFYPA KFLAVVFCLI AYVPSVILFT YIASFTFKKI LNTKEFWSFI
YSVTALACVA ITETTFFLQY AVTAVFHYTF CIAIPIYPLL GCLISFIKGS WKNMPKNENT
YNPWDRLLVA VIMPYLQCIL WIFLLQHYEK IHGGRSIRKD PFFRALSQKA KNKKFPEPPI
NEDEDEDVKA ERLKVKELMG CQCCEEKPAI MVCNLHKEYD DKKDFLHSRK TTKVATKYIS
FCVKKGEILG LLGPNGAGKS TVINTLVGDV EPTSGKIFLG DYGSHSSEDD ESIKCMGYCP
QTNPLWPDLT LQEHFEIYGA VKGMSPGDMK EVISRITKAL DLKEHLQKTV KKLPAGIKRK
LCFALSMLGN PQVTLLDEPS TGMDPRAKQH MWRAIRTAFK NKKRAALLTT HYMEEAEAVC
DRVAIMVSGQ LRCIGTVQHL KSKFGKGYFL EIKLKDWIEN LEIDRLQREI QYIFPNASRQ
ESFSSILAFK IPKEDVQSLS QSFAKLEEAK RTFAIEEYSF SQATLEQVFV ELTKEQEEED
NSCGTLASTL WWERTQEDRV VF
