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   24-JAN-2024, entry version 144.
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};
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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   GlyCosmos; Q8K448; 5 sites, No reported glycans.
DR   GlyGen; Q8K448; 5 sites.
DR   iPTMnet; Q8K448; -.
DR   PhosphoSitePlus; Q8K448; -.
DR   SwissPalm; Q8K448; -.
DR   MaxQB; Q8K448; -.
DR   PaxDb; 10090-ENSMUSP00000047927; -.
DR   PeptideAtlas; Q8K448; -.
DR   ProteomicsDB; 285952; -.
DR   Pumba; Q8K448; -.
DR   Antibodypedia; 19335; 188 antibodies from 28 providers.
DR   DNASU; 217265; -.
DR   Ensembl; ENSMUST00000043961.12; ENSMUSP00000047927.6; ENSMUSG00000018800.15.
DR   GeneID; 217265; -.
DR   KEGG; mmu:217265; -.
DR   UCSC; uc007mdm.1; mouse.
DR   AGR; MGI:2386607; -.
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; ITYFMGY; -.
DR   OrthoDB; 6951at2759; -.
DR   PhylomeDB; Q8K448; -.
DR   TreeFam; TF105192; -.
DR   Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR   BioGRID-ORCS; 217265; 3 hits in 77 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 187 other cell types or tissues.
DR   ExpressionAtlas; Q8K448; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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: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; 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   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; Q8K448; MM.
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
//