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   24-JAN-2024, entry version 159.
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.
DR   RefSeq; XP_016879894.1; XM_017024405.1.
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   GlyCosmos; Q8N139; 3 sites, No reported glycans.
DR   GlyGen; Q8N139; 3 sites.
DR   iPTMnet; Q8N139; -.
DR   PhosphoSitePlus; Q8N139; -.
DR   SwissPalm; Q8N139; -.
DR   BioMuta; ABCA6; -.
DR   DMDM; 115503764; -.
DR   EPD; Q8N139; -.
DR   jPOST; Q8N139; -.
DR   MassIVE; Q8N139; -.
DR   PaxDb; 9606-ENSP00000284425; -.
DR   PeptideAtlas; 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; 180 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   AGR; HGNC:36; -.
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; ITSQIVF; -.
DR   OrthoDB; 6951at2759; -.
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; 26 hits in 1153 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 129 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
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: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:0006869; P:lipid transport; IBA:GO_Central.
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; IPR026082; ABCA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19229:SF13; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 6; 1.
DR   PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   Pfam; PF12698; ABC2_membrane_3; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; Q8N139; HS.
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
//