MRP6_MOUSE
ID MRP6_MOUSE Reviewed; 1498 AA.
AC Q9R1S7; A2TAJ0; A2TAJ1; F8VPT2; Q80YB6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ATP-binding cassette sub-family C member 6;
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O88269};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:O95255};
DE AltName: Full=Multidrug resistance-associated protein 6;
GN Name=Abcc6; Synonyms=Mrp6;
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].
RC STRAIN=ddY; TISSUE=Liver;
RA Morikawa A., Suzuki H., Hirohashi T., Sugiyama Y.;
RT "Mus musculus mRNA for multidrug resistance-associated protein 6 (MRP6),
RT complete cds.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ, and DBA/2J; TISSUE=Kidney;
RX PubMed=17360558; DOI=10.1073/pnas.0607620104;
RA Meng H., Vera I., Che N., Wang X., Wang S.S., Ingram-Drake L., Schadt E.E.,
RA Drake T.A., Lusis A.J.;
RT "Identification of Abcc6 as the major causal gene for dystrophic cardiac
RT calcification in mice through integrative genomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4530-4535(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 685-1498.
RC STRAIN=FVB/N; TISSUE=Liver;
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 DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=15888484; DOI=10.1093/hmg/ddi183;
RA Gorgels T.G., Hu X., Scheffer G.L., van der Wal A.C., Toonstra J.,
RA de Jong P.T., van Kuppevelt T.H., Levelt C.N., de Wolf A., Loves W.J.,
RA Scheper R.J., Peek R., Bergen A.A.;
RT "Disruption of Abcc6 in the mouse: novel insight in the pathogenesis of
RT pseudoxanthoma elasticum.";
RL Hum. Mol. Genet. 14:1763-1773(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 SUBCELLULAR LOCATION.
RX PubMed=23625951; DOI=10.1161/circresaha.111.300194;
RA Pomozi V., Le Saux O., Brampton C., Apana A., Ilias A., Szeri F.,
RA Martin L., Monostory K., Paku S., Sarkadi B., Szakacs G., Varadi A.;
RT "ABCC6 is a basolateral plasma membrane protein.";
RL Circ. Res. 112:E148-E151(2013).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=24277820; DOI=10.1073/pnas.1319582110;
RA Jansen R.S., Kuecuekosmanoglu A., de Haas M., Sapthu S., Otero J.A.,
RA Hegman I.E., Bergen A.A., Gorgels T.G., Borst P., van de Wetering K.;
RT "ABCC6 prevents ectopic mineralization seen in pseudoxanthoma elasticum by
RT inducing cellular nucleotide release.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20206-20211(2013).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that actively extrudes physiological compounds, and xenobiotics
CC from cells. Mediates ATP-dependent transport of glutathione conjugates
CC such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-
CC GS) (in vitro), and an anionic cyclopentapeptide endothelin antagonist,
CC BQ-123. {ECO:0000250|UniProtKB:O95255}.
CC -!- FUNCTION: Mediates the release of nucleoside triphosphates,
CC predominantly ATP, into the circulation, where it is rapidly converted
CC into AMP and the mineralization inhibitor inorganic pyrophosphate (PPi)
CC by the ecto-enzyme ectonucleotide pyrophosphatase phosphodiesterase 1
CC (ENPP1), therefore playing a role in PPi homeostasis.
CC {ECO:0000250|UniProtKB:O95255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:O95255};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:O95255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95255};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:O95255};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:15888484, ECO:0000269|PubMed:23625951}; Multi-pass
CC membrane protein {ECO:0000255, ECO:0000269|PubMed:23625951}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:O95255}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice spontaneously develop
CC calcification and elastic fiber abnormalities in blood vessels and
CC Bruch's membrane in the eye, whereas no clear changes were seen in the
CC extracellular matrix of the skin. Calcification of blood vessels is
CC most prominent in small arteries in the cortex of the kidney, but in
CC old mice, it occurrs also in other organs and in the aorta and vena
CC cava (PubMed:15888484). Mice have reduced inorganic pyrophosphate (PPi)
CC plasma levels, a strong inhibitor of mineralization (PubMed:24277820).
CC {ECO:0000269|PubMed:15888484, ECO:0000269|PubMed:24277820}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AB028737; BAA83820.1; -; mRNA.
DR EMBL; EF109740; ABM89087.1; -; mRNA.
DR EMBL; EF109741; ABM89088.1; -; mRNA.
DR EMBL; AC115036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049980; AAH49980.1; -; mRNA.
DR CCDS; CCDS21272.1; -.
DR RefSeq; NP_061265.2; NM_018795.2.
DR AlphaFoldDB; Q9R1S7; -.
DR SMR; Q9R1S7; -.
DR STRING; 10090.ENSMUSP00000002850; -.
DR GlyGen; Q9R1S7; 2 sites.
DR iPTMnet; Q9R1S7; -.
DR PhosphoSitePlus; Q9R1S7; -.
DR SwissPalm; Q9R1S7; -.
DR jPOST; Q9R1S7; -.
DR MaxQB; Q9R1S7; -.
DR PaxDb; Q9R1S7; -.
DR PeptideAtlas; Q9R1S7; -.
DR PRIDE; Q9R1S7; -.
DR ProteomicsDB; 291411; -.
DR Antibodypedia; 11866; 166 antibodies from 32 providers.
DR DNASU; 27421; -.
DR Ensembl; ENSMUST00000002850; ENSMUSP00000002850; ENSMUSG00000030834.
DR GeneID; 27421; -.
DR KEGG; mmu:27421; -.
DR UCSC; uc009gya.1; mouse.
DR CTD; 368; -.
DR MGI; MGI:1351634; Abcc6.
DR VEuPathDB; HostDB:ENSMUSG00000030834; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000157145; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9R1S7; -.
DR OMA; AAMYLTY; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9R1S7; -.
DR TreeFam; TF105199; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 27421; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Abcc6; mouse.
DR PRO; PR:Q9R1S7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R1S7; protein.
DR Bgee; ENSMUSG00000030834; Expressed in liver and 39 other tissues.
DR ExpressionAtlas; Q9R1S7; baseline and differential.
DR Genevisible; Q9R1S7; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0030504; F:inorganic diphosphate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0015867; P:ATP transport; ISS:UniProtKB.
DR GO; GO:0110148; P:biomineralization; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; ISO:MGI.
DR GO; GO:0030505; P:inorganic diphosphate transport; IDA:MGI.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0055062; P:phosphate ion homeostasis; IDA:MGI.
DR GO; GO:0032026; P:response to magnesium ion; IMP:MGI.
DR GO; GO:1904383; P:response to sodium phosphate; IMP:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:MGI.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR030239; ABCC6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF339; PTHR24223:SF339; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1498
FT /note="ATP-binding cassette sub-family C member 6"
FT /id="PRO_0000093367"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 59..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 100..104
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 126..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 138..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 156..173
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..194
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 195..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 301..321
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 322..347
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 348..368
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 369..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 425..445
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 446..448
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 449..469
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 470..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 532..552
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 553..574
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 575..595
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 596..934
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 935..955
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 956..992
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 993..1013
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1014..1056
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1057..1077
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1078
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1079..1099
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1100..1170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1171..1191
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1192..1193
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1194..1214
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1215..1498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 309..592
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 627..851
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 942..1223
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1260..1494
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 855..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 661..668
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1294..1301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="R -> S (in Ref. 1; BAA83820)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="A -> V (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="V -> M (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="L -> Q (in Ref. 2; ABM89087)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> A (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="I -> V (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="F -> L (in Ref. 1; BAA83820)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="R -> G (in Ref. 2; ABM89087)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="L -> P (in Ref. 2; ABM89087)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="V -> L (in Ref. 2; ABM89087)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="R -> C (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="V -> A (in Ref. 1; BAA83820 and 2; ABM89087/
FT ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="K -> R (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="L -> P (in Ref. 2; ABM89087)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="T -> I (in Ref. 1; BAA83820 and 2; ABM89087/
FT ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="L -> Q (in Ref. 2; ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="A -> T (in Ref. 2; ABM89087/ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1370
FT /note="L -> P (in Ref. 2; ABM89087)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="Q -> H (in Ref. 1; BAA83820)"
FT /evidence="ECO:0000305"
FT CONFLICT 1448
FT /note="V -> L (in Ref. 1; BAA83820)"
FT /evidence="ECO:0000305"
FT CONFLICT 1451
FT /note="I -> T (in Ref. 2; ABM89088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1477
FT /note="S -> N (in Ref. 1; BAA83820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1498 AA; 164857 MW; 1F426D8CF629E835 CRC64;
MNRGRSMATP GEQCAGLRVW NQTEQEPAAY HLLSLCFVRA ASSWVPPMYL WVLGPIYLLY
IHRHGRCYLR MSHLFKTKMV LGLALILLYT FNVAVPLWRI HQGVPQAPEL LIHPTVWLTT
MSFATFLIHM ERRKGVRSSG VLFGYWLLCC ILPGINTVQQ ASAGNFRQEP LHHLATYLCL
SLVVAELVLS CLVDQPPFFS EDSQPLNPCP EAEASFPSKA MFWWASGLLW RGYKKLLGPK
DLWSLGRENS SEELVSQLER EWRRSCNGLP GHKGHSSVGA PETEAFLQPE RSQRGPLLRA
IWRVFRSTFL LGTLSLVISD AFRFAVPKLL SLFLEFMGDR NSSAWTGWLL AVLMFAAACL
QTLFEQQHMY RAKVLQMRLR TAITGLVYRK VLVLSSGSRK SSAAGDVVNL VSVDIQRLAE
SIIYLNGLWL LFLWIFVCFV YLWQLLGPSA LTAVAVFLSL LPLNFFITKK RGFHQEEQMR
QKASRARLTS SMLRTVRTIK SHGWEHAFLE RLLHIRGQEL SALKTSTLLF SVSLVSFQVS
TFLVALVVFA VHTLVAEDNA MDAEKAFVTL TVLSILNKAQ AFLPFSVHCI VQARVSFDRL
AAFLCLEEVD PNGMIASNSR RSSKDRISVH NGTFAWSQES PPCLHGINLT VPQGCLLAVV
GPVGAGKSSL LSALLGELLK VEGSVSIEGS VAYVPQEAWV QNTSVVENVC FRQELDLPWL
QKVLDACALG SDVASFPAGV HTPIGEQGMN LSGGQKQRLS LARAVYKKAA IYLLDDPLAA
LDAHVSQQVF KQVIGPSGLL QGTTRILVTH TLHVLPQADR ILVLANGTIA EMGSYQDLLQ
RNGALVGLLD GARQPAGTHD AATSDDLGGF PGGGRPTCRP DRPRPTEAAP VKGRSTSEVQ
MEASLDDPEA TGLTAEEDSV RYGRVKTTIY LSYLRAVGTP LCTYTLFLFL CQQVASFSQG
YWLSLWADDP VVDGRQMHAA LRGWVFGLLG CLQAIGLFAS MAAVFLGGAR ASGLLFRSLL
WDVARSPIGF FERTPVGNLL NRFSKETDTV DVDIPDKLRS LLTYAFGLLE VGLAVTMATP
LAIVAILPLM VLYAGFQSLY VATSCQLRRL ESARYSSVCS HMAETFQGSL VVRAFRAQAS
FTAQHDALMD ENQRVSFPKL VADRWLATNL ELLGNGLVFV AATCAVLSKA HLSAGLVGFS
VSAALQVTQT LQWVVRSWTD LENSMVAVER VQDYARIPKE APWRLPTCAA QPLWPCGGQI
EFRDFGLRHR PELPLAVQGV SLKIHAGEKV GIVGRTGAGK SSLAWGLLRL QEAAEGNIWI
DGVPITHVGL HTLRSRITII PQDPVLFPGS LRMNLDLLQE HTDEGIWAAL ETVQLKAFVT
SLPGQLQYEC AGQGDDLSVG QKQLLCLARA LLRKTQILIL DEATASVDPG TEMQMQAALE
RWFTQCTVLL IAHRLRSVMD CARVLVMDEG QVAESGSPAQ LLAQKGLFYR LAHESGLA
