AB2C_ARATH
ID AB2C_ARATH Reviewed; 1623 AA.
AC Q42093; O22449; O24526; O48907; O48908; O64590;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ABC transporter C family member 2;
DE Short=ABC transporter ABCC.2;
DE Short=AtABCC2;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 2;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 2;
DE AltName: Full=Multidrug resistance-associated protein 2;
GN Name=ABCC2; Synonyms=EST4, MRP2; OrderedLocusNames=At2g34660;
GN ORFNames=T29F13.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9528668; DOI=10.1016/s0005-2736(97)00213-7;
RA Marin E., Leonhardt N., Vavasseur A., Forestier C.;
RT "Cloning of AtMRP1, an Arabidopsis thaliana cDNA encoding a homologue of
RT the mammalian multidrug resistance-associated protein.";
RL Biochim. Biophys. Acta 1369:7-13(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9490749; DOI=10.2307/3870704;
RA Lu Y.-P., Li Z.-S., Drozdowicz Y.M., Hoertensteiner S., Martinoia E.,
RA Rea P.A.;
RT "AtMRP2, an Arabidopsis ATP-binding cassette transporter able to transport
RT glutathione S-conjugates and chlorophyll catabolites: functional
RT comparisons with AtMRP1.";
RL Plant Cell 10:267-282(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1174-1295.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Desprez T., Amselem J., Chiapello H., Caboche M., Hofte H.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1491, AND INDUCTION.
RX PubMed=9271206; DOI=10.1016/s0014-5793(97)00702-3;
RA Tommasini R., Vogt E., Schmid J., Fromentau M., Amrhein N., Martinoia E.;
RT "Differential expression of genes coding for ABC transporters after
RT treatment of Arabidopsis thaliana with xenobiotics.";
RL FEBS Lett. 411:206-210(1997).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11115509; DOI=10.1074/jbc.m009690200;
RA Liu G., Sanchez-Fernandez R., Li Z.-S., Rea P.A.;
RT "Enhanced multispecificity of Arabidopsis vacuolar multidrug resistance-
RT associated protein-type ATP-binding cassette transporter, AtMRP2.";
RL J. Biol. Chem. 276:8648-8656(2001).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [9]
RP GENE FAMILY.
RX PubMed=11855639; DOI=10.1007/s004250100661;
RA Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT "Multifunctionality of plant ABC transporters -- more than just
RT detoxifiers.";
RL Planta 214:345-355(2002).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
RA Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D.,
RA Martinoia E., Schulz B.;
RT "Family business: the multidrug-resistance related protein (MRP) ABC
RT transporter genes in Arabidopsis thaliana.";
RL Planta 216:107-119(2002).
RN [11]
RP INTERACTION WITH FKBP42/TWD1.
RX PubMed=15133126; DOI=10.1091/mbc.e03-11-0831;
RA Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N.,
RA Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B.,
RA Martinoia E.;
RT "Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar
RT ABC transporters.";
RL Mol. Biol. Cell 15:3393-3405(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [13]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
CC -!- FUNCTION: Pump for glutathione S-conjugates. Mediates the transport of
CC S-conjugates such as GSH, S-(2,4-dinitrophenyl)-glutathione (DNP-GS),
CC GSSG, cyanidin 3-glucoside-GS (C3G-GS) and metolachlor-GS (MOC-GS),
CC glucuronides such as 17-beta-estradiol 17-(beta-D-glucuronide)
CC (E(2)17betaG), and of the chlorophyll catabolite such as B.napus
CC nonfluorescent chlorophyll catabolite (Bn-NCC-1).
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- ACTIVITY REGULATION: Reciprocal promotion of DNP-GS and E(2)17betaG
CC uptake. E(2)17betaG uptake is also stimulated by GSH and S-methyl-
CC glutathione (S-methyl-GS), and, to a lower extent, by GSSG and C3G-GS.
CC Metolachlor-GS and decyl-GS slightly inhibit E(2)17betaG uptake.
CC {ECO:0000269|PubMed:11115509}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=750 uM for E(2)17betaG (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC KM=240 uM for E(2)17betaG (with 100 uM DNP-GS at pH 8.0 and 25
CC degrees Celsius) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC KM=4.7 uM for E(2)17betaG (with 500 uM GSH at pH 8.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC KM=66 uM for DNP-GS (at pH 8) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC KM=20 uM for DNP-GS (with 100 uM E(2)17betaG at pH 8 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC KM=73 uM for GSSG (at pH 8) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC KM=75 uM for MOC-GS (at pH 8) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC KM=15 uM for Bn-NCC-1 (at pH 8) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC Vmax=8.8 nmol/min/mg enzyme with E(2)17betaG as substrate (at pH 8.0
CC and 25 degrees Celsius) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC Vmax=11.5 nmol/min/mg enzyme with E(2)17betaG as substrate (with 100
CC uM DNP-GS at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC Vmax=33 nmol/min/mg enzyme with E(2)17betaG as substrate (with 500 uM
CC GSH at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC Vmax=2 nmol/min/mg enzyme with DNP-GS as substrate (at pH 8 and 25
CC degrees Celsius) {ECO:0000269|PubMed:11115509,
CC ECO:0000269|PubMed:9490749};
CC Vmax=1.8 nmol/min/mg enzyme with DNP-GS as substrate (with 100 uM
CC E(2)17betaG at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC Vmax=3.8 nmol/min/mg enzyme with GSSG as substrate (at pH 8)
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC Vmax=13.6 nmol/min/mg enzyme with MOC-GS as substrate (at pH 8)
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC Vmax=6.3 nmol/min/mg enzyme with Bn-NCC-1 as substrate (at pH 8)
CC {ECO:0000269|PubMed:11115509, ECO:0000269|PubMed:9490749};
CC -!- SUBUNIT: Interacts with FKBP42/TWD1 and probably with calmodulin (CaM).
CC {ECO:0000269|PubMed:15133126}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC Note=Tonoplast. {ECO:0000269|PubMed:11115509}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, at low levels.
CC {ECO:0000269|PubMed:12430019, ECO:0000269|PubMed:9490749}.
CC -!- INDUCTION: By 1-chloro-2,4-dinitrobenzene (CDNB).
CC {ECO:0000269|PubMed:9271206}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04246.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC49798.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA81250.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF014960; AAC49988.1; -; mRNA.
DR EMBL; AF020288; AAC04245.1; -; mRNA.
DR EMBL; AF020289; AAC04246.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AC003096; AAC16268.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09005.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09006.1; -; Genomic_DNA.
DR EMBL; Z26467; CAA81250.1; ALT_FRAME; mRNA.
DR EMBL; U96400; AAC49798.1; ALT_FRAME; mRNA.
DR PIR; T01369; T01369.
DR RefSeq; NP_001189675.1; NM_001202746.1.
DR RefSeq; NP_181013.1; NM_129020.3.
DR AlphaFoldDB; Q42093; -.
DR SMR; Q42093; -.
DR BioGRID; 3377; 1.
DR IntAct; Q42093; 1.
DR STRING; 3702.AT2G34660.1; -.
DR TCDB; 3.A.1.208.5; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q42093; -.
DR PaxDb; Q42093; -.
DR PRIDE; Q42093; -.
DR ProteomicsDB; 243291; -.
DR EnsemblPlants; AT2G34660.1; AT2G34660.1; AT2G34660.
DR EnsemblPlants; AT2G34660.2; AT2G34660.2; AT2G34660.
DR GeneID; 818031; -.
DR Gramene; AT2G34660.1; AT2G34660.1; AT2G34660.
DR Gramene; AT2G34660.2; AT2G34660.2; AT2G34660.
DR KEGG; ath:AT2G34660; -.
DR Araport; AT2G34660; -.
DR TAIR; locus:2061559; AT2G34660.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_2_1; -.
DR InParanoid; Q42093; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q42093; -.
DR BioCyc; ARA:AT2G34660-MON; -.
DR PRO; PR:Q42093; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q42093; baseline and differential.
DR Genevisible; Q42093; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:1902417; F:(+)-abscisic acid D-glucopyranosyl ester transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:1902418; P:(+)-abscisic acid D-glucopyranosyl ester transmembrane transport; IDA:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
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; Calmodulin-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1623
FT /note="ABC transporter C family member 2"
FT /id="PRO_0000226073"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1032..1054
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1058..1077
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1143..1163
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 302..582
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 614..838
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 921..1205
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1242..1476
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 842..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1251
FT /note="Interaction with calmodulin and FKP42/TWD1"
FT /evidence="ECO:0000250"
FT COMPBIAS 859..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1276..1283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 21
FT /note="Q -> T (in Ref. 2; AAC04245/AAC04246)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="A -> T (in Ref. 1; AAC49988)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="W -> C (in Ref. 1; AAC49988)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="H -> R (in Ref. 1; AAC49988)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="A -> P (in Ref. 2; AAC04245)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="V -> G (in Ref. 2; AAC04245/AAC04246)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="F -> S (in Ref. 1; AAC49988)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="K -> N (in Ref. 2; AAC04245)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="L -> V (in Ref. 2; AAC04246)"
FT /evidence="ECO:0000305"
FT CONFLICT 1250
FT /note="R -> C (in Ref. 1; AAC49988)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294..1295
FT /note="EV -> GG (in Ref. 5; CAA81250)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="K -> E (in Ref. 2; AAC04245)"
FT /evidence="ECO:0000305"
FT CONFLICT 1392
FT /note="A -> G (in Ref. 1; AAC49988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1623 AA; 182130 MW; F074F0F6ED7A4D47 CRC64;
MGFEFIEWYC KPVPNGVWTK QVANAFGAYT PCATDSFVLG ISQLVLLVLC LYRIWLALKD
HKVERFCLRS RLYNYFLALL AAYATAEPLF RLIMGISVLD FDGPGLPPFE AFGLGVKAFA
WGAVMVMILM ETKIYIRELR WYVRFAVIYA LVGDMVLLNL VLSVKEYYSS YVLYLYTSEV
GAQVLFGILL FMHLPNLDTY PGYMPVRSET VDDYEYEEIS DGQQICPEKH ANIFDKIFFS
WMNPLMTLGS KRPLTEKDVW YLDTWDQTET LFTSFQHSWD KELQKPQPWL LRALNNSLGG
RFWWGGFWKI GNDCSQFVGP LLLNQLLKSM QEDAPAWMGY IYAFSIFVGV VFGVLCEAQY
FQNVMRVGYR LRSALIAAVF RKSLRLTNEG RRKFQTGKIT NLMTTDAESL QQICQSLHTM
WSAPFRIIIA LILLYQQLGV ASLIGALLLV LMFPLQTVII SKMQKLTKEG LQRTDKRIGL
MNEVLAAMDT VKCYAWENSF QSKVQTVRDD ELSWFRKSQL LGALNMFILN SIPVLVTIVS
FGVFTLLGGD LTPARAFTSL SLFAVLRFPL FMLPNIITQV VNANVSLKRL EEVLATEERI
LLPNPPIEPG EPAISIRNGY FSWDSKGDRP TLSNINLDVP LGSLVAVVGS TGEGKTSLIS
AILGELPATS DAIVTLRGSV AYVPQVSWIF NATVRDNILF GSPFDREKYE RAIDVTSLKH
DLELLPGGDL TEIGERGVNI SGGQKQRVSM ARAVYSNSDV YIFDDPLSAL DAHVGQQVFE
KCIKRELGQK TRVLVTNQLH FLSQVDRIVL VHEGTVKEEG TYEELSSNGP LFQRLMENAG
KVEEYSEENG EAEADQTAEQ PVANGNTNGL QMDGSDDKKS KEGNKKGGKS VLIKQEERET
GVVSWRVLKR YQDALGGAWV VMMLLLCYVL TEVFRVTSST WLSEWTDAGT PKSHGPLFYN
LIYALLSFGQ VLVTLTNSYW LIMSSLYAAK KLHDNMLHSI LRAPMSFFHT NPLGRIINRF
AKDLGDIDRT VAVFVNMFMG QVSQLLSTVV LIGIVSTLSL WAIMPLLVLF YGAYLYYQNT
AREVKRMDSI SRSPVYAQFG EALNGLSTIR AYKAYDRMAD INGRSMDNNI RFTLVNMGAN
RWLGIRLETL GGLMIWLTAS FAVMQNGRAE NQQAFASTMG LLLSYALNIT SLLTGVLRLA
SLAENSLNAV ERVGNYIEIP PEAPPVIENN RPPPGWPSSG SIKFEDVVLR YRPQLPPVLH
GVSFFIHPTD KVGIVGRTGA GKSSLLNALF RIVEVEKGRI LIDDCDVGKF GLMDLRKVLG
IIPQSPVLFS GTVRFNLDPF GEHNDADLWE SLERAHLKDT IRRNPLGLDA EVSEAGENFS
VGQRQLLSLS RALLRRSKIL VLDEATAAVD VRTDALIQKT IREEFKSCTM LIIAHRLNTI
IDCDKILVLD SGRVQEFSSP ENLLSNEGSS FSKMVQSTGA ANAEYLRSLV LDNKRAKDDS
HHLQGQRKWL ASSRWAAAAQ FALAASLTSS HNDLQSLEIE DDSSILKRTN DAVVTLRSVL
EGKHDKEIAE SLEEHNISRE GWLSSLYRMV EGLAVMSRLA RNRMQQPDYN FEGNTFDWDN
VEM
