ABCBA_MOUSE
ID ABCBA_MOUSE Reviewed; 715 AA.
AC Q9JI39; Q542P7; Q9D0C7;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ATP-binding cassette sub-family B member 10, mitochondrial {ECO:0000305};
DE AltName: Full=ABC-mitochondrial erythroid protein {ECO:0000303|PubMed:10835348};
DE Short=ABC-me protein {ECO:0000303|PubMed:10835348};
DE AltName: Full=ATP-binding cassette transporter 10;
DE Short=ABC transporter 10 protein;
DE Flags: Precursor;
GN Name=Abcb10 {ECO:0000312|MGI:MGI:1860508};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Erythroleukemia;
RX PubMed=10835348; DOI=10.1093/emboj/19.11.2492;
RA Shirihai O.S., Gregory T., Yu C., Orkin S.H., Weiss M.J.;
RT "ABC-me: a novel mitochondrial transporter induced by GATA-1 during
RT erythroid differentiation.";
RL EMBO J. 19:2492-2502(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 TRANSIT PEPTIDE CLEAVAGE SITE, AND SUBUNIT.
RX PubMed=15215243; DOI=10.1074/jbc.m405040200;
RA Graf S.A., Haigh S.E., Corson E.D., Shirihai O.S.;
RT "Targeting, import, and dimerization of a mammalian mitochondrial ATP
RT binding cassette (ABC) transporter, ABCB10 (ABC-me).";
RL J. Biol. Chem. 279:42954-42963(2004).
RN [5]
RP INTERACTION WITH SLC25A37, AND INDUCTION.
RX PubMed=19805291; DOI=10.1073/pnas.0904519106;
RA Chen W., Paradkar P.N., Li L., Pierce E.L., Langer N.B.,
RA Takahashi-Makise N., Hyde B.B., Shirihai O.S., Ward D.M., Kaplan J.,
RA Paw B.H.;
RT "Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its
RT stability and function in the erythroid mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16263-16268(2009).
RN [6]
RP INTERACTION WITH FECH, AND INDUCTION.
RX PubMed=20427704; DOI=10.1182/blood-2009-12-259614;
RA Chen W., Dailey H.A., Paw B.H.;
RT "Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10
RT for erythroid heme biosynthesis.";
RL Blood 116:628-630(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Spleen, 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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22240895; DOI=10.1038/cdd.2011.195;
RA Hyde B.B., Liesa M., Elorza A.A., Qiu W., Haigh S.E., Richey L.,
RA Mikkola H.K., Schlaeger T.M., Shirihai O.S.;
RT "The mitochondrial transporter ABC-me (ABCB10), a downstream target of
RT GATA-1, is essential for erythropoiesis in vivo.";
RL Cell Death Differ. 19:1117-1126(2012).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24421385; DOI=10.1128/mcb.00865-13;
RA Yamamoto M., Arimura H., Fukushige T., Minami K., Nishizawa Y.,
RA Tanimoto A., Kanekura T., Nakagawa M., Akiyama S., Furukawa T.;
RT "Abcb10 role in heme biosynthesis in vivo: Abcb10 knockout in mice causes
RT anemia with protoporphyrin IX and iron accumulation.";
RL Mol. Cell. Biol. 34:1077-1084(2014).
RN [10]
RP ACTIVITY REGULATION, MUTAGENESIS OF GLY-497; LYS-498; CYS-547; GLY-602;
RP GLU-624 AND CYS-675, GLUTATHIONYLATION AT CYS-547, AND FUNCTION.
RX PubMed=26053025; DOI=10.1371/journal.pone.0129772;
RA Qiu W., Liesa M., Carpenter E.P., Shirihai O.S.;
RT "ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by
RT Glutathione.";
RL PLoS ONE 10:e0129772-e0129772(2015).
RN [11]
RP FUNCTION.
RX PubMed=28808058; DOI=10.1074/jbc.m117.797415;
RA Seguin A., Takahashi-Makise N., Yien Y.Y., Huston N.C., Whitman J.C.,
RA Musso G., Wallace J.A., Bradley T., Bergonia H.A., Kafina M.D.,
RA Matsumoto M., Igarashi K., Phillips J.D., Paw B.H., Kaplan J., Ward D.M.;
RT "Reductions in the mitochondrial ABC transporter Abcb10 affect the
RT transcriptional profile of heme biosynthesis genes.";
RL J. Biol. Chem. 292:16284-16299(2017).
RN [12]
RP SUBUNIT.
RX PubMed=30765471; DOI=10.3324/haematol.2018.214320;
RA Maio N., Kim K.S., Holmes-Hampton G., Singh A., Rouault T.A.;
RT "Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an
RT architecturally defined molecular complex required for heme biosynthesis.";
RL Haematologica 104:1756-1767(2019).
CC -!- FUNCTION: Catalyzes the export of an unknown physiological substrate
CC from the mitochondrial matrix to the cytosol in an ATP-dependent manner
CC (PubMed:26053025). May also transport the heme analog Zn (II)
CC mesoporphyrin (ZnMP) in an ATP dependent manner but can't export the
CC heme precursor 5-aminolevulinic acid (ALA) from mitochondria
CC (PubMed:28808058, PubMed:26053025). Plays a role in the early step of
CC the heme biosynthetic process during insertion of iron into
CC protoporphyrin IX (PPIX). In turn participates in hemoglobin synthesis
CC and also protects against oxidative stress (PubMed:22240895,
CC PubMed:28808058, PubMed:24421385). In addition may be involved in
CC mitochondrial unfolded protein response (UPRmt) signaling pathway,
CC although ABCB10 probably does not participate in peptide export from
CC mitochondria (By similarity). {ECO:0000250|UniProtKB:Q9NRK6,
CC ECO:0000269|PubMed:22240895, ECO:0000269|PubMed:24421385,
CC ECO:0000269|PubMed:26053025, ECO:0000269|PubMed:28808058}.
CC -!- ACTIVITY REGULATION: Oxidized glutathione (GSSG) stimulates ATP
CC hydrolysis without affecting ATP binding, whereas reduced glutathione
CC (GSH) inhibits ATP binding and hydrolysis.
CC {ECO:0000269|PubMed:26053025}.
CC -!- SUBUNIT: Homodimer or homooligomer (PubMed:15215243, PubMed:30765471).
CC Interacts with PAAT (By similarity). Interacts with SLC25A37; this
CC interaction stabilizes SLC25A37 and enhances the function of SLC25A37
CC to import mitochondrial iron during erythroid differentiation
CC (PubMed:19805291). Interacts with FECH; this interaction may allow the
CC formation of an oligomeric complex with SLC25A37 (PubMed:20427704).
CC Forms a complex with ABCB7 and FECH, where a dimeric FECH bridges ABCB7
CC and ABCB10 homodimers; this complex may be required for cellular iron
CC homeostasis, mitochondrial function and heme biosynthesis
CC (PubMed:30765471). Interacts with FECH (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRK6, ECO:0000269|PubMed:15215243,
CC ECO:0000269|PubMed:19805291, ECO:0000269|PubMed:20427704,
CC ECO:0000269|PubMed:30765471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10835348}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at particularly high levels in fetal
CC liver, and erythroid tissues of embryos and adults. Found also in adult
CC bone marrow, liver and kidney, and at lower levels in heart, brain and
CC spleen. {ECO:0000269|PubMed:10835348}.
CC -!- DEVELOPMENTAL STAGE: Abundant in the liver but not in non-hematopoietic
CC tissues of 13 dpc embryos. {ECO:0000269|PubMed:10835348}.
CC -!- INDUCTION: By transcription factor GATA-1 during erythroid
CC differentiation and in vitro, by DMSO during terminal erythroid
CC maturation. Induced during cell erythroid differentiation
CC (PubMed:20427704). {ECO:0000269|PubMed:10835348,
CC ECO:0000269|PubMed:20427704}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for ABCB10 are embryonic
CC lethal and embryos are pale and die between 10.5 and 11.5 dpc because
CC of embryonic hematopoietic failure (PubMed:24421385, PubMed:22240895).
CC Embryos are completely resorbed by the uterus by 13.5 dpc and present
CC severe anemia at 10.5 dpc (PubMed:22240895).
CC {ECO:0000269|PubMed:22240895, ECO:0000269|PubMed:24421385}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. {ECO:0000305}.
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DR EMBL; AF266284; AAF76889.1; -; mRNA.
DR EMBL; AK081782; BAC38331.1; -; mRNA.
DR EMBL; BC046818; AAH46818.1; -; mRNA.
DR EMBL; BC053020; AAH53020.1; -; mRNA.
DR EMBL; BC054793; AAH54793.1; -; mRNA.
DR CCDS; CCDS22766.1; -.
DR RefSeq; NP_062425.1; NM_019552.2.
DR AlphaFoldDB; Q9JI39; -.
DR SMR; Q9JI39; -.
DR BioGRID; 207837; 6.
DR IntAct; Q9JI39; 6.
DR STRING; 10090.ENSMUSP00000075011; -.
DR iPTMnet; Q9JI39; -.
DR PhosphoSitePlus; Q9JI39; -.
DR SwissPalm; Q9JI39; -.
DR EPD; Q9JI39; -.
DR jPOST; Q9JI39; -.
DR MaxQB; Q9JI39; -.
DR PaxDb; Q9JI39; -.
DR PeptideAtlas; Q9JI39; -.
DR PRIDE; Q9JI39; -.
DR ProteomicsDB; 285954; -.
DR Antibodypedia; 34677; 228 antibodies from 30 providers.
DR DNASU; 56199; -.
DR Ensembl; ENSMUST00000075578; ENSMUSP00000075011; ENSMUSG00000031974.
DR GeneID; 56199; -.
DR KEGG; mmu:56199; -.
DR UCSC; uc009nwv.1; mouse.
DR CTD; 23456; -.
DR MGI; MGI:1860508; Abcb10.
DR VEuPathDB; HostDB:ENSMUSG00000031974; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000157680; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q9JI39; -.
DR OMA; WGTYLVK; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q9JI39; -.
DR TreeFam; TF105198; -.
DR Reactome; R-MMU-1369007; Mitochondrial ABC transporters.
DR BioGRID-ORCS; 56199; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Abcb10; mouse.
DR PRO; PR:Q9JI39; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9JI39; protein.
DR Bgee; ENSMUSG00000031974; Expressed in fetal liver hematopoietic progenitor cell and 240 other tissues.
DR Genevisible; Q9JI39; MM.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:UniProtKB.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR030260; ABCB10-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF553; PTHR24221:SF553; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Glutathionylation; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..82
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15215243"
FT CHAIN 83..715
FT /note="ATP-binding cassette sub-family B member 10,
FT mitochondrial"
FT /id="PRO_0000000256"
FT TOPO_DOM 83..137
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 159..180
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 202..266
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 288..360
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 382..395
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 417..715
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 136..422
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 457..696
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 492..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRK6"
FT MOD_RES 547
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 497
FT /note="G->A: Decreases ATP binding about 50%."
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 498
FT /note="K->R: Decreases ATP binding about 50%."
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 547
FT /note="C->A: Does not affect ABCB10 glutathionylation."
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 602
FT /note="G->D: Affects ATP hydrolysis but not binding."
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 602
FT /note="G->V: Affects ATP hydrolysis but not binding."
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 624
FT /note="E->Q: Affects ATP hydrolysis but not binding."
FT /evidence="ECO:0000269|PubMed:26053025"
FT MUTAGEN 675
FT /note="C->A: Prevents ABCB10 glutathionylation."
FT /evidence="ECO:0000269|PubMed:26053025"
SQ SEQUENCE 715 AA; 77188 MW; C07BE44A478B89A2 CRC64;
MRAPSARALL LIPRRGPAVR AWAPAVSSRI WLASEWTPLV RAWTSLIHKP GSGLRFPAPL
SGLPGGVGQW ATSSGARRCW VLAGPRAAHP LFARLQGAAA TGVRDLGNDS QRRPAATGRS
EVWKLLGLVR PERGRLSAAV GFLAVSSVIT MSAPFFLGRI IDVIYTNPSE GYGDSLTRLC
AVLTCVFLCG AAANGIRVYL MQSSGQSIVN RLRTSLFSSI LRQEVAFFDK TRTGELINRL
SSDTALLGRS VTENLSDGLR AGAQASVGVG MMFFVSPSLA TFVLSVVPPI SVLAVIYGRY
LRKLSKATQD SLAEATQLAE ERIGNIRTIR AFGKEMTEVE KYTGRVDQLL QLAQKEALAR
AGFFGAAGLS GNLIVLSVLY KGGLLMGSAH MTVGELSSFL MYAFWVGLSI GGLSSFYSEL
MKGLGAGGRL WELLERQPRL PFNEGMVLDE KTFQGALEFR NVHFTYPARP EVSVFQDFSL
SIPSGSVTAL VGPSGSGKST VVSLLLRLYD PNSGTVSLDG HDIRQLNPVW LRSKIGTVSQ
EPVLFSCSVA ENIAYGADNL SSVTAQQVER AAEVANAAEF IRSFPQGFDT VVGEKGILLS
GGQKQRIAIA RALLKNPKIL LLDEATSALD AENEHLVQEA LDRLMEGRTV LIIAHRLSTI
KNANFVAVLD HGKICEHGTH EELLLKPNGL YRKLMNKQSF LSYNGAEQFL EPARA
