ABCB7_MOUSE
ID ABCB7_MOUSE Reviewed; 752 AA.
AC Q61102; A2AC46; Q3U7S8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial;
DE AltName: Full=ATP-binding cassette transporter 7;
DE Short=ABC transporter 7 protein;
DE Flags: Precursor;
GN Name=Abcb7 {ECO:0000312|MGI:MGI:109533}; Synonyms=Abc7;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [MRNA] OF 59-752.
RC STRAIN=DBA/2J;
RX PubMed=9143506; DOI=10.1006/geno.1997.4658;
RA Savary S., Allikmets R., Denizot F., Luciani M.-F., Mattei M.-G., Dean M.,
RA Chimini G.;
RT "Isolation and chromosomal mapping of a novel ATP-binding cassette
RT transporter conserved in mouse and human.";
RL Genomics 41:275-278(1997).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16424901; DOI=10.1038/sj.emboj.7600954;
RA Clarke S.L., Vasanthakumar A., Anderson S.A., Pondarre C., Koh C.M.,
RA Deck K.M., Pitula J.S., Epstein C.J., Fleming M.D., Eisenstein R.S.;
RT "Iron-responsive degradation of iron-regulatory protein 1 does not require
RT the Fe-S cluster.";
RL EMBO J. 25:544-553(2006).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16467350; DOI=10.1093/hmg/ddl012;
RA Pondarre C., Antiochos B.B., Campagna D.R., Clarke S.L., Greer E.L.,
RA Deck K.M., McDonald A., Han A.P., Medlock A., Kutok J.L., Anderson S.A.,
RA Eisenstein R.S., Fleming M.D.;
RT "The mitochondrial ATP-binding cassette transporter Abcb7 is essential in
RT mice and participates in cytosolic iron-sulfur cluster biogenesis.";
RL Hum. Mol. Genet. 15:953-964(2006).
RN [7]
RP MUTAGENESIS OF GLU-433, AND FUNCTION.
RX PubMed=17192398; DOI=10.1182/blood-2006-04-015768;
RA Pondarre C., Campagna D.R., Antiochos B., Sikorski L., Mulhern H.,
RA Fleming M.D.;
RT "Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia,
RT is essential for hematopoiesis.";
RL Blood 109:3567-3569(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216; LYS-251 AND LYS-350, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [10]
RP FUNCTION, INTERACTION WITH FECH, AND 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: Exports glutathione-coordinated iron-sulfur clusters such as
CC [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-
CC dependent manner allowing the assembly of the cytosolic iron-sulfur
CC (Fe/S) cluster-containing proteins and participates in iron homeostasis
CC (PubMed:16424901, PubMed:16467350). Moreover, through a functional
CC complex formed of ABCB7, FECH and ABCB10, also plays a role in the
CC cellular iron homeostasis, mitochondrial function and heme biosynthesis
CC (PubMed:30765471). In cardiomyocytes, regulates cellular iron
CC homeostasis and cellular reactive oxygen species (ROS) levels through
CC its interaction with COX4I1 (By similarity). May also play a role in
CC hematopoiesis (PubMed:17192398). {ECO:0000250|UniProtKB:Q704E8,
CC ECO:0000269|PubMed:16424901, ECO:0000269|PubMed:16467350,
CC ECO:0000269|PubMed:17192398, ECO:0000269|PubMed:30765471}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O =
CC (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O75027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029;
CC Evidence={ECO:0000250|UniProtKB:O75027};
CC -!- SUBUNIT: Homodimer or heterodimer. Interacts with C10orf88/PAAT (By
CC similarity). Forms a complex with ABCB10 and FECH, where a dimeric FECH
CC bridges ABCB7 and ABCB10 homodimers; this complex may be required for
CC cellular iron homeostasis, mitochondrial function and heme biosynthesis
CC (PubMed:30765471). Interacts with FECH (PubMed:30765471). Interacts
CC with ATP5F1A. Interacts with COX4I1; this interaction allows the
CC regulation of cellular iron homeostasis and cellular reactive oxygen
CC species (ROS) levels in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:O75027, ECO:0000250|UniProtKB:Q704E8,
CC ECO:0000269|PubMed:30765471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40416}.
CC -!- DISRUPTION PHENOTYPE: Heterozygous females for Abcb7 with a maternally
CC inherited mutant allele die embryonically, due to a defect in the
CC extra-embryonic visceral endoderm, while heterozygous females with a
CC paternally inherited mutant allele are viable (PubMed:16467350). The
CC systemic and tissue-specific deletion of ABCB7 in most organs,
CC including CNS and bone marrow, is lethal (PubMed:16467350).
CC Conditionnal knockout in hepatocyte causes periportal hepatocellular
CC iron deposition with characteristic round structures and leads to iron-
CC dependent regulation of IRP1 protein (PubMed:16467350,
CC PubMed:16424901). {ECO:0000269|PubMed:16424901,
CC ECO:0000269|PubMed:16467350}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK151967; BAE30838.1; -; mRNA.
DR EMBL; AK152535; BAE31291.1; -; mRNA.
DR EMBL; AK152816; BAE31519.1; -; mRNA.
DR EMBL; AL663052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151037; AAI51038.1; -; mRNA.
DR EMBL; U43892; AAC53152.1; -; mRNA.
DR CCDS; CCDS53167.1; -.
DR RefSeq; NP_033722.1; NM_009592.1.
DR AlphaFoldDB; Q61102; -.
DR SMR; Q61102; -.
DR BioGRID; 197903; 7.
DR IntAct; Q61102; 9.
DR MINT; Q61102; -.
DR STRING; 10090.ENSMUSP00000033695; -.
DR iPTMnet; Q61102; -.
DR PhosphoSitePlus; Q61102; -.
DR SwissPalm; Q61102; -.
DR EPD; Q61102; -.
DR jPOST; Q61102; -.
DR MaxQB; Q61102; -.
DR PaxDb; Q61102; -.
DR PeptideAtlas; Q61102; -.
DR PRIDE; Q61102; -.
DR ProteomicsDB; 296469; -.
DR Antibodypedia; 28030; 303 antibodies from 33 providers.
DR Ensembl; ENSMUST00000033695; ENSMUSP00000033695; ENSMUSG00000031333.
DR GeneID; 11306; -.
DR KEGG; mmu:11306; -.
DR UCSC; uc009uaf.2; mouse.
DR CTD; 22; -.
DR MGI; MGI:109533; Abcb7.
DR VEuPathDB; HostDB:ENSMUSG00000031333; -.
DR eggNOG; KOG0057; Eukaryota.
DR GeneTree; ENSGT00940000156281; -.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q61102; -.
DR OMA; VTEWRTH; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; Q61102; -.
DR TreeFam; TF105195; -.
DR Reactome; R-MMU-1369007; Mitochondrial ABC transporters.
DR BioGRID-ORCS; 11306; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Abcb7; mouse.
DR PRO; PR:Q61102; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61102; protein.
DR Bgee; ENSMUSG00000031333; Expressed in digastric muscle group and 248 other tissues.
DR Genevisible; Q61102; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0140481; F:ABC-type iron-sulfur cluster transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0034755; P:iron ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; ISS:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; IMP:UniProtKB.
DR GO; GO:1903331; P:positive regulation of iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 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; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..752
FT /note="Iron-sulfur clusters transporter ABCB7,
FT mitochondrial"
FT /id="PRO_0000093295"
FT TOPO_DOM 23..140
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 162..185
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 207..259
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 281..290
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 312..382
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 404..409
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 431..752
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 140..436
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 472..706
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 38..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 315..319
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 378..381
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 428
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 505..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q704E8"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q704E8"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q704E8"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MUTAGEN 433
FT /note="E->K: Exhibits siderocytosis with increased zinc
FT protoporphyrin."
FT /evidence="ECO:0000269|PubMed:17192398"
FT CONFLICT 702
FT /note="S -> T (in Ref. 1; BAE30838/BAE31291/BAE31519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 82581 MW; 79B2BC8A7A07555A CRC64;
MALLAIHSWR WAAAAVAFEK HKHSAVLTRA LVSMCGSGPR WSSSQRGASG SARLSQTTES
LRNTTQQRWG KDNSRQLLDA TKALQTWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI
IKAMLSYVWP EDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD
APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF
HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIVFEMML VSSVLYYKCG AQFALVTLGT
LGAYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNEK YEAQRYDGFL
KTYETASLKS TSTLAMLNFG QNAIFSVGLT AIMVLASQGI VAGALTVGDL VMVNGLLFQL
SLPLNFLGTV YRETRQALID MNTLFTLLKV DTRIKDKVMA PPLQITPQTA TVAFDNVHFE
YIEGQKVLNG VSFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNLQDVS
LESLRRAVGV VPQDAVLFHN TIYYNLLYGN INASPEEVYA VAKLAGLHDA ILRMPHGYDT
QVGERGLKLS GGEKQRVAIA RAILKNPPVI LYDEATSSLD SITEETILGA MRDVVKHRTS
IFIAHRLSTV VDADEIIVLS QGKVAERGTH YGLLANSSSI YSEMWHTQSN RVQNQDSLGW
DAKKESLSKE EERKKLQEEI VNSVKGCGNC SC
