AB1B_ARATH
ID AB1B_ARATH Reviewed; 1286 AA.
AC Q9ZR72; Q8L6X6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ABC transporter B family member 1;
DE Short=ABC transporter ABCB.1;
DE Short=AtABCB1;
DE AltName: Full=Multidrug resistance protein 1;
DE AltName: Full=P-glycoprotein 1;
DE Short=AtPgp1;
GN Name=ABCB1; Synonyms=MDR1, PGP1; OrderedLocusNames=At2g36910;
GN ORFNames=T1J8.9;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=1372894; DOI=10.1016/s0021-9258(18)42636-1;
RA Dudler R., Hertig C.;
RT "Structure of an mdr-like gene from Arabidopsis thaliana: evolutionary
RT implications.";
RL J. Biol. Chem. 267:5882-5888(1992).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP PROTEIN SEQUENCE OF 238-249, FUNCTION, AND INTERACTION WITH NPA.
RX PubMed=11701880; DOI=10.2307/3871586;
RA Noh B., Murphy A.S., Spalding E.P.;
RT "Multidrug resistance-like genes of Arabidopsis required for auxin
RT transport and auxin-mediated development.";
RL Plant Cell 13:2441-2454(2001).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9761790; DOI=10.2307/3870761;
RA Sidler M., Hassa P., Hasan S., Ringli C., Dudler R.;
RT "Involvement of an ABC transporter in a developmental pathway regulating
RT hypocotyl cell elongation in the light.";
RL Plant Cell 10:1623-1636(1998).
RN [7]
RP FUNCTION.
RX PubMed=10760241; DOI=10.2307/3871066;
RA Thomas C., Rajagopal A., Windsor B., Dudler R., Lloyd A., Roux S.J.;
RT "A role for ectophosphatase in xenobiotic resistance.";
RL Plant Cell 12:519-533(2000).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FKBP42.
RX PubMed=14517332; DOI=10.1091/mbc.e02-10-0698;
RA Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J., Saal B.,
RA Frangne N., Koncz-Kalman Z., Koncz C., Dudler R., Blakeslee J.J.,
RA Murphy A.S., Martinoia E., Schulz B.;
RT "TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like
RT protein, interacts with Arabidopsis multidrug resistance-like transporters
RT AtPGP1 and AtPGP19.";
RL Mol. Biol. Cell 14:4238-4249(2003).
RN [10]
RP FUNCTION.
RX PubMed=12640467; DOI=10.1038/nbt809;
RA Windsor B., Roux S.J., Lloyd A.;
RT "Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in
RT Arabidopsis thaliana.";
RL Nat. Biotechnol. 21:428-433(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [12]
RP FUNCTION.
RX PubMed=15908594; DOI=10.1104/pp.105.061572;
RA Lin R., Wang H.;
RT "Two homologous ATP-binding cassette transporter proteins, AtMDR1 and
RT AtPGP1, regulate Arabidopsis photomorphogenesis and root development by
RT mediating polar auxin transport.";
RL Plant Physiol. 138:949-964(2005).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16212599; DOI=10.1111/j.1365-313x.2005.02519.x;
RA Geisler M., Blakeslee J.J., Bouchard R., Lee O.R., Vincenzetti V.,
RA Bandyopadhyay A., Titapiwatanakun B., Peer W.A., Bailly A., Richards E.L.,
RA Ejendal K.F.K., Smith A.P., Baroux C., Grossniklaus U., Mueller A.,
RA Hrycyna C.A., Dudler R., Murphy A.S., Martinoia E.;
RT "Cellular efflux of auxin catalyzed by the Arabidopsis MDR/PGP transporter
RT AtPGP1.";
RL Plant J. 44:179-194(2005).
RN [14]
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).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Auxin efflux transporter that acts as a negative regulator of
CC light signaling to promote hypocotyl elongation. Mediates the
CC accumulation of chlorophyll and anthocyanin, as well as the expression
CC of genes in response to light. Participates directly in auxin efflux
CC and thus regulates the polar (presumably basipetal) auxin transport
CC (from root tips to root elongating zone). Transports also some auxin
CC metabolites such as oxindoleacetic acid and indoleacetaldehyde.
CC Involved in diverse auxin-mediated responses including gravitropism,
CC phototropism and lateral root formation. Confers resistance to
CC herbicides such as dicamba, pendimethalin, oryzalin, and monosodium
CC acid methanearsonate (MSMA), but not to herbicides such as glyphosate,
CC atrazine, bentazon and fluazifop-p-butyl. Mediates also resistance to
CC xenobiotics such as cycloheximide and the cytokinin N6-(2-
CC isopentenyl)adenine (2IP). {ECO:0000269|PubMed:10760241,
CC ECO:0000269|PubMed:11701880, ECO:0000269|PubMed:12640467,
CC ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15908594,
CC ECO:0000269|PubMed:16212599, ECO:0000269|PubMed:9761790}.
CC -!- ACTIVITY REGULATION: Transport activity inhibited by 1-N-
CC naphthylphthalamic acid (NPA), cyclopropyl propane dione (CPD),
CC cyclosporin A, verapamil and quercetin.
CC -!- SUBUNIT: Interacts with 1-naphthylphthalamic acid (NPA) and
CC FKBP42/TWD1. {ECO:0000269|PubMed:11701880,
CC ECO:0000269|PubMed:14517332}.
CC -!- INTERACTION:
CC Q9ZR72; Q9LDC0: FKBP42; NbExp=2; IntAct=EBI-366396, EBI-360006;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14517332,
CC ECO:0000269|PubMed:16212599, ECO:0000269|PubMed:9761790}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:16212599,
CC ECO:0000269|PubMed:9761790}. Note=Non-polar distribution in apical
CC cells. Predominant basal (top) localization in root tissues above the
CC elongation zone, especially in mature cortical and endodermal cells.
CC Basal and apical localization in the root elongation zone.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with high levels in peduncles. Mostly
CC localized in young developing tissues, including meristems, as well as
CC root and shoot apices. {ECO:0000269|PubMed:1372894,
CC ECO:0000269|PubMed:16212599, ECO:0000269|PubMed:9761790}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:16212599}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; X61370; CAA43646.1; -; Genomic_DNA.
DR EMBL; AC006922; AAD31576.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09320.1; -; Genomic_DNA.
DR EMBL; AY140105; AAM98246.1; -; mRNA.
DR PIR; A42150; A42150.
DR RefSeq; NP_181228.1; NM_129247.3.
DR AlphaFoldDB; Q9ZR72; -.
DR SMR; Q9ZR72; -.
DR BioGRID; 3609; 11.
DR IntAct; Q9ZR72; 8.
DR STRING; 3702.AT2G36910.1; -.
DR TCDB; 3.A.1.201.5; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9ZR72; -.
DR PaxDb; Q9ZR72; -.
DR PRIDE; Q9ZR72; -.
DR ProteomicsDB; 244510; -.
DR EnsemblPlants; AT2G36910.1; AT2G36910.1; AT2G36910.
DR GeneID; 818265; -.
DR Gramene; AT2G36910.1; AT2G36910.1; AT2G36910.
DR KEGG; ath:AT2G36910; -.
DR Araport; AT2G36910; -.
DR TAIR; locus:2057961; AT2G36910.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9ZR72; -.
DR OMA; YIYLNYG; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9ZR72; -.
DR BioCyc; ARA:AT2G36910-MON; -.
DR PRO; PR:Q9ZR72; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZR72; baseline and differential.
DR Genevisible; Q9ZR72; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010328; F:auxin influx transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0043481; P:anthocyanin accumulation in tissues in response to UV light; IMP:TAIR.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IDA:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IGI:TAIR.
DR GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009637; P:response to blue light; IMP:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
DR GO; GO:0048443; P:stamen development; IGI:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 3.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 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; Auxin signaling pathway; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1286
FT /note="ABC transporter B family member 1"
FT /id="PRO_0000227912"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 821..843
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 845..867
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 44..333
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 368..604
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 700..988
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1024..1260
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 614..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1286
FT /note="Interaction with FKBP42/TWD1"
FT /evidence="ECO:0000269|PubMed:14517332"
FT BINDING 403..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1059..1066
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 293
FT /note="G -> D (in Ref. 4; AAM98246)"
FT /evidence="ECO:0000305"
FT CONFLICT 1188
FT /note="E -> G (in Ref. 4; AAM98246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1286 AA; 140573 MW; A6C90AF42CC1FF01 CRC64;
MDNDGGAPPP PPTLVVEEPK KAEIRGVAFK ELFRFADGLD YVLMGIGSVG AFVHGCSLPL
FLRFFADLVN SFGSNSNNVE KMMEEVLKYA LYFLVVGAAI WASSWAEISC WMWSGERQTT
KMRIKYLEAA LNQDIQFFDT EVRTSDVVFA INTDAVMVQD AISEKLGNFI HYMATFVSGF
IVGFTAVWQL ALVTLAVVPL IAVIGGIHTT TLSKLSNKSQ ESLSQAGNIV EQTVVQIRVV
MAFVGESRAS QAYSSALKIA QKLGYKTGLA KGMGLGATYF VVFCCYALLL WYGGYLVRHH
LTNGGLAIAT MFAVMIGGLA LGQSAPSMAA FAKAKVAAAK IFRIIDHKPT IERNSESGVE
LDSVTGLVEL KNVDFSYPSR PDVKILNNFC LSVPAGKTIA LVGSSGSGKS TVVSLIERFY
DPNSGQVLLD GQDLKTLKLR WLRQQIGLVS QEPALFATSI KENILLGRPD ADQVEIEEAA
RVANAHSFII KLPDGFDTQV GERGLQLSGG QKQRIAIARA MLKNPAILLL DEATSALDSE
SEKLVQEALD RFMIGRTTLI IAHRLSTIRK ADLVAVLQQG SVSEIGTHDE LFSKGENGVY
AKLIKMQEAA HETAMSNARK SSARPSSARN SVSSPIMTRN SSYGRSPYSR RLSDFSTSDF
SLSIDASSYP NYRNEKLAFK DQANSFWRLA KMNSPEWKYA LLGSVGSVIC GSLSAFFAYV
LSAVLSVYYN PDHEYMIKQI DKYCYLLIGL SSAALVFNTL QHSFWDIVGE NLTKRVREKM
LSAVLKNEMA WFDQEENESA RIAARLALDA NNVRSAIGDR ISVIVQNTAL MLVACTAGFV
LQWRLALVLV AVFPVVVAAT VLQKMFMTGF SGDLEAAHAK GTQLAGEAIA NVRTVAAFNS
EAKIVRLYTA NLEPPLKRCF WKGQIAGSGY GVAQFCLYAS YALGLWYASW LVKHGISDFS
KTIRVFMVLM VSANGAAETL TLAPDFIKGG QAMRSVFELL DRKTEIEPDD PDTTPVPDRL
RGEVELKHID FSYPSRPDIQ IFRDLSLRAR AGKTLALVGP SGCGKSSVIS LIQRFYEPSS
GRVMIDGKDI RKYNLKAIRK HIAIVPQEPC LFGTTIYENI AYGHECATEA EIIQAATLAS
AHKFISALPE GYKTYVGERG VQLSGGQKQR IAIARALVRK AEIMLLDEAT SALDAESERS
VQEALDQACS GRTSIVVAHR LSTIRNAHVI AVIDDGKVAE QGSHSHLLKN HPDGIYARMI
QLQRFTHTQV IGMTSGSSSR VKEDDA
