BPT1_YEAST
ID BPT1_YEAST Reviewed; 1559 AA.
AC P14772; D6VXY7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Bile pigment transporter 1;
GN Name=BPT1; OrderedLocusNames=YLL015W; ORFNames=L1313;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046100;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT known genes, a new member of the seripauperins family and a new ABC
RT transporter homologous to the human multidrug resistance protein.";
RL Yeast 13:183-188(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245.
RX PubMed=2545538; DOI=10.1016/0378-1119(89)90355-7;
RA Boy-Marcotte E., Damak F., Camonis J., Garreau H., Jacquet M.;
RT "The C-terminal part of a gene partially homologous to CDC 25 gene
RT suppresses the cdc25-5 mutation in Saccharomyces cerevisiae.";
RL Gene 77:21-30(1989).
RN [6]
RP FUNCTION.
RX PubMed=10790694;
RX DOI=10.1002/(sici)1097-0061(200004)16:6<561::aid-yea551>3.0.co;2-l;
RA Petrovic S., Pascolo L., Gallo R., Cupelli F., Ostrow J.D., Goffeau A.,
RA Tiribelli C., Bruschi C.V.;
RT "The products of YCF1 and YLL015w (BPT1) cooperate for the ATP-dependent
RT vacuolar transport of unconjugated bilirubin in Saccharomyces cerevisiae.";
RL Yeast 16:561-571(2000).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12044871; DOI=10.1016/s0014-5793(02)02767-9;
RA Klein M., Mamnun Y.M., Eggmann T., Schueller C., Wolfger H., Martinoia E.,
RA Kuchler K.;
RT "The ATP-binding cassette (ABC) transporter Bpt1p mediates vacuolar
RT sequestration of glutathione conjugates in yeast.";
RL FEBS Lett. 520:63-67(2002).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927; SER-931 AND THR-934, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND THR-916, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-885; THR-889;
RP SER-893; SER-895 AND THR-916, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Cooperates for the ATP-dependent vacuolar transport of
CC bilirubin and glutathione conjugates. {ECO:0000269|PubMed:10790694,
CC ECO:0000269|PubMed:12044871}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12044871};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:12044871}.
CC -!- DEVELOPMENTAL STAGE: Levels increase in early stationary phase.
CC {ECO:0000269|PubMed:12044871}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; X97560; CAA66162.1; -; Genomic_DNA.
DR EMBL; Z73120; CAA97460.1; -; Genomic_DNA.
DR EMBL; X91488; CAA62776.1; -; Genomic_DNA.
DR EMBL; M26647; AAA16564.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09303.1; -; Genomic_DNA.
DR PIR; S64757; S64757.
DR RefSeq; NP_013086.1; NM_001181835.1.
DR AlphaFoldDB; P14772; -.
DR SMR; P14772; -.
DR BioGRID; 31236; 120.
DR DIP; DIP-2866N; -.
DR IntAct; P14772; 9.
DR MINT; P14772; -.
DR STRING; 4932.YLL015W; -.
DR TCDB; 3.A.1.208.18; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P14772; -.
DR MaxQB; P14772; -.
DR PaxDb; P14772; -.
DR PRIDE; P14772; -.
DR EnsemblFungi; YLL015W_mRNA; YLL015W; YLL015W.
DR GeneID; 850645; -.
DR KEGG; sce:YLL015W; -.
DR SGD; S000003938; BPT1.
DR VEuPathDB; FungiDB:YLL015W; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000157145; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; P14772; -.
DR OMA; MDLMTFL; -.
DR BioCyc; YEAST:G3O-32120-MON; -.
DR Reactome; R-SCE-189483; Heme degradation.
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-9749641; Aspirin ADME.
DR Reactome; R-SCE-9753281; Paracetamol ADME.
DR Reactome; R-SCE-9754706; Atorvastatin ADME.
DR PRO; PR:P14772; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P14772; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
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:0015127; F:bilirubin transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015723; P:bilirubin transport; IMP:SGD.
DR GO; GO:0015691; P:cadmium ion transport; IDA:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 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; 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; Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..1559
FT /note="Bile pigment transporter 1"
FT /id="PRO_0000093448"
FT TOPO_DOM 1..29
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 51..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 106..110
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 128..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 161..178
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 200..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 305..333
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 355..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 432..434
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 456..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 540..560
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 582..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 994..1030
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1031..1052
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1053..1095
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1096..1116
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1117
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1118..1138
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1139..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1210..1230
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1231..1235
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1236..1256
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1257..1559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 292..578
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 639..871
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 980..1265
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1302..1553
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 877..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 672..679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1336..1343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 889
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 916
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 934
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1559 AA; 176874 MW; 0460F3561E3125D5 CRC64;
MSSLEVVDGC PYGYRPYPDS GTNALNPCFI SVISAWQAVF FLLIGSYQLW KLYKNNKVPP
RFKNFPTLPS KINSRHLTHL TNVCFQSTLI ICELALVSQS SDRVYPFILK KALYLNLLFN
LGISLPTQYL AYFKSTFSMG NQLFYYMFQI LLQLFLILQR YYHGSSNERL TVISGQTAMI
LEVLLLFNSV AIFIYDLCIF EPINELSEYY KKNGWYPPVH VLSYITFIWM NKLIVETYRN
KKIKDPNQLP LPPVDLNIKS ISKEFKANWE LEKWLNRNSL WRAIWKSFGR TISVAMLYET
TSDLLSVVQP QFLRIFIDGL NPETSSKYPP LNGVFIALTL FVISVVSVFL TNQFYIGIFE
AGLGIRGSLA SLVYQKSLRL TLAERNEKST GDILNLMSVD VLRIQRFFEN AQTIIGAPIQ
IIVVLTSLYW LLGKAVIGGL VTMAIMMPIN AFLSRKVKKL SKTQMKYKDM RIKTITELLN
AIKSIKLYAW EEPMMARLNH VRNDMELKNF RKIGIVSNLI YFAWNCVPLM VTCSTFGLFS
LFSDSPLSPA IVFPSLSLFN ILNSAIYSVP SMINTIIETS VSMERLKSFL LSDEIDDSFI
ERIDPSADER ALPAIEMNNI TFLWKSKEVL TSSQSGDNLR TDEESIIGSS QIALKNIDHF
EAKRGDLVCV VGRVGAGKST FLKAILGQLP CMSGSRDSIP PKLIIRSSSV AYCSQESWIM
NASVRENILF GHKFDQDYYD LTIKACQLLP DLKILPDGDE TLVGEKGISL SGGQKARLSL
ARAVYSRADI YLLDDILSAV DAEVSKNIIE YVLIGKTALL KNKTIILTTN TVSILKHSQM
IYALENGEIV EQGNYEDVMN RKNNTSKLKK LLEEFDSPID NGNESDVQTE HRSESEVDEP
LQLKVTESET EDEVVTESEL ELIKANSRRA SLATLRPRPF VGAQLDSVKK TAQKAEKTEV
GRVKTKIYLA YIKACGVLGV VLFFLFMILT RVFDLAENFW LKYWSESNEK NGSNERVWMF
VGVYSLIGVA SAAFNNLRSI MMLLYCSIRG SKKLHESMAK SVIRSPMTFF ETTPVGRIIN
RFSSDMDAVD SNLQYIFSFF FKSILTYLVT VILVGYNMPW FLVFNMFLVV IYIYYQTFYI
VLSRELKRLI SISYSPIMSL MSESLNGYSI IDAYDHFERF IYLNYEKIQY NVDFVFNFRS
TNRWLSVRLQ TIGATIVLAT AILALATMNT KRQLSSGMVG LLMSYSLEVT GSLTWIVRTT
VTIETNIVSV ERIVEYCELP PEAQSINPEK RPDENWPSKG GIEFKNYSTK YRENLDPVLN
NINVKIEPCE KVGIVGRTGA GKSTLSLALF RILEPTEGKI IIDGIDISDI GLFDLRSHLA
IIPQDAQAFE GTVKTNLDPF NRYSEDELKR AVEQAHLKPH LEKMLHSKPR GDDSNEEDGN
VNDILDVKIN ENGSNLSVGQ RQLLCLARAL LNRSKILVLD EATASVDMET DKIIQDTIRR
EFKDRTILTI AHRIDTVLDS DKIIVLDQGS VREFDSPSKL LSDKTSIFYS LCEKGGYLK
