ABCBB_CANLF
ID ABCBB_CANLF Reviewed; 1325 AA.
AC B8K1W2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Bile salt export pump {ECO:0000303|PubMed:18985798};
DE EC=7.6.2.- {ECO:0000269|PubMed:18985798};
GN Name=Abcb11e {ECO:0000250|UniProtKB:O95342};
GN Synonyms=BSEP {ECO:0000303|PubMed:18985798};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=18985798; DOI=10.1002/bdd.629;
RA Yabuuchi H., Tanaka K., Maeda M., Takemura M., Oka M., Ohashi R., Tamai I.;
RT "Cloning of the dog bile salt export pump (BSEP; ABCB11) and functional
RT comparison with the human and rat proteins.";
RL Biopharm. Drug Dispos. 29:441-448(2008).
CC -!- FUNCTION: Catalyzes the transport of the major hydrophobic bile salts,
CC such as taurine and glycine-conjugated cholic acid across the
CC canalicular membrane of hepatocytes in an ATP-dependent manner,
CC therefore participates in hepatic bile acid homeostasis and
CC consequently to lipid homeostasis through regulation of biliary lipid
CC secretion in a bile salts dependent manner (PubMed:18985798).
CC Transports taurine-conjugated bile salts more rapidly than glycine-
CC conjugated bile salts. Also transports non-bile acid compounds, such as
CC pravastatin and fexofenadine in an ATP-dependent manner and may be
CC involved in their biliary excretion (By similarity).
CC {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:18985798}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate(in) + H2O = ADP + cholate(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:50048, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50049;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:18985798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000305|PubMed:18985798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycochenodeoxycholate(in) + H2O = ADP +
CC glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50060,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50061;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurochenodeoxycholate(in) = ADP + H(+) +
CC phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:50064,
CC ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50065;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycoursodeoxycholate(in) + H2O = ADP +
CC glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50069;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + tauroursodeoxycholate(in) = ADP + H(+) + phosphate
CC + tauroursodeoxycholate(out); Xref=Rhea:RHEA:50072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50073;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurodeoxycholate(in) = ADP + H(+) + phosphate +
CC taurodeoxycholate(out); Xref=Rhea:RHEA:50080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36261,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50081;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) +
CC phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50085;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pravastatin(in) = ADP + H(+) + phosphate +
CC pravastatin(out); Xref=Rhea:RHEA:63908, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:63660, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63909;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- ACTIVITY REGULATION: The uptake of taurocholate is inhibited by
CC taurolithocholate sulfate with an IC(50) of 9 uM. Pravastatin
CC competitively inhibits the transport of taurocholic acid
CC (PubMed:18985798). Cyclosporin A, glibenclamide, rifampicin and
CC troglitazonestrongly competitively inhibit the transport activity of
CC taurocholate (PubMed:18985798). The canalicular transport activity of
CC taurocholate is strongly dependent on canalicular membrane cholesterol
CC content. The uptake of taurocholate is increased by short- and medium-
CC chain fatty acids. Cholesterol increases transport capacity of
CC taurocholate without affecting the affinity for the substrate (By
CC similarity). {ECO:0000250|UniProtKB:O95342,
CC ECO:0000269|PubMed:18985798}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.7 uM for taurocholate {ECO:0000269|PubMed:18985798};
CC Vmax=219 pmol/min/mg enzyme for taurocholate transport
CC {ECO:0000269|PubMed:18985798};
CC -!- SUBUNIT: Interacts with HAX1 (By similarity). Interacts with the
CC adapter protein complex 2 (AP-2) throught AP2A2 or AP2A1; this
CC interaction regulates cell membrane expression of ABCB11 through its
CC internalization in a clathrin-dependent manner and its subsequent
CC degradation (By similarity). {ECO:0000250|UniProtKB:O70127,
CC ECO:0000250|UniProtKB:O95342}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O70127}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O70127}. Endosome
CC {ECO:0000250|UniProtKB:O70127}. Cell membrane
CC {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O70127}. Note=Internalized at the canalicular
CC membrane through interaction with the adapter protein complex 2 (AP-2).
CC At steady state, localizes in the canalicular membrane but is also
CC present in recycling endosomes. ABCB11 constantly and rapidly exchanges
CC between the two sites through tubulo-vesicles carriers that move along
CC microtubules. Microtubule-dependent trafficking of ABCB11 is enhanced
CC by taurocholate and cAMP and regulated by STK11 through a PKA-mediated
CC pathway. Trafficking of newly synthesized ABCB11 through endosomal
CC compartment to the bile canalicular membrane is accelerated by cAMP but
CC not by taurocholate (By similarity). Cell membrane expression is up-
CC regulated by short- and medium-chain fatty acids (By similarity).
CC {ECO:0000250|UniProtKB:O70127, ECO:0000250|UniProtKB:O95342}.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:18985798}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.
CC -!- PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface
CC expression of ABCB11. {ECO:0000250|UniProtKB:O95342}.
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; DQ157431; ABA39075.1; -; mRNA.
DR RefSeq; NP_001137404.1; NM_001143932.1.
DR AlphaFoldDB; B8K1W2; -.
DR SMR; B8K1W2; -.
DR Ensembl; ENSCAFT00030042019; ENSCAFP00030036654; ENSCAFG00030022858.
DR Ensembl; ENSCAFT00845036706; ENSCAFP00845028736; ENSCAFG00845020713.
DR GeneID; 488390; -.
DR KEGG; cfa:488390; -.
DR CTD; 8647; -.
DR VEuPathDB; HostDB:ENSCAFG00845020713; -.
DR GeneTree; ENSGT00940000157564; -.
DR OrthoDB; 186078at2759; -.
DR Proteomes; UP000002254; Chromosome 36.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
DR GO; GO:0046691; C:intracellular canaliculus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015432; F:ABC-type bile acid transporter activity; IDA:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015126; F:canalicular bile acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015721; P:bile acid and bile salt transport; IDA:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:0120189; P:positive regulation of bile acid secretion; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:1904251; P:regulation of bile acid metabolic process; IEA:Ensembl.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0046618; P:xenobiotic export from cell; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
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; IPR030278; BSEP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF165; PTHR24221:SF165; 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endosome; Glycoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1325
FT /note="Bile salt export pump"
FT /id="PRO_0000451041"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 84..147
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 169..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 262..319
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 341..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 375..759
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 781..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 820..894
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 916..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 1005..1014
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1015..1035
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 1036..1325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 62..385
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 420..656
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 759..1047
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1082..1320
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1117..1124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1325 AA; 146456 MW; 2AF77DC15062A782 CRC64;
MSDAVILRSV KKFGEDNYGF ESSTFYNNDK NSGLQDERKG DSSQVGFFQL FRFSSTTDIW
LMFVGSLCAF LHGLSHPGVL LIFGTMTDVF IAYDTELQEL KIPGKACVNN TIVWINSSLN
QNVTNGTQCG LLDIESEMIK FASYYAGIAL LVLITGYIQI CFWVIAAARQ IQKMRKISFR
KVMRMEIGWF DCNSVGELNT RFSDDINRVN DAIADQMPIF IQRMTTSICG FLLGFYQGWK
LTLVIISVSP LIGIGAAIIG LSVSKFTDYE LKAYAKAGSV ADEVISSMRT VAAFGGEKKE
VERYEKNLVF AQRWGIRKGI VMGFFTGFMW CLIFLCYALA FWYGSKLVLE DGEYTAGTLV
QIFLSILLGA LNLGNASSCL EAFATGRAAA TSIFHTIDRK PIIDCMSEDG YKLDRIKGEI
EFHNVTFHYP SRPEVKILNN LSMVIKSGEM TAVVGSSGSG KSTALQLIQR FYDPSEGMVT
LDGHDIRSLN IQWLRTQIGI VEQEPVLFST TIAENIRYGR EDATMEDIVR AAKAANAYNF
IMDLPEQFDT LVGEGGGQMS GGQKQRVAIA RALVRNPKIL LLDMATSALD NESEAMVQEA
LSKIQQGHTI ISVAHRLSTV RAADVIIGFE HGTAVERGSH EELLERKGVY FTLVTLQSQG
EPTANAEGIR GEEETDGVSL DNEQTFCRGS YQSSLRASLR QRSKSQLSYL AHEPPLAVVD
HKSTYEEDRK DKDIPVEEEI EPAPVRRILK FNAPEWPYML FGAVGAAVNG SVTPLYAFLF
SQILGTFSLP DKEEQRSQIN GVCLLFVAVG CVSLCTQFLQ GYAFAKSGEL LTKRLRKYGF
RAMLGQDIGW FDDLRNSPGA LTTRLATDAS QVQGAAGSQI GMMVNSFTNV TVAMIIAFFF
SWKLSLVIMC FFPFLALSGA LQTRMLTGFA TQDKEALEIA GQITNEALSN IRTVAGIGKE
RQFIEAFEAE LEKPFKTAFR KANVYGFCFG FSQCIVFVAN SASYRYGGYL IPNEGLHFSY
VFRVISSVVL SATALGRASS YTPSYAKAKI SAARFFQLLD RQPPIKVYSS AGEKWDNFQG
QVDFVDCKFT YPSRPDTQVL NGLSVSVRPG QTLAFVGSSG CGKSTSIQLL ERFYDPDQGK
VMIDGHDSRK VNVQFLRSNI GIVSQEPVLF ACSIMDNIKY GDNTREIPME KVIEAAKQAQ
LHDFVMSLPE KYETNVGSQG SQLSRGEKQR IAIARAIVRN PKILLLDEAT SALDTESEKT
VQVALDKARE GRTCIVIAHR LSTIQNSDII AVMSQGIVIE KGTHEELMAQ KGAYYKLVTT
GAPIS
