ABCBB_RABIT
ID ABCBB_RABIT Reviewed; 1321 AA.
AC Q9N0V3;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Bile salt export pump {ECO:0000303|Ref.1};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O95342};
DE AltName: Full=ATP-binding cassette sub-family B member 11;
DE AltName: Full=Sister of P-glycoprotein;
GN Name=ABCB11 {ECO:0000250|UniProtKB:O95342};
GN Synonyms=BSEP {ECO:0000303|Ref.1}, SPGP {ECO:0000303|Ref.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RA Balasubramanian N.V., Suchy F.J., Ananthanarayanan M.;
RT "Molecular cloning and characterization of rabbit liver bile salt export
RT pump (Bsep/spgp).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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. Transports taurine-
CC conjugated bile salts more rapidly than glycine-conjugated bile salts.
CC Also transports non-bile acid compounds, such as pravastatin and
CC fexofenadine in an ATP-dependent manner and may be involved in their
CC biliary excretion. {ECO:0000250|UniProtKB:O95342}.
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:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000250|UniProtKB:O95342};
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. Cyclosporin
CC A, glibenclamide, rifampicin and troglitazonestrongly competitively
CC inhibit the transport activity of taurocholate. The canalicular
CC transport activity of taurocholate is strongly dependent on canalicular
CC membrane cholesterol content. The uptake of taurocholate is increased
CC by short- and medium-chain fatty acids. Cholesterol increases transport
CC capacity of taurocholate without affecting the affinity for the
CC substrate. {ECO:0000250|UniProtKB:O95342}.
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: Expressed predominantly, if not exclusively in the
CC liver, where it was further localized to the canalicular microvilli and
CC to subcanalicular vesicles of the hepatocytes by in situ.
CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
CC containing a hydrophobic membrane-anchoring domain and an ATP binding
CC cassette (ABC) domain.
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; AF249879; AAF65552.1; -; mRNA.
DR RefSeq; NP_001075552.1; NM_001082083.1.
DR AlphaFoldDB; Q9N0V3; -.
DR SMR; Q9N0V3; -.
DR STRING; 9986.ENSOCUP00000001184; -.
DR PRIDE; Q9N0V3; -.
DR GeneID; 100008767; -.
DR KEGG; ocu:100008767; -.
DR CTD; 8647; -.
DR eggNOG; KOG0055; Eukaryota.
DR InParanoid; Q9N0V3; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0015432; F:ABC-type bile acid transporter activity; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0055091; P:phospholipid homeostasis; ISS:UniProtKB.
DR GO; GO:0120189; P:positive regulation of bile acid secretion; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:1904251; P:regulation of bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Endosome; Glycoprotein; Lipid transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1321
FT /note="Bile salt export pump"
FT /id="PRO_0000093298"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 84..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 169..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 237..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 262..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 341..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 375..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 777..794
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 816..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 912..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1001..1011
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1033..1321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 755..1043
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1078..1316
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 651..672
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000250"
FT REGION 659..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1113..1120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 586
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY30"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70127"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70127"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1321 AA; 146377 MW; 457539FCD6D717A2 CRC64;
MSDSVILRSV KKFGEENHGF ESDGSYNNEK KSRLQDKKKS DSVRIGFFQL FRFSSWTDIW
LMCMGSLCAC IHGIAQPGVL LIFGTMTDVF IDYDTELQEL KIPGKACVNN TIVWINSSLN
QNVTNGTRCG LLDIESEMIR FAGYYAGIGI AVLTTGYIQI CFWGIAAAHQ IQKMRKSYFR
KIMRMGIGWV DCNSVGKLNT PFSVDFNKIN DSSADQLAIF IQGMTSPIFG FLVGFSQWWK
LTLVIISVSP LIGLGAAIIG LSVSKFTDYE LKAYAKAGSV ADEVISSMRT VAAFGGEKKE
VERYEKNLVF AQRWGIRKGI VMGFFTGYMW CLIFFCYALA FWYGSKLVLE EGEYSPGALV
QIFLSVIIGA LNLGNASPCL EAFAAGRAAA SSIFETIDRK PIIDCMSEDG YKLERIKGEI
EFHNVTFHYP SRPEVKILNN LSMVIKPGEM TALVGPSGAG KSTALQLIHR FYGPTEGMVT
VESHDIRSSH IQWLRNQIGI VEQEPVLFFH TIAEKIRYGR EDATMEDLIQ AAKEANAYNF
IMDLPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEAMVQEA
LSKTQHGHTI VSVAHRPATI RTADVIIGCE HGAAVERGTE EELLERKGVY FALVTLQSQR
NQGDQEENEK DATEDDIPEK TFSRGNYQDS LRASLRQRSK SQLSYLAHEP PMAVEDHKST
HEEDRKDKDL PAQEDIEPAS VRRIMKLNAP EWPYMLLGSM GAAVNGAVTP LYAFLFSQIL
GTFSLPDKEE QRSQINGICL LFVTLGCVSF FTQFLQGYTF AKSGELLTKR LRKFGFRAML
GQDIGWFDDL RNSPGALTTR LATDASQVQG ATGSQIGMMV NSFTNVTVAM IIAFLFSWKL
TLGIVCFFPF LALSGALQTK MLTGFASRDK QALEKAGQIT SEALSNIRTV AGIGKERKFI
ETFEAELEKP YKMAIKKANV YGLCFGFSQC ITFIANSASY RYGGYLISNE GLHFSYVFRV
ISAVVLSATA LGRASSYTPS YAKAKISAAR FFQLLDRQPP INVYSSAGEK WDNFQGKIDF
VDCKFTYPSR PDIQVLNGLS VSMSPRQTLA FVGSSGCGKS TSIQLLERFY DPDHGKVMID
GHDSRKVNIQ FLRSNIGIVS QEPVLFACSI KDNIKYGDNT QEIPMERIIA AAKKAQVHDF
VMSLPEKYET NVGSQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQVA
LDKAREGRTC IVIAHRLSTI QNSDIIAVMS QGMVIEKGTH EELMVQKGAY YKLVTTGSPI
S
