MDR3_RAT
ID MDR3_RAT Reviewed; 1278 AA.
AC Q08201; Q78E07;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Phosphatidylcholine translocator ABCB4 {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P21440};
DE AltName: Full=ATP-binding cassette sub-family B member 4 {ECO:0000312|RGD:620248};
DE AltName: Full=Multidrug resistance protein 2 {ECO:0000303|PubMed:8103593};
DE AltName: Full=Multidrug resistance protein 3 {ECO:0000250|UniProtKB:P21439};
DE AltName: Full=P-glycoprotein 2 {ECO:0000303|PubMed:10067174};
DE AltName: Full=P-glycoprotein 3 {ECO:0000303|PubMed:7948020};
GN Name=Abcb4 {ECO:0000312|RGD:620248};
GN Synonyms=Mdr2 {ECO:0000303|PubMed:8103593},
GN Pgp3 {ECO:0000303|PubMed:7948020}, Pgy2 {ECO:0000303|PubMed:10067174};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer;
RX PubMed=8103593; DOI=10.1093/nar/21.16.3885;
RA Brown P.C., Thorgeirsson S.S., Silverman J.A.;
RT "Cloning and regulation of the rat mdr2 gene.";
RL Nucleic Acids Res. 21:3885-3891(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1211-1278.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1348630; DOI=10.1016/0167-4781(92)90523-3;
RA Deuchars K.L., Duthie M., Ling V.;
RT "Identification of distinct P-glycoprotein gene sequences in rat.";
RL Biochim. Biophys. Acta 1130:157-165(1992).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=7948020; DOI=10.1016/0167-4781(94)90222-4;
RA Furuya K.N., Gebhardt R., Schuetz E.G., Schuetz J.D.;
RT "Isolation of rat pgp3 cDNA: evidence for gender and zonal regulation of
RT expression in the liver.";
RL Biochim. Biophys. Acta 1219:636-644(1994).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10067174; DOI=10.1538/expanim.47.283;
RA Moralejo D.H., Wei K., Wei S., Ogino T., Yamada T., Sogawa K., Hamakawa H.,
RA Szpirer C., Carbone C., Matsumoto K.;
RT "Mapping of the genes for rat P-glycoprotein 1, 2, and 3 (Pgy1, Pgy2, and
RT Pgy3) to chromosome 4.";
RL Exp. Anim. 47:283-284(1998).
RN [5]
RP INTERACTION WITH HAX1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15159385; DOI=10.1074/jbc.m404337200;
RA Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.;
RT "Identification of HAX-1 as a protein that binds bile salt export protein
RT and regulates its abundance in the apical membrane of Madin-Darby canine
RT kidney cells.";
RL J. Biol. Chem. 279:32761-32770(2004).
CC -!- FUNCTION: Energy-dependent phospholipid efflux translocator that acts
CC as a positive regulator of biliary lipid secretion. Functions as a
CC floppase that translocates specifically phosphatidylcholine (PC) from
CC the inner to the outer leaflet of the canalicular membrane bilayer into
CC the canaliculi of hepatocytes. Translocation of PC makes the biliary
CC phospholipids available for extraction into the canaliculi lumen by
CC bile salt mixed micelles and therefore protects the biliary tree from
CC the detergent activity of bile salts. Plays a role in the recruitment
CC of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and
CC sphingomyelin (SM) molecules to nonraft membranes and to further
CC enrichment of SM and cholesterol in raft membranes in hepatocytes.
CC Required for proper phospholipid bile formation. Indirectly involved in
CC cholesterol efflux activity from hepatocytes into the canalicular lumen
CC in the presence of bile salts in an ATP-dependent manner. May promote
CC biliary phospholipid secretion as canaliculi-containing vesicles from
CC the canalicular plasma membrane. In cooperation with ATP8B1, functions
CC to protect hepatocytes from the deleterious detergent activity of bile
CC salts. Does not confer multidrug resistance.
CC {ECO:0000250|UniProtKB:P21439, ECO:0000250|UniProtKB:P21440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:P21440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P21440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66273;
CC Evidence={ECO:0000250|UniProtKB:P21440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:36439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P21439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36440;
CC Evidence={ECO:0000250|UniProtKB:P21439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P21439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38904;
CC Evidence={ECO:0000250|UniProtKB:P21439};
CC -!- ACTIVITY REGULATION: Translocation activity is inhibited by the ATPase
CC inhibitor vanadate and the calcium channel blocker verapamil.
CC Translocation activity is enhanced by the addition of the bile salt
CC taurocholate. {ECO:0000250|UniProtKB:P21439}.
CC -!- SUBUNIT: Interacts with HAX1 (PubMed:15159385). May interact with RACK1
CC (By similarity). {ECO:0000250|UniProtKB:P21439,
CC ECO:0000269|PubMed:15159385}.
CC -!- INTERACTION:
CC Q08201; Q7TSE9: Hax1; NbExp=3; IntAct=EBI-929988, EBI-930005;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21439};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC Apical cell membrane {ECO:0000250|UniProtKB:P21439}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Membrane raft
CC {ECO:0000250|UniProtKB:P21439}. Cytoplasm
CC {ECO:0000250|UniProtKB:P21439}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:15159385}. Note=Localized at the apical
CC canalicular membrane of the epithelial cells lining the lumen of the
CC bile canaliculi and biliary ductules. Localized preferentially in lipid
CC nonraft domains of canalicular plasma membranes. Transported from the
CC Golgi to the apical bile canalicular membrane in a RACK1-dependent
CC manner. Redistributed into pseudocanaliculi formed between cells in a
CC bezafibrate- or PPARA-dependent manner. {ECO:0000250|UniProtKB:P21439,
CC ECO:0000250|UniProtKB:P21440}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver (PubMed:15159385). Expressed
CC in hepatocytes (PubMed:7948020, PubMed:10067174).
CC {ECO:0000269|PubMed:10067174, ECO:0000269|PubMed:15159385,
CC ECO:0000269|PubMed:7948020}.
CC -!- PTM: Phosphorylated. Phosphorylation is required for PC efflux
CC activity. Phosphorylation occurs on serine and threonine residues in a
CC protein kinase A- or C-dependent manner. May be phosphorylated on Thr-
CC 41 and Ser-46. {ECO:0000250|UniProtKB:P21439}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21439}.
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; L15079; AAA02937.1; -; mRNA.
DR EMBL; X61105; CAA43417.1; -; Genomic_DNA.
DR PIR; S41646; S41646.
DR RefSeq; NP_036822.1; NM_012690.2.
DR AlphaFoldDB; Q08201; -.
DR SMR; Q08201; -.
DR IntAct; Q08201; 1.
DR STRING; 10116.ENSRNOP00000042556; -.
DR ChEMBL; CHEMBL2073706; -.
DR GlyGen; Q08201; 2 sites.
DR PhosphoSitePlus; Q08201; -.
DR PaxDb; Q08201; -.
DR PRIDE; Q08201; -.
DR GeneID; 24891; -.
DR KEGG; rno:24891; -.
DR CTD; 5244; -.
DR RGD; 620248; Abcb4.
DR eggNOG; KOG0055; Eukaryota.
DR InParanoid; Q08201; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q08201; -.
DR BRENDA; 7.6.2.2; 5301.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR PRO; PR:Q08201; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0046581; C:intercellular canaliculus; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:UniProtKB.
DR GO; GO:0099038; F:ceramide floppase activity; IBA:GO_Central.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISS:UniProtKB.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0032782; P:bile acid secretion; ISS:UniProtKB.
DR GO; GO:1903413; P:cellular response to bile acid; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; ISO:RGD.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; ISS:UniProtKB.
DR GO; GO:0061092; P:positive regulation of phospholipid translocation; ISS:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
DR GO; GO:1901557; P:response to fenofibrate; ISS:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR Gene3D; 1.20.1560.10; -; 3.
DR Gene3D; 3.40.50.300; -; 3.
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; IPR030275; MDR3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF241; PTHR24221:SF241; 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; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Glycoprotein;
KW Lipid transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1278
FT /note="Phosphatidylcholine translocator ABCB4"
FT /id="PRO_0000093338"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..70
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 71..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 137..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 208..214
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 236..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 316..329
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 330..351
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 352..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 732..754
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 776..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 852
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 853..872
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 873..932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 933..955
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 956..971
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 972..993
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 994..1278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 54..356
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 391..627
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 710..998
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1033..1271
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 622..646
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000269|PubMed:15159385"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21439"
FT BINDING 429..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21439,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21439"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21439"
FT BINDING 1045
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21439"
FT BINDING 1070..1076
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21439,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21439"
FT BINDING 1176..1178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21439,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21440"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1278 AA; 140655 MW; D4FB6BE745AF73BF CRC64;
MDLEAARNGT ARRLDGDFEL GSISNQSREK KKKVNLIGPL TLFRYSDWQD KLFMLLGTAM
AIAHGSGLPL MMIVFGEMTD KFVDNAGNFS LPVNFSLSML NPGRILEEEM TRYAYYYSGL
GGGVLLAAYI QVSFWTLAAG RQIRKIRQKF FHAILRQEMG WFDIKGTTEL NTRLTDDISK
ISEGIGDKVG MFFQAIATFF AGFIVGFIRG WKLTLVIMAI TAILGLSTAV WAKILSTFSD
KELAAYAKAG AVAEEALGAI RTVIAFGGQN KELERYQKHL ENAKKIGIKK AISANISMGI
AFLLIYASYA LAFWYGSTLV ISKEYTIGNA MTVFFSILIG AFSVGQAAPC IDAFPNARGA
AYVIFDIIDN NPKIDSFSER GHKPDSIKGN LEFSDVHFSY PSRANIKILK GLNLKVKSGQ
TVALVGNSGC GKSTTVQLLQ RLYDPTEGTI SIDGQDIRNF NVRCLREFIG VVSQEPVLFS
TTIAENIRYG RGNVTMDEIK KAVKEANAYD FIMKLPQKFD TLVGDRGAQL SGGQKQRIAI
ARALVRNPKI LLLDEATSAL DTESEAEVQA ALDKAREGRT TIVIAHRLST VRNADVIAGF
EDGVIVEQGS HSELIKKEGI YFRLVNMQTS GSQILSEEFE VELSDEKAAG GVAPNGWKAR
IFRNSTKKSL KSSRAHQNRL DVETNELDAN VPPVSFLKVL RLNKTEWPYF VVGTLCAIAN
GALQPAFSII LSEMIAIFGP GDDTVKQQKC NMFSLVFLGL GVHSFFTFFL QGFTFGKAGE
ILTTRLRSMA FKAMLRQDMS WFDDHKNSTG ALSTRLATDA AQVQGATGTR LALIAQNTAN
LGTGIIISFI YGWQLTLLLL SVVPFIAVAG IVEMKMLAGN AKRDKKEMEA AGKIATEAIE
NIRTVVSLTQ ERKFESMYVE KLHGPYRNSV RKAHIYGITF SISQAFMYFS YAGCFRFGSY
LIVNGHMRFK DVILVFSAIV LGAVALGHAS SFAPDYAKAK LSAAYLFSLF ERQPLIDSYS
REGMWPDKFE GSVTFNEVVF NYPTRANVPV LQGLSLEVKK GQTLALVGSS GCGKSTVVQL
LERFYDPMAG TVLLDGQEAK KLNVQWLRAQ LGIVSQEPIL FDCSIAKNIA YGDNSRVVSQ
DEIVRAAKEA NIHPFIETLP QKYETRVGDK GTQLSGGQKQ RIAIARALIR QPRVLLLDEA
TSALDTESEK VVQEALDKAR EGRTCIVIAH RLSTIQNADL IVVIDNGKVK EHGTHQQLLA
QKGIYFSMVN IQAGTQNL
