CFTR_PLEMO
ID CFTR_PLEMO Reviewed; 1480 AA.
AC Q2QLB4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cystic fibrosis transmembrane conductance regulator;
DE Short=CFTR;
DE AltName: Full=ATP-binding cassette sub-family C member 7;
DE AltName: Full=Channel conductance-controlling ATPase;
DE EC=5.6.1.6 {ECO:0000250|UniProtKB:P13569};
DE AltName: Full=cAMP-dependent chloride channel;
GN Name=CFTR; Synonyms=ABCC7;
OS Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC Pitheciidae; Callicebinae; Plecturocebus.
OX NCBI_TaxID=9523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Epithelial ion channel that plays an important role in the
CC regulation of epithelial ion and water transport and fluid homeostasis.
CC Mediates the transport of chloride ions across the cell membrane (By
CC similarity). Channel activity is coupled to ATP hydrolysis. The ion
CC channel is also permeable to HCO(3)(-); selectivity depends on the
CC extracellular chloride concentration. Exerts its function also by
CC modulating the activity of other ion channels and transporters.
CC Contributes to the regulation of the pH and the ion content of the
CC epithelial fluid layer. Modulates the activity of the epithelial sodium
CC channel (ENaC) complex, in part by regulating the cell surface
CC expression of the ENaC complex. May regulate bicarbonate secretion and
CC salvage in epithelial cells by regulating the transporter SLC4A7. Can
CC inhibit the chloride channel activity of ANO1 (By similarity). Plays a
CC role in the chloride and bicarbonate homeostasis during sperm
CC epididymal maturation and capacitation (By similarity).
CC {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open
CC Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000250|UniProtKB:P13569};
CC -!- SUBUNIT: Monomer; does not require oligomerization for channel
CC activity. May form oligomers in the membrane (By similarity). Interacts
CC with SLC26A3, SLC26A6 and SLC9A3R1 (By similarity). Interacts with
CC SHANK2 (By similarity). Interacts with MYO6 (By similarity). Interacts
CC (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR
CC internalization and thereby decreases channel activity. Interacts with
CC SLC4A7 through SLC9A3R1. Found in a complex with MYO5B and RAB11A.
CC Interacts with ANO1. Interacts with SLC26A8 (By similarity). Interacts
CC with AHCYL1; the interaction increases CFTR activity (By similarity).
CC Interacts with CSE1L (By similarity). The core-glycosylated form
CC interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER
CC stress (By similarity). Interacts with MARCHF2; the interaction leads
CC to CFTR ubiqtuitination and degradation (By similarity).
CC {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361,
CC ECO:0000250|UniProtKB:P34158}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Cell membrane
CC {ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Nucleus {ECO:0000250|UniProtKB:P34158}.
CC Note=The channel is internalized from the cell surface into an
CC endosomal recycling compartment, from where it is recycled to the cell
CC membrane. In the oviduct and bronchus, detected on the apical side of
CC epithelial cells, but not associated with cilia. In Sertoli cells, a
CC processed product is detected in the nucleus. ER stress induces
CC GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of
CC core-glycosylated CFTR to cell membrane. {ECO:0000250|UniProtKB:P13569,
CC ECO:0000250|UniProtKB:P34158}.
CC -!- DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC
CC transporter nucleotide-binding domains. The two ATP-binding domains
CC interact with each other, forming a head-to-tail dimer. Normal ATPase
CC activity requires interaction between the two domains. The first ABC
CC transporter nucleotide-binding domain has no ATPase activity by itself.
CC {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
CC -!- DOMAIN: The PDZ-binding motif mediates interactions with GOPC and with
CC the SLC4A7, SLC9A3R1/EBP50 complex. {ECO:0000250|UniProtKB:P13569}.
CC -!- DOMAIN: The disordered R region mediates channel activation when it is
CC phosphorylated, but not in the absence of phosphorylation.
CC {ECO:0000250|UniProtKB:P13569}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.
CC -!- PTM: Phosphorylated; cAMP treatment promotes phosphorylation and
CC activates the channel. Dephosphorylation decreases the ATPase activity
CC (in vitro). Phosphorylation at PKA sites activates the channel.
CC Phosphorylation at PKC sites enhances the response to phosphorylation
CC by PKA. Phosphorylated by AMPK; this inhibits channel activity.
CC {ECO:0000250|UniProtKB:P13569}.
CC -!- PTM: Ubiquitinated, leading to its degradation in the lysosome.
CC Deubiquitination by USP10 in early endosomes enhances its endocytic
CC recycling to the cell membrane. Ubiquitinated by RNF185 during ER
CC stress. Ubiquitinated by MARCHF2 (By similarity).
CC {ECO:0000250|UniProtKB:P13569}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
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DR EMBL; DP000019; ABB89795.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2QLB4; -.
DR SMR; Q2QLB4; -.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005260; F:intracellularly ATP-gated chloride channel activity; ISS:UniProtKB.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
DR GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
DR GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
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; IPR009147; CFTR/ABCC7.
DR InterPro; IPR025837; CFTR_reg_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF19; PTHR24223:SF19; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14396; CFTR_R; 1.
DR PRINTS; PR01851; CYSFIBREGLTR.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR TIGRFAMs; TIGR01271; CFTR_protein; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Chloride; Chloride channel;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Isomerase; Isopeptide bond; Lipoprotein; Membrane; Nucleotide-binding;
KW Nucleus; Palmitate; Phosphoprotein; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..1480
FT /note="Cystic fibrosis transmembrane conductance regulator"
FT /id="PRO_0000226369"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 78..98
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 99..122
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 123..146
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 147..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 196..216
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 217..222
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 223..243
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 244..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 299..319
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 320..339
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 340..358
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 359..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 859..879
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 880..918
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 919..939
FT /note="Discontinuously helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 940..990
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 991..1011
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1012..1013
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1014..1034
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1035..1095
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1096..1116
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1117..1130
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1131..1151
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1152..1480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT DOMAIN 81..365
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 423..646
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 859..1155
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1210..1443
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 654..831
FT /note="Disordered R region"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1386..1480
FT /note="Interaction with GORASP2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1452..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1478..1480
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT COMPBIAS 1463..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 458..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P26361"
FT BINDING 1219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 1244..1251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 670
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 717
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 1444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT LIPID 524
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT LIPID 1395
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P13569"
SQ SEQUENCE 1480 AA; 168247 MW; 6F14FCBAFAB2E32B CRC64;
MQRSPLEKAS VVSKLFFSWT RPILKKGYRQ RLELSDIYQI PSADSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGILLYL GEVTKAVQPL LLGRIIASYD PDNKTERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVAL LMGLIWELLQ ASVFCGLGFL IVLALFQAGL
GRMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA
YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQSNNNRK
TSNGHDNLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMM IMGELEPSEG
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLRPDF SSKLMGYDSF DQFSSERRNS
ILTETLRRFS LEGDAPVSWT ETKKQSFKQT GEFGEKRKNS ILNSINSIRK FSIVHKTPLQ
MNGIEEDSDE PSERRLSLIP DSEQGEAILP RISVINTGPA LQVRRRQSVL NMMTHSVNQG
QSVHRKTTAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDDMESI
PAVTTWNTYL RYITLHKSLI FVLIWCLVIF LAEVAASLVV LWLLGNTSFQ DKGNSTYSRN
NSYAVIITNT SSYYVFYIYV GVADTLLALG FFRGLPLVHT LITVSKILHH KMLHSVLQAP
MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVSV LQPYIFLATV
PVIAAFILLR AYFLQTSQQL KQLESAGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK
ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGTVG IILTLAMNIM
STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEGKPTKSTK AYKNGQLSKV MIIENSHVKK
DDIWPSGGQM TIKDLTAKYI EGGNAILENI SFSISPGQRV GLLGRTGSGK STLLSAFLRL
LNTEGEIQID GVSWDSVTLQ QWRKAFGVIP QKVFIFTGTF RKNLDPYEQW SDQEVWKVAD
EVGLRSVIEQ FPGKLDFVLV DGGCVLSHGH KQLMCLARSV LSKAKILLLD EPSAHLDPVT
YQIIRRALKQ AFADCTVILC EHRIEAMLEC QQFLVIEENK VRQYDSIQKL LNEKSLFQQA
ISHSDRVKLF PHRNSSKYKS RPQIASLKEE TEEEVQETRL
