CFTR_BOVIN
ID CFTR_BOVIN Reviewed; 1481 AA.
AC P35071; A4D7S2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1719001; DOI=10.1016/s0021-9258(18)54633-0;
RA Diamond G., Scanlin T.F., Zasloff M.A., Bevins C.L.;
RT "A cross-species analysis of the cystic fibrosis transmembrane conductance
RT regulator. Potential functional domains and regulatory sites.";
RL J. Biol. Chem. 266:22761-22769(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12917688; DOI=10.1038/nature01858;
RA Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA Haussler D., Green P., Miller W., Green E.D.;
RT "Comparative analyses of multi-species sequences from targeted genomic
RT regions.";
RL Nature 424:788-793(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M76128; AAA30772.1; -; mRNA.
DR EMBL; DP000008; AAR16263.1; -; Genomic_DNA.
DR PIR; A39323; A39323.
DR RefSeq; NP_776443.1; NM_174018.2.
DR AlphaFoldDB; P35071; -.
DR SMR; P35071; -.
DR STRING; 9913.ENSBTAP00000049907; -.
DR PaxDb; P35071; -.
DR PRIDE; P35071; -.
DR GeneID; 281067; -.
DR KEGG; bta:281067; -.
DR CTD; 1080; -.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; P35071; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 2: Evidence at transcript level;
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; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..1481
FT /note="Cystic fibrosis transmembrane conductance regulator"
FT /id="PRO_0000093416"
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..1481
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..645
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 1211..1444
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 653..831
FT /note="Disordered R region"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1387..1481
FT /note="Interaction with GORASP2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1453..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1479..1481
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT COMPBIAS 1464..1481
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 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P26361"
FT BINDING 1220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 1245..1252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 659
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 669
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 685
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 699
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 736
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 767
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 790
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 795
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 813
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT LIPID 523
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT LIPID 1396
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 CROSSLNK 687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT CONFLICT 15
FT /note="L -> V (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="Q -> R (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="L -> V (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="E -> D (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="S -> N (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="M -> L (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="P -> A (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068..1069
FT /note="FG -> LD (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1237
FT /note="P -> S (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1327
FT /note="S -> A (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1415
FT /note="L -> F (in Ref. 1; AAA30772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1481 AA; 167758 MW; 8368B627796D2D4B CRC64;
MQRSPLEKAS VVSKLFFSWT RPILKKGYRQ RLELSDIYHI SSSDSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGIILYL GEVTKAVQPL LLGRIIASYD PDNKVERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVTL LMGLLWELLQ AFTFCGLAFL IVLALLQAGL
GKMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKIIENLRQ TELKLTRKAA
YVRYLNSSAF FFSGFFVVFL SVLPYALLKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT DVVMENVTAF WEEGFSKLFE KAKENNNSRK
ISNGDNSLFF SNLLLGTPVL KDISFKIERG QLLAVAGSTG AGKTSLLMMI MGELEPSEGK
IKHSGRISFC SQYSWIMPGT IKDNIIFGVS YDEYRYRSVI KACQLEEDIS KFAEKDNVVL
GEGGITLSGG QRARISLARA VYKDADLYLL DSPFGYLDVL TEKEIFESCI CKLMANKTRI
LVTSKMEHLK KADKILILHE GSIYFYGTFS ELQNQRPDFS SKLMGCDTFD QFTAERRNSI
ITETLRRFSL EGDTSVSWNE TKKPSFKQTG EFGEKRKNSI LSSINSIRKF SVVQKTSLQM
NGIEGAADAP LERRLSLVPH SEPGEGILPR SNAVNSGPTF LGGRRQSVLN LMTGSSVNQG
QSIHRKTATS TRKMSLAPQA SLAEIDIYSR RLSQDTGLEI SEEINEEDLR DCFFDDVENI
PAVTTWNTYL RYITVHKSLM FVLIWCLVVF LVEVAASLVV LCLFPKIFFQ DKGNSTKSAN
NSYAVIITST SSYYIFYIYV GVADTLLALG LFRGLPLVHT LITVSKTLHH KMLQSVLQAP
MSTLNTLKTG GILNRFSKDI AVLDDLLPLT IFDFVQLLLI VIGAVVVVSV LQPYIFLATV
PVIAAFILLR AYFLHTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK
ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM
GTLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEDGKPNNSF RPSKDSQPSK VMIIENQHVK
KDDIWPSGGQ MTVKDLTAKY TDGGNAILEN ISFSISPGQR VGLLGRTGSG KSTLLLAFLR
LLNTKGEIQI DGVSWDSITL QQWRKAFGVI PQKVFIFSGT FRKNLDPYGQ WSDQEIWKVA
DEVGLRSVIE QFPGKLDFVL VDGGCVLSHG HKQLMCLARS VLSKAKILLL DEPSAHLDPI
TYQIIRRTLK QAFANCTVIL SEHRIEAMLE CQRFLVIEEN KVRQYDSIQR MLSEKSLFRQ
AISPADRLKL LPHRNSSRQR SRSNIAALKE ETEEEVQETK L
