CFTR_PIG
ID CFTR_PIG Reviewed; 1482 AA.
AC Q6PQZ2; Q2QLD5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RA Wang Y., Yang H., Gao H., He C., Ma T.;
RT "Cloning and functional analysis of porcine cystic fibrosis transmembrane
RT conductance regulator.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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).
RN [3]
RP FUNCTION.
RX PubMed=26823428; DOI=10.1126/science.aad5589;
RA Shah V.S., Meyerholz D.K., Tang X.X., Reznikov L., Abou Alaiwa M.,
RA Ernst S.E., Karp P.H., Wohlford-Lenane C.L., Heilmann K.P., Leidinger M.R.,
RA Allen P.D., Zabner J., McCray P.B. Jr., Ostedgaard L.S., Stoltz D.A.,
RA Randak C.O., Welsh M.J.;
RT "Airway acidification initiates host defense abnormalities in cystic
RT fibrosis mice.";
RL Science 351:503-507(2016).
CC -!- FUNCTION: Epithelial ion channel that plays an important role in the
CC regulation of epithelial ion and water transport and fluid homeostasis
CC (PubMed:26823428). Mediates the transport of chloride ions across the
CC cell membrane (By similarity). Channel activity is coupled to ATP
CC hydrolysis. The ion channel is also permeable to HCO(3)(-); selectivity
CC depends on the extracellular chloride concentration. Exerts its
CC function also by modulating the activity of other ion channels and
CC transporters. Contributes to the regulation of the pH and the ion
CC content of the epithelial fluid layer (PubMed:26823428). Modulates the
CC activity of the epithelial sodium channel (ENaC) complex, in part by
CC regulating the cell surface expression of the ENaC complex. May
CC regulate bicarbonate secretion and salvage in epithelial cells by
CC regulating the transporter SLC4A7. Can inhibit the chloride channel
CC activity of ANO1 (By similarity). Plays a role in the chloride and
CC bicarbonate homeostasis during sperm epididymal maturation and
CC capacitation (By similarity). {ECO:0000250|UniProtKB:P13569,
CC ECO:0000250|UniProtKB:P26361, ECO:0000269|PubMed:26823428}.
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; AY585334; AAS98211.1; -; mRNA.
DR EMBL; DP000017; AAR16305.1; -; Genomic_DNA.
DR RefSeq; NP_001098420.1; NM_001104950.1.
DR AlphaFoldDB; Q6PQZ2; -.
DR SMR; Q6PQZ2; -.
DR STRING; 9823.ENSSSCP00000017611; -.
DR PaxDb; Q6PQZ2; -.
DR GeneID; 403154; -.
DR KEGG; ssc:403154; -.
DR CTD; 1080; -.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; Q6PQZ2; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0005829; C:cytosol; IBA:GO_Central.
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:0016020; C:membrane; IBA:GO_Central.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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..1482
FT /note="Cystic fibrosis transmembrane conductance regulator"
FT /id="PRO_0000093426"
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..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 860..880
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 881..919
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 920..940
FT /note="Discontinuously helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 941..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 992..1012
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1013..1014
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1015..1035
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1036..1096
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1097..1117
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1118..1131
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1132..1152
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1153..1482
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 860..1156
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1212..1445
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 654..832
FT /note="Disordered R region"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1388..1482
FT /note="Interaction with GORASP2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1454..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1480..1482
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT COMPBIAS 1464..1482
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 1221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 1246..1253
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 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 1458
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 1397
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 901
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"
FT CONFLICT 145
FT /note="P -> L (in Ref. 2; AAR16305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1482 AA; 168188 MW; 7584378DD43DC1B7 CRC64;
MQRSPLEKAS IFSKLFFSWT RPILRKGYRQ RLELSDIYHI SSSDSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGIILYL GEVTKAVQPL LLGRIIASYD PDNKAERSIA
IYLGVGLCLL FIVRTLLLHP AIFGPHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVTL LMGLLWELLQ ASAFCGLAFL VVLALFQAGL
GKMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA
YVRYFNSSAF FFSGLFVVFL SVLPYALLKG IMLRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGKLFE KAKQNNNSRK
ISNGDNSLFF SNFSLLGTPV LKDISFKIER GQLLAVAGST GAGKTSLLMM IMGELEPSEG
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQSQRPDF SSKLMGYDTF DQFTAERRNS
IITETLRRFS LEGDASVSWN ETKKQSFKQT GEFGEKRKNS ILNSINSIRK FSIVQKTPLQ
MNGFEEDSGE PLERRLSLVP DSEHGEAILP RSNVINAGPT FQGRRRQSVL NLMTRSSVNQ
GQSIHRKTAT STRKMSLVPQ ANLTEIDIYS RRLSQDTGLE ISEEINEEDL RECFFDDVES
IPTVTTWNTY LRYVTVHKSL IFVLIWCLVV FLAEVAACLV VLCLLKKTSP QDKGNSTKGA
NNSYAVIITS TSAYYVFYIY VGVADGLLAL GLFRGLPLVH TLITVSKILH RKMLHSVLQA
PMSTLNTLKA GGILNRFSKD IAVLDDLLPL TIFDFIQLLL IVIGAVAVVS VLKPYIFLAT
VPVIVAFILL RAYFLHTSQQ LKQLESEGRS PIFTHLITSL KGLWTLRAFG RQPYFETLFH
KALNLHTANW FLYLSTLRWF QMRIEMIFVI FFIAVTFISI LTTGEGEGTV GIILTLAMNI
MSTLQWAVNS SIDVDSLMRS VSRVFKFIDM PAEGDQPNRS FKPSKDGQLS KVMIIENQHV
KKDDIWPSGG QMTVKDLTAK YVDGGNAVLE NISFSISPGQ RVGLLGRTGS GKSTLLLAFL
RLLNTEGEIQ VDGVSWDSIT LQQWRKAFGV IPQKVFIFSG TFRKNLDPYG QWNDQEIWKV
AEEVGLRSVI EQFPGKLDFV LVDGGCVLSH GHKQLMCLAR SVLGKAKILL LDEPSAHLDP
ITYQIIRRTL KQAFADCTVI LSEHRIEAML ECQRFLVIEE NKVRQYDSIQ RLLSEKSLFR
QAISPLDRLK LLPHRNSSKQ RSRSKIAALK EETEEEVQET RL
