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CFTR_MACFU
ID   CFTR_MACFU              Reviewed;        1481 AA.
AC   Q7JII7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Macaca fuscata fuscata (Japanese macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wine J.J., Kuo E., Hurlock G., Glavac D., Dean M.;
RT   "CFTR genomic sequences from five primate species.";
RL   Submitted (JUN-1999) 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; AF162373; AAD46904.1; -; Genomic_DNA.
DR   EMBL; AF162347; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162348; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162349; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162350; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162351; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162352; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162353; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162354; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162355; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162356; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162357; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162358; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162359; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162360; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162361; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162362; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162363; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162364; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162365; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162366; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162367; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162368; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162369; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162370; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162371; AAD46904.1; JOINED; Genomic_DNA.
DR   EMBL; AF162372; AAD46904.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q7JII7; -.
DR   BMRB; Q7JII7; -.
DR   SMR; Q7JII7; -.
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..1481
FT                   /note="Cystic fibrosis transmembrane conductance regulator"
FT                   /id="PRO_0000093421"
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..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          1211..1444
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          1387..1481
FT                   /note="Interaction with GORASP2"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOTIF           1479..1481
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
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         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         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         1445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         1457
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           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        688
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
SQ   SEQUENCE   1481 AA;  168489 MW;  A9AE0F3BB1197570 CRC64;
     MQRSPLEKAS VVSKLFFSWT RPILRKGYRQ RLELSDIYQI PSADSADNLS EKLEREWDRE
     LASKKNPKLI NALRRCFFWR FMFYGILLYL GEVTKAVQPL LLGRIIASYD PDNKEERSIA
     IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
     VSLLSNNLNK FDEGLALAHF VWIVPLQVAL LMGLIWELLQ ASAFCGLGFL IVLALFQAGL
     GRMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA
     YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IVLRKIFTTI SFCIVLRMAV TRQFPWAVQT
     WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQNNSNRK
     TSNDDDSLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMM IMGELEPSEG
     KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV INACQLEEDI SKFAEKDNIV
     LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
     ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLRPDF SSKLMGYDSF DQFSAERRNS
     ILTETLRRFS LEGDAPVSWT ETKKQSFKQT GEFGEKRKNS ILNPINSIRK FSIVQKTPLQ
     MNGIEEDSDE PLERRLSLVP DSEQGEVILP RISVISTGPT LQARRRQSVL NLMTHSVNQG
     QSIHRKTAAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDDMESI
     PAVTTWNTYL RYITVHKSLI FVLIWCLVIF LAEVAASLVV LWFLGNTPPQ DKGNSTYSRN
     NSYAVIITRT SSYYVFYIYV GVADTLLAMG FFRGLPLVHT LITVSKILHH KMLHSVLQAP
     MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVAV LQPYIFVATV
     PVIVAFIMLR AYFLQTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK
     ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGTVG IILTLAMNIM
     STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEEGKPTRST KPYKNGQLSK VMVIENSHVK
     KDDIWPSGGQ MTVKDLTAKY TEGGNPILEN ISFSISPGQR VGLLGRTGSG KSTLLSAFLR
     LLNTEGEIQI DGVSWDSITL QQWRKAFGVI PQKVFIFSGT FRKNLDPYEQ WSDQEIWKVA
     DEVGLRSVIE QFPGKLDFVL VDGGCVLSHG HKQLMCLARS VLSKAKILLL DEPSAHLDPV
     TYQIIRRTLK QAFADCTVIL CEHRIEAMLE CQQFLVIEEN KVRQYDSIQK LLNERSLFRQ
     AISPSDRVKL FPHRNSSKCK TQPQIAALKE ETEEEVQDTR L
 
 
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