ASIC1_CHICK
ID ASIC1_CHICK Reviewed; 527 AA.
AC Q1XA76;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Acid-sensing ion channel 1;
DE Short=ASIC1;
DE AltName: Full=Amiloride-sensitive cation channel 2, neuronal;
GN Name=ASIC1; Synonyms=ACCN2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16002453; DOI=10.1113/jphysiol.2005.087734;
RA Coric T., Zheng D., Gerstein M., Canessa C.M.;
RT "Proton sensitivity of ASIC1 appeared with the rise of fishes by changes of
RT residues in the region that follows TM1 in the ectodomain of the channel.";
RL J. Physiol. (Lond.) 568:725-735(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 26-463, SUBUNIT, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-367 AND ASN-394, FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND MUTAGENESIS OF 1-MET--SER-25 AND 464-LEU--CYS-527.
RX PubMed=17882215; DOI=10.1038/nature06163;
RA Jasti J., Furukawa H., Gonzales E.B., Gouaux E.;
RT "Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH.";
RL Nature 449:316-323(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-466, DISULFIDE BONDS, FUNCTION,
RP TOPOLOGY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19641589; DOI=10.1038/nature08218;
RA Gonzales E.B., Kawate T., Gouaux E.;
RT "Pore architecture and ion sites in acid-sensing ion channels and P2X
RT receptors.";
RL Nature 460:599-604(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 26-463 IN COMPLEX WITH SPIDER
RP VENOM PSALMOTOXIN-1, INTERACTION WITH SPIDER VENOM PSALMOTOXIN, SUBUNIT,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-367 AND ASN-394, AND MUTAGENESIS OF
RP 1-MET--SER-25 AND 464-LEU--CYS-527.
RX PubMed=22760635; DOI=10.1038/ncomms1917;
RA Dawson R.J., Benz J., Stohler P., Tetaz T., Joseph C., Huber S., Schmid G.,
RA Hugin D., Pflimlin P., Trube G., Rudolph M.G., Hennig M., Ruf A.;
RT "Structure of the acid-sensing ion channel 1 in complex with the gating
RT modifier Psalmotoxin 1.";
RL Nat. Commun. 3:936-943(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 14-463, GLYCOSYLATION AT ASN-367
RP AND ASN-394, FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF 1-MET--SER-13;
RP GLU-80 AND 464-LEU--CYS-527, AND DISULFIDE BOND.
RX PubMed=22842900; DOI=10.1038/nature11375;
RA Baconguis I., Gouaux E.;
RT "Structural plasticity and dynamic selectivity of acid-sensing ion channel-
RT spider toxin complexes.";
RL Nature 489:400-405(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 14-463 IN COMPLEXES WITH SODIUM
RP IONS; AMILORIDE AND THE HETERODIMERIC SNAKE VENOM NEUROTOXIN COMPOSED OF
RP MITTX-ALPHA AND MITTX-BETA, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP ACTIVITY REGULATION, TOPOLOGY, DOMAIN, AND DISULFIDE BOND.
RX PubMed=24507937; DOI=10.1016/j.cell.2014.01.011;
RA Baconguis I., Bohlen C.J., Goehring A., Julius D., Gouaux E.;
RT "X-ray structure of acid-sensing ion channel 1-snake toxin complex reveals
RT open state of a Na(+)-selective channel.";
RL Cell 156:717-729(2014).
CC -!- FUNCTION: Proton-gated sodium channel; it is activated by a drop of the
CC extracellular pH and then becomes rapidly desensitized. Generates a
CC biphasic current with a fast inactivating and a slow sustained phase.
CC Has high selectivity for sodium ions and can also transport lithium
CC ions with high efficiency. Can also transport potassium ions, but with
CC lower efficiency. It is nearly impermeable to the larger rubidium and
CC cesium ions. {ECO:0000269|PubMed:16002453, ECO:0000269|PubMed:17882215,
CC ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22842900,
CC ECO:0000269|PubMed:24507937}.
CC -!- ACTIVITY REGULATION: Inhibited by the diuretic amiloride. Inhibited by
CC Cs(1+) ions. Inhibited by the spider venom psalmotoxin-1; this locks
CC the channel into its desensitized conformation. Channel activity is
CC increased by the heterodimeric snake venom neurotoxin composed of
CC MitTx-alpha and MitTx-beta; this slows channel closure and increases
CC the magnitude of the steady-state current that is triggered by low pH.
CC {ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937}.
CC -!- SUBUNIT: Homotrimer. Interacts with spider venom psalmotoxin 1 with a
CC one to one stoichiometry. Interacts with the heterodimeric snake venom
CC neurotoxin composed of MitTx-alpha and MitTx-beta.
CC {ECO:0000269|PubMed:17882215, ECO:0000269|PubMed:19641589,
CC ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:24507937}.
CC -!- INTERACTION:
CC Q1XA76; Q1XA76: ASIC1; NbExp=10; IntAct=EBI-15659618, EBI-15659618;
CC Q1XA76; P60514; Xeno; NbExp=2; IntAct=EBI-15659618, EBI-16002043;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17882215,
CC ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:24507937}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:17882215,
CC ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:24507937}.
CC -!- DOMAIN: Channel opening involves a conformation change that affects
CC primarily the extracellular domain and the second transmembrane helix
CC and its orientation in the membrane. In the open state, the second
CC transmembrane helix is nearly perpendicular to the plane of the
CC membrane; in the desensitized state it is strongly tilted. Besides, the
CC second transmembrane domain is discontinuously helical in the open
CC state. The GAS motif of the selectivity filter is in an extended
CC conformation, giving rise to a distinct kink in the polypeptide chain.
CC A domain swap between subunits gives rise to a full-length
CC transmembrane helix. {ECO:0000269|PubMed:24507937}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC1 subfamily. {ECO:0000305}.
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DR EMBL; AY956393; AAY28986.1; -; mRNA.
DR RefSeq; NP_001035557.1; NM_001040467.1.
DR RefSeq; XP_015155720.1; XM_015300234.1.
DR RefSeq; XP_015155721.1; XM_015300235.1.
DR PDB; 2QTS; X-ray; 1.90 A; A/B/C/D/E/F=26-463.
DR PDB; 3IJ4; X-ray; 3.00 A; A=2-466.
DR PDB; 3S3W; X-ray; 2.60 A; A/B/C=26-463.
DR PDB; 3S3X; X-ray; 2.99 A; A/B/C=26-463.
DR PDB; 4FZ0; X-ray; 2.80 A; A/B/C=14-463.
DR PDB; 4FZ1; X-ray; 3.36 A; A=14-463.
DR PDB; 4NTW; X-ray; 2.07 A; A=14-463.
DR PDB; 4NTX; X-ray; 2.27 A; A=14-463.
DR PDB; 4NTY; X-ray; 2.65 A; A=14-463.
DR PDB; 4NYK; X-ray; 3.00 A; A=2-466.
DR PDB; 5WKU; X-ray; 2.95 A; A/B/C=25-463.
DR PDB; 5WKV; X-ray; 3.20 A; A/B/C=25-463.
DR PDB; 5WKX; X-ray; 4.03 A; A/B/C=25-463.
DR PDB; 5WKY; X-ray; 4.00 A; A/B/C=25-463.
DR PDB; 6AVE; EM; 3.70 A; A/B/C=1-527.
DR PDB; 6CMC; X-ray; 3.67 A; A=14-463.
DR PDB; 6VTK; EM; 2.82 A; A/B/C=1-527.
DR PDB; 6VTL; EM; 3.65 A; A/B/C=1-527.
DR PDB; 6X9H; X-ray; 3.01 A; A/B/C=26-463.
DR PDBsum; 2QTS; -.
DR PDBsum; 3IJ4; -.
DR PDBsum; 3S3W; -.
DR PDBsum; 3S3X; -.
DR PDBsum; 4FZ0; -.
DR PDBsum; 4FZ1; -.
DR PDBsum; 4NTW; -.
DR PDBsum; 4NTX; -.
DR PDBsum; 4NTY; -.
DR PDBsum; 4NYK; -.
DR PDBsum; 5WKU; -.
DR PDBsum; 5WKV; -.
DR PDBsum; 5WKX; -.
DR PDBsum; 5WKY; -.
DR PDBsum; 6AVE; -.
DR PDBsum; 6CMC; -.
DR PDBsum; 6VTK; -.
DR PDBsum; 6VTL; -.
DR PDBsum; 6X9H; -.
DR AlphaFoldDB; Q1XA76; -.
DR SMR; Q1XA76; -.
DR DIP; DIP-59283N; -.
DR IntAct; Q1XA76; 1.
DR STRING; 9031.ENSGALP00000010079; -.
DR TCDB; 1.A.6.1.5; the epithelial na(+) channel (enac) family.
DR iPTMnet; Q1XA76; -.
DR PRIDE; Q1XA76; -.
DR Ensembl; ENSGALT00000055224; ENSGALP00000057289; ENSGALG00000034025.
DR GeneID; 426883; -.
DR KEGG; gga:426883; -.
DR CTD; 41; -.
DR VEuPathDB; HostDB:geneid_426883; -.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000158414; -.
DR HOGENOM; CLU_020415_1_2_1; -.
DR InParanoid; Q1XA76; -.
DR OMA; RNCSHLF; -.
DR PhylomeDB; Q1XA76; -.
DR Reactome; R-GGA-2672351; Stimuli-sensing channels.
DR EvolutionaryTrace; Q1XA76; -.
DR PRO; PR:Q1XA76; -.
DR Proteomes; UP000000539; Unplaced.
DR Bgee; ENSGALG00000034025; Expressed in cerebellum and 4 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0044736; F:acid-sensing ion channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..527
FT /note="Acid-sensing ion channel 1"
FT /id="PRO_0000308417"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT TRANSMEM 47..70
FT /note="Helical"
FT TOPO_DOM 71..426
FT /note="Extracellular"
FT TRANSMEM 427..453
FT /note="Discontinuously helical"
FT TOPO_DOM 454..527
FT /note="Cytoplasmic"
FT MOTIF 443..445
FT /note="Selectivity filter"
FT /evidence="ECO:0000305"
FT SITE 72
FT /note="Important for channel gating"
FT SITE 80
FT /note="Important for channel desensitizing"
FT SITE 288
FT /note="Important for channel gating"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900"
FT DISULFID 94..195
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT DISULFID 173..180
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT DISULFID 291..366
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT DISULFID 309..362
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT DISULFID 313..360
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT DISULFID 322..344
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT DISULFID 324..336
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:22760635,
FT ECO:0000269|PubMed:22842900, ECO:0000269|PubMed:24507937,
FT ECO:0007744|PDB:2QTS, ECO:0007744|PDB:3IJ4,
FT ECO:0007744|PDB:3S3W, ECO:0007744|PDB:3S3X,
FT ECO:0007744|PDB:4FZ0, ECO:0007744|PDB:4FZ1,
FT ECO:0007744|PDB:4NTW, ECO:0007744|PDB:4NTX,
FT ECO:0007744|PDB:4NTY, ECO:0007744|PDB:4NYK"
FT MUTAGEN 1..25
FT /note="Missing: Impairs channel activity; when associated
FT with missing 464-L--C-527."
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:22760635"
FT MUTAGEN 1..13
FT /note="Missing: No effect on channel activity; when
FT associated with missing 464-L--C-527."
FT /evidence="ECO:0000269|PubMed:22842900"
FT MUTAGEN 80
FT /note="E->A: Strongly increases speed of desensitation."
FT /evidence="ECO:0000269|PubMed:22842900"
FT MUTAGEN 464..527
FT /note="Missing: No effect on channel activity; when
FT associated with missing 1-M--S-13. Impairs channel
FT activity; when associated with missing 1-M--S-25."
FT /evidence="ECO:0000269|PubMed:17882215,
FT ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6VTK"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6VTK"
FT HELIX 45..69
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6VTK"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:2QTS"
FT TURN 113..117
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:3IJ4"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6X9H"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 270..282
FT /evidence="ECO:0007829|PDB:2QTS"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4NTW"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 365..381
FT /evidence="ECO:0007829|PDB:2QTS"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:2QTS"
FT STRAND 404..425
FT /evidence="ECO:0007829|PDB:2QTS"
FT HELIX 427..457
FT /evidence="ECO:0007829|PDB:2QTS"
SQ SEQUENCE 527 AA; 60010 MW; 05BF363097F5A63E CRC64;
MMDLKVDEEE VDSGQPVSIQ AFASSSTLHG ISHIFSYERL SLKRVVWALC FMGSLALLAL
VCTNRIQYYF LYPHVTKLDE VAATRLTFPA VTFCNLNEFR FSRVTKNDLY HAGELLALLN
NRYEIPDTQT ADEKQLEILQ DKANFRNFKP KPFNMLEFYD RAGHDIREML LSCFFRGEQC
SPEDFKVVFT RYGKCYTFNA GQDGKPRLIT MKGGTGNGLE IMLDIQQDEY LPVWGETDET
SFEAGIKVQI HSQDEPPLID QLGFGVAPGF QTFVSCQEQR LIYLPPPWGD CKATTGDSEF
YDTYSITACR IDCETRYLVE NCNCRMVHMP GDAPYCTPEQ YKECADPALD FLVEKDNEYC
VCEMPCNVTR YGKELSMVKI PSKASAKYLA KKYNKSEQYI GENILVLDIF FEALNYETIE
QKKAYEVAGL LGDIGGQMGL FIGASILTVL ELFDYAYEVI KHRLCRRGKC RKNHKRNNTD
KGVALSMDDV KRHNPCESLR GHPAGMTYAA NILPHHPARG TFEDFTC
