ASIC2_HUMAN
ID ASIC2_HUMAN Reviewed; 512 AA.
AC Q16515; E9PBX2; Q13553; Q6DJU1; Q8N3E2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Acid-sensing ion channel 2 {ECO:0000303|PubMed:10842183};
DE Short=ASIC2 {ECO:0000303|PubMed:10842183};
DE AltName: Full=Amiloride-sensitive brain sodium channel;
DE AltName: Full=Amiloride-sensitive cation channel 1, neuronal;
DE AltName: Full=Amiloride-sensitive cation channel neuronal 1;
DE AltName: Full=Brain sodium channel 1 {ECO:0000303|PubMed:9037075};
DE Short=BNC1 {ECO:0000303|PubMed:8626462};
DE Short=BNaC1 {ECO:0000303|PubMed:9037075};
DE AltName: Full=Mammalian degenerin homolog {ECO:0000303|PubMed:8631835};
DE Short=MDEG {ECO:0000303|PubMed:8631835};
GN Name=ASIC2; Synonyms=ACCN, ACCN1, BNAC1, MDEG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8626462; DOI=10.1074/jbc.271.14.7879;
RA Price M.P., Snyder P.M., Welsh M.J.;
RT "Cloning and expression of a novel human brain Na+ channel.";
RL J. Biol. Chem. 271:7879-7882(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8631835; DOI=10.1074/jbc.271.18.10433;
RA Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M.;
RT "The mammalian degenerin MDEG, an amiloride-sensitive cation channel
RT activated by mutations causing neurodegeneration in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 271:10433-10436(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Frontal cortex;
RX PubMed=9037075; DOI=10.1073/pnas.94.4.1459;
RA Garcia-Anoveros J., Derfler B.H., Neville-Golden J., Hyman B.T.,
RA Corey D.P.;
RT "BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels
RT related to degenerins and epithelial sodium channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1459-1464(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH ASIC3, AND TISSUE SPECIFICITY.
RX PubMed=10842183; DOI=10.1074/jbc.m004114200;
RA Babinski K., Catarsi S., Biagini G., Seguela P.;
RT "Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric proton-
RT gated channels sensitive to Gd3+.";
RL J. Biol. Chem. 275:28519-28525(2000).
RN [8]
RP INTERACTION WITH PRKCABP.
RX PubMed=11802773; DOI=10.1042/0264-6021:3610443;
RA Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.;
RT "Interaction of the synaptic protein PICK1 (protein interacting with C
RT kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+
RT channel 1) and ASIC (acid-sensing ion channel).";
RL Biochem. J. 361:443-450(2002).
RN [9]
RP INTERACTION WITH MAMBALGIN-1, AND SUBUNIT.
RX PubMed=23034652; DOI=10.1038/nature11494;
RA Diochot S., Baron A., Salinas M., Douguet D., Scarzello S.,
RA Dabert-Gay A.-S., Debayle D., Friend V., Alloui A., Lazdunski M.,
RA Lingueglia E.;
RT "Black mamba venom peptides target acid-sensing ion channels to abolish
RT pain.";
RL Nature 490:552-555(2012).
CC -!- FUNCTION: Cation channel with high affinity for sodium, which is gated
CC by extracellular protons and inhibited by the diuretic amiloride. Also
CC permeable for Li(+) and K(+). Generates a biphasic current with a fast
CC inactivating and a slow sustained phase. Heteromeric channel assembly
CC seems to modulate.
CC -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
CC similarity). Interacts with STOM; this regulates channel activity (By
CC similarity). Interacts with PRKCABP and ASIC3. Heterotrimer of Asic1a-
CC Asic2a interacts with the snake venom mambalgin-1 (PubMed:23034652).
CC Heterotrimer of Asic1a-Asic2a interacts with the snake venom mambalgin-
CC 2 and mambalgin-3 (By similarity). Heterotrimer of Asic1a-Asic2b
CC interacts with the snake venom mambalgin-1 and mambalgin-2 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q62962,
CC ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11802773}.
CC -!- INTERACTION:
CC Q16515; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-79149, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Localized at the plasma membrane of
CC neurons, in the soma and punctated peripheral processes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Asic2a {ECO:0000303|PubMed:10842183};
CC IsoId=Q16515-1; Sequence=Displayed;
CC Name=2; Synonyms=Asic2b, MDEG2;
CC IsoId=Q16515-2; Sequence=VSP_015590, VSP_015591;
CC -!- TISSUE SPECIFICITY: Brain and spinal cord. Isoform 1 is also detected
CC in testis, liver, colon and ovary. {ECO:0000269|PubMed:10842183,
CC ECO:0000269|PubMed:8631835}.
CC -!- MISCELLANEOUS: Inhibited by anti-inflammatory drugs like salicylic acid
CC (By similarity). Regulated by Zn(2+). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC2 subfamily. {ECO:0000305}.
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DR EMBL; U50352; AAC50432.1; -; mRNA.
DR EMBL; U53212; AAC50498.1; -; mRNA.
DR EMBL; U57352; AAB49182.1; -; mRNA.
DR EMBL; AL834182; CAD38879.1; -; mRNA.
DR EMBL; AC003687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075042; AAH75042.1; -; mRNA.
DR EMBL; BC075043; AAH75043.1; -; mRNA.
DR CCDS; CCDS11276.1; -. [Q16515-2]
DR CCDS; CCDS42296.1; -. [Q16515-1]
DR RefSeq; NP_001085.2; NM_001094.4. [Q16515-1]
DR RefSeq; NP_899233.1; NM_183377.1. [Q16515-2]
DR PDB; 6L6P; X-ray; 3.08 A; A/B/C=13-461.
DR PDBsum; 6L6P; -.
DR AlphaFoldDB; Q16515; -.
DR SMR; Q16515; -.
DR BioGRID; 106558; 18.
DR IntAct; Q16515; 2.
DR MINT; Q16515; -.
DR DrugBank; DB00594; Amiloride.
DR DrugCentral; Q16515; -.
DR GuidetoPHARMACOLOGY; 685; -.
DR GlyGen; Q16515; 2 sites.
DR iPTMnet; Q16515; -.
DR PhosphoSitePlus; Q16515; -.
DR BioMuta; ASIC2; -.
DR DMDM; 2500840; -.
DR jPOST; Q16515; -.
DR MassIVE; Q16515; -.
DR PeptideAtlas; Q16515; -.
DR PRIDE; Q16515; -.
DR ProteomicsDB; 19311; -.
DR ProteomicsDB; 60887; -. [Q16515-1]
DR ProteomicsDB; 60888; -. [Q16515-2]
DR Antibodypedia; 15465; 218 antibodies from 32 providers.
DR DNASU; 40; -.
DR Ensembl; ENST00000225823.7; ENSP00000225823.2; ENSG00000108684.15. [Q16515-2]
DR Ensembl; ENST00000359872.6; ENSP00000352934.6; ENSG00000108684.15. [Q16515-1]
DR GeneID; 40; -.
DR KEGG; hsa:40; -.
DR MANE-Select; ENST00000225823.7; ENSP00000225823.2; NM_183377.2; NP_899233.1. [Q16515-2]
DR UCSC; uc002hht.4; human. [Q16515-1]
DR CTD; 40; -.
DR DisGeNET; 40; -.
DR GeneCards; ASIC2; -.
DR HGNC; HGNC:99; ASIC2.
DR HPA; ENSG00000108684; Group enriched (brain, cervix, endometrium, retina).
DR MIM; 601784; gene.
DR neXtProt; NX_Q16515; -.
DR OpenTargets; ENSG00000108684; -.
DR PharmGKB; PA24433; -.
DR VEuPathDB; HostDB:ENSG00000108684; -.
DR GeneTree; ENSGT00940000154991; -.
DR HOGENOM; CLU_020415_1_2_1; -.
DR InParanoid; Q16515; -.
DR OMA; FPSHTQV; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q16515; -.
DR TreeFam; TF330663; -.
DR PathwayCommons; Q16515; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q16515; -.
DR BioGRID-ORCS; 40; 7 hits in 1060 CRISPR screens.
DR ChiTaRS; ASIC2; human.
DR GeneWiki; ACCN1; -.
DR GenomeRNAi; 40; -.
DR Pharos; Q16515; Tchem.
DR PRO; PR:Q16515; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q16515; protein.
DR Bgee; ENSG00000108684; Expressed in prefrontal cortex and 98 other tissues.
DR Genevisible; Q16515; HS.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0022839; F:ion gated channel activity; IEA:Ensembl.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; TAS:ProtInc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0007422; P:peripheral nervous system development; TAS:ProtInc.
DR GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:0003026; P:regulation of systemic arterial blood pressure by aortic arch baroreceptor feedback; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0050915; P:sensory perception of sour taste; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
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; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Acid-sensing ion channel 2"
FT /id="PRO_0000181290"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..427
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62962"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62962"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 92..193
FT /evidence="ECO:0000250"
FT DISULFID 171..178
FT /evidence="ECO:0000250"
FT DISULFID 289..364
FT /evidence="ECO:0000250"
FT DISULFID 307..360
FT /evidence="ECO:0000250"
FT DISULFID 311..358
FT /evidence="ECO:0000250"
FT DISULFID 320..342
FT /evidence="ECO:0000250"
FT DISULFID 322..334
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015590"
FT VAR_SEQ 185
FT /note="T -> MSRIGGAGLPAAALTGPGRFRMAREEPAPAALAAAGQPGGGRGGERA
FT LQGPGVARRGRPSLSRAKLHGLRHMCAGRTAAGGSFQRRALWVLAFCTSFGLLLSWSSN
FT RLLYWLSFPSHTRVHREWSRQLPFPAVTVCNNNPLRFPRLSKGDLYYAGHWLGLLLPNR
FT TARPLVSELLRGDEPRRQWFRKLADFRLFLPPRHFEGISAAFMDRLGHQLEDMLLSCKY
FT RGELCGPHNFSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015591"
FT VARIANT 354
FT /note="D -> G (in dbSNP:rs16967895)"
FT /id="VAR_052036"
FT CONFLICT 495
FT /note="T -> A (in Ref. 1; AAC50432)"
FT /evidence="ECO:0000305"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:6L6P"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 44..68
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6L6P"
FT TURN 111..115
FT /evidence="ECO:0007829|PDB:6L6P"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 268..280
FT /evidence="ECO:0007829|PDB:6L6P"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 364..379
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:6L6P"
FT STRAND 402..422
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 425..439
FT /evidence="ECO:0007829|PDB:6L6P"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:6L6P"
FT CONFLICT Q16515-2:67
FT /note="H -> R (in Ref. 4; CAD38879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57709 MW; 7C95B0B32EFF2814 CRC64;
MDLKESPSEG SLQPSSIQIF ANTSTLHGIR HIFVYGPLTI RRVLWAVAFV GSLGLLLVES
SERVSYYFSY QHVTKVDEVV AQSLVFPAVT LCNLNGFRFS RLTTNDLYHA GELLALLDVN
LQIPDPHLAD PSVLEALRQK ANFKHYKPKQ FSMLEFLHRV GHDLKDMMLY CKFKGQECGH
QDFTTVFTKY GKCYMFNSGE DGKPLLTTVK GGTGNGLEIM LDIQQDEYLP IWGETEETTF
EAGVKVQIHS QSEPPFIQEL GFGVAPGFQT FVATQEQRLT YLPPPWGECR SSEMGLDFFP
VYSITACRID CETRYIVENC NCRMVHMPGD APFCTPEQHK ECAEPALGLL AEKDSNYCLC
RTPCNLTRYN KELSMVKIPS KTSAKYLEKK FNKSEKYISE NILVLDIFFE ALNYETIEQK
KAYEVAALLG DIGGQMGLFI GASILTILEL FDYIYELIKE KLLDLLGKEE DEGSHDENVS
TCDTMPNHSE TISHTVNVPL QTTLGTLEEI AC
