ACHA2_HUMAN
ID ACHA2_HUMAN Reviewed; 529 AA.
AC Q15822; A8KAX3; B4DK19; J3KMY9; Q9HAQ3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-2;
DE Flags: Precursor;
GN Name=CHRNA2;
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), AND VARIANT ALA-125.
RC TISSUE=Hypothalamus;
RX PubMed=8906617; DOI=10.1007/bf02736842;
RA Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E.,
RA Johnson E.C., Velicelebi G., Harpold M.M.;
RT "Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4
RT nicotinic acetylcholine receptor subunits and functional expression of the
RT alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits.";
RL J. Mol. Neurosci. 7:217-228(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-125.
RA Groot Kormelink P.J.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-125.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 59-265, SUBUNIT, AND MUTAGENESIS
RP OF TRP-115 AND TYR-225.
RX PubMed=27493220; DOI=10.1073/pnas.1602619113;
RA Kouvatsos N., Giastas P., Chroni-Tzartou D., Poulopoulou C., Tzartos S.J.;
RT "Crystal structure of a human neuronal nAChR extracellular domain in
RT pentameric assembly: Ligand-bound alpha2 homopentamer.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9635-9640(2016).
RN [7]
RP VARIANT ENFL4 ASN-279, AND CHARACTERIZATION OF VARIANT ENFL4 ASN-279.
RX PubMed=16826524; DOI=10.1086/506459;
RA Aridon P., Marini C., Di Resta C., Brilli E., De Fusco M., Politi F.,
RA Parrini E., Manfredi I., Pisano T., Pruna D., Curia G., Cianchetti C.,
RA Pasqualetti M., Becchetti A., Guerrini R., Casari G.;
RT "Increased sensitivity of the neuronal nicotinic receptor alpha2 subunit
RT causes familial epilepsy with nocturnal wandering and ictal fear.";
RL Am. J. Hum. Genet. 79:342-350(2006).
RN [8]
RP VARIANT BFIS6 TRP-376.
RX PubMed=25847220; DOI=10.1111/epi.12967;
RA Trivisano M., Terracciano A., Milano T., Cappelletti S., Pietrafusa N.,
RA Bertini E.S., Vigevano F., Specchio N.;
RT "Mutation of CHRNA2 in a family with benign familial infantile seizures:
RT Potential role of nicotinic acetylcholine receptor in various phenotypes of
RT epilepsy.";
RL Epilepsia 56:E53-E57(2015).
CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC extensive change in conformation that affects all subunits and leads to
CC opening of an ion-conducting channel across the plasma membrane.
CC -!- SUBUNIT: Neuronal AChR seems to be composed of two different types of
CC subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined
CC to beta-2 or beta-4 to give rise to functional receptors. The alpha-
CC 2:beta-2 nAChR complex is proposed to be a heteropentamer with two
CC subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and
CC HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3
CC stoichiometry; the subtypes differ in their subunit binding interfaces
CC which are involved in ligand binding. {ECO:0000305|PubMed:27493220}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15822-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15822-2; Sequence=VSP_055156;
CC -!- DISEASE: Epilepsy, nocturnal frontal lobe, 4 (ENFL4) [MIM:610353]: An
CC autosomal dominant focal epilepsy characterized by nocturnal seizures
CC associated with fear sensation, tongue movements, and nocturnal
CC wandering, closely resembling nightmares and sleep walking.
CC {ECO:0000269|PubMed:16826524}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Seizures, benign familial infantile, 6 (BFIS6) [MIM:610353]: A
CC form of benign familial infantile epilepsy, a neurologic disorder
CC characterized by afebrile seizures occurring in clusters during the
CC first year of life, without neurologic sequelae. BFIS6 inheritance is
CC autosomal dominant. {ECO:0000269|PubMed:25847220}. Note=The disease may
CC be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: With the use of epibatidine as high affinity ligand, an alpha-
CC 2 homopentamer has been purified and crystallized. Its physiological
CC relevance has not been proven. {ECO:0000305|PubMed:27493220}.
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DR EMBL; U62431; AAB40109.1; -; mRNA.
DR EMBL; Y16281; CAA76154.1; -; mRNA.
DR EMBL; AK296348; BAG59031.1; -; mRNA.
DR EMBL; AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC153866; AAI53867.1; -; mRNA.
DR CCDS; CCDS6059.1; -. [Q15822-1]
DR CCDS; CCDS64856.1; -. [Q15822-2]
DR RefSeq; NP_000733.2; NM_000742.3. [Q15822-1]
DR RefSeq; NP_001269384.1; NM_001282455.1. [Q15822-2]
DR RefSeq; XP_006716345.1; XM_006716282.1.
DR RefSeq; XP_011542690.1; XM_011544388.1.
DR PDB; 5FJV; X-ray; 3.20 A; A/B/C/D/E=59-265.
DR PDBsum; 5FJV; -.
DR AlphaFoldDB; Q15822; -.
DR SMR; Q15822; -.
DR ComplexPortal; CPX-2170; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR ComplexPortal; CPX-2190; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR CORUM; Q15822; -.
DR STRING; 9606.ENSP00000385026; -.
DR BindingDB; Q15822; -.
DR ChEMBL; CHEMBL2109230; -.
DR ChEMBL; CHEMBL2109236; -.
DR DrugBank; DB00732; Atracurium besylate.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB00411; Carbamoylcholine.
DR DrugBank; DB00565; Cisatracurium.
DR DrugBank; DB01245; Decamethonium.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB01135; Doxacurium.
DR DrugBank; DB07720; Epibatidine.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB00472; Fluoxetine.
DR DrugBank; DB00483; Gallamine triethiodide.
DR DrugBank; DB08960; Hexamethonium.
DR DrugBank; DB00657; Mecamylamine.
DR DrugBank; DB01336; Metocurine.
DR DrugBank; DB00416; Metocurine iodide.
DR DrugBank; DB01226; Mivacurium.
DR DrugBank; DB00184; Nicotine.
DR DrugBank; DB01337; Pancuronium.
DR DrugBank; DB01338; Pipecuronium.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB00728; Rocuronium.
DR DrugBank; DB05740; RPI-78M.
DR DrugBank; DB00202; Succinylcholine.
DR DrugBank; DB01199; Tubocurarine.
DR DrugBank; DB01339; Vecuronium.
DR DrugCentral; Q15822; -.
DR GuidetoPHARMACOLOGY; 463; -.
DR GlyGen; Q15822; 3 sites.
DR iPTMnet; Q15822; -.
DR PhosphoSitePlus; Q15822; -.
DR BioMuta; CHRNA2; -.
DR DMDM; 308153405; -.
DR MaxQB; Q15822; -.
DR PaxDb; Q15822; -.
DR PeptideAtlas; Q15822; -.
DR PRIDE; Q15822; -.
DR ProteomicsDB; 60776; -. [Q15822-1]
DR Antibodypedia; 10197; 174 antibodies from 24 providers.
DR DNASU; 1135; -.
DR Ensembl; ENST00000240132.7; ENSP00000240132.2; ENSG00000120903.13. [Q15822-2]
DR Ensembl; ENST00000407991.3; ENSP00000385026.1; ENSG00000120903.13. [Q15822-1]
DR GeneID; 1135; -.
DR KEGG; hsa:1135; -.
DR MANE-Select; ENST00000407991.3; ENSP00000385026.1; NM_000742.4; NP_000733.2.
DR UCSC; uc010lur.4; human. [Q15822-1]
DR CTD; 1135; -.
DR DisGeNET; 1135; -.
DR GeneCards; CHRNA2; -.
DR GeneReviews; CHRNA2; -.
DR HGNC; HGNC:1956; CHRNA2.
DR HPA; ENSG00000120903; Group enriched (brain, prostate).
DR MalaCards; CHRNA2; -.
DR MIM; 118502; gene.
DR MIM; 610353; phenotype.
DR neXtProt; NX_Q15822; -.
DR OpenTargets; ENSG00000120903; -.
DR Orphanet; 98784; Autosomal dominant nocturnal frontal lobe epilepsy.
DR PharmGKB; PA26489; -.
DR VEuPathDB; HostDB:ENSG00000120903; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158299; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q15822; -.
DR OMA; QHAKNKD; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q15822; -.
DR TreeFam; TF315605; -.
DR PathwayCommons; Q15822; -.
DR Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-HSA-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR SignaLink; Q15822; -.
DR BioGRID-ORCS; 1135; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; CHRNA2; human.
DR GeneWiki; CHRNA2; -.
DR GenomeRNAi; 1135; -.
DR Pharos; Q15822; Tchem.
DR PRO; PR:Q15822; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15822; protein.
DR Bgee; ENSG00000120903; Expressed in lateral nuclear group of thalamus and 138 other tissues.
DR ExpressionAtlas; Q15822; baseline and differential.
DR Genevisible; Q15822; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0050997; F:quaternary ammonium group binding; IEA:Ensembl.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; NAS:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:1905144; P:response to acetylcholine; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00254; NICOTINICR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..529
FT /note="Neuronal acetylcholine receptor subunit alpha-2"
FT /id="PRO_0000000340"
FT TOPO_DOM 27..264
FT /note="Extracellular"
FT TRANSMEM 265..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..502
FT /note="Cytoplasmic"
FT TRANSMEM 503..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 27..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..197
FT /evidence="ECO:0000250"
FT DISULFID 247..248
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT VAR_SEQ 82..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055156"
FT VARIANT 22
FT /note="T -> I (in dbSNP:rs2472553)"
FT /id="VAR_027639"
FT VARIANT 125
FT /note="T -> A (in dbSNP:rs891398)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8906617, ECO:0000269|Ref.2"
FT /id="VAR_027640"
FT VARIANT 279
FT /note="I -> N (in ENFL4; markedly increases receptor
FT sensitivity to acetylcholine; dbSNP:rs104894063)"
FT /evidence="ECO:0000269|PubMed:16826524"
FT /id="VAR_027641"
FT VARIANT 376
FT /note="R -> W (in BFIS6; unknown pathological significance;
FT dbSNP:rs1018084204)"
FT /evidence="ECO:0000269|PubMed:25847220"
FT /id="VAR_076498"
FT MUTAGEN 115
FT /note="W->A: Changes ligand activation kinetics in a alpha-
FT 2(+):alpha-2(-) subunit interface (in LS nAChR subtype)."
FT /evidence="ECO:0000269|PubMed:27493220"
FT MUTAGEN 225
FT /note="Y->F: Decreases ligand activation in LS nAChR
FT subtype; no effect in HS nAChR subtype."
FT /evidence="ECO:0000269|PubMed:27493220"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 84..99
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 104..116
FT /evidence="ECO:0007829|PDB:5FJV"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 124..129
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5FJV"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:5FJV"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:5FJV"
SQ SEQUENCE 529 AA; 59765 MW; E47062A1145E8BCC CRC64;
MGPSCPVFLS FTKLSLWWLL LTPAGGEEAK RPPPRAPGDP LSSPSPTALP QGGSHTETED
RLFKHLFRGY NRWARPVPNT SDVVIVRFGL SIAQLIDVDE KNQMMTTNVW LKQEWSDYKL
RWNPTDFGNI TSLRVPSEMI WIPDIVLYNN ADGEFAVTHM TKAHLFSTGT VHWVPPAIYK
SSCSIDVTFF PFDQQNCKMK FGSWTYDKAK IDLEQMEQTV DLKDYWESGE WAIVNATGTY
NSKKYDCCAE IYPDVTYAFV IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SDCGEKITLC
ISVLLSLTVF LLLITEIIPS TSLVIPLIGE YLLFTMIFVT LSIVITVFVL NVHHRSPSTH
TMPHWVRGAL LGCVPRWLLM NRPPPPVELC HPLRLKLSPS YHWLESNVDA EEREVVVEEE
DRWACAGHVA PSVGTLCSHG HLHSGASGPK AEALLQEGEL LLSPHMQKAL EGVHYIADHL
RSEDADSSVK EDWKYVAMVI DRIFLWLFII VCFLGTIGLF LPPFLAGMI
