ACHB_HUMAN
ID ACHB_HUMAN Reviewed; 501 AA.
AC P11230; B7Z5H1; Q8IZ46; Q96FB8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Acetylcholine receptor subunit beta;
DE Flags: Precursor;
GN Name=CHRNB1; Synonyms=ACHRB, CHRNB;
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).
RX PubMed=2740233; DOI=10.1093/nar/17.11.4391;
RA Beeson D.M.W., Brydson M., Newsom-Davis J.;
RT "Nucleotide sequence of human muscle acetylcholine receptor beta-subunit.";
RL Nucleic Acids Res. 17:4391-4391(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-32 AND
RP TYR-124.
RC TISSUE=Eye, and Muscle;
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 [5]
RP SUBUNIT.
RX PubMed=15609996; DOI=10.1021/bi048918g;
RA Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
RT "Alpha-conotoxins ImI and ImII target distinct regions of the human alpha7
RT nicotinic acetylcholine receptor and distinguish human nicotinic receptor
RT subtypes.";
RL Biochemistry 43:16019-16026(2004).
RN [6]
RP VARIANT CMS2A MET-285.
RX PubMed=8651643; DOI=10.1002/ana.410390607;
RA Gomez C.M., Maselli R., Gammack J., Lasalde J., Tamamizu S.,
RA Cornblath D.R., Lehar M., McNamee M., Kuncl R.W.;
RT "A beta-subunit mutation in the acetylcholine receptor channel gate causes
RT severe slow-channel syndrome.";
RL Ann. Neurol. 39:712-723(1996).
RN [7]
RP VARIANT CMS2A MET-289.
RX PubMed=8872460; DOI=10.1093/hmg/5.9.1217;
RA Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C.,
RA Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P.,
RA Sine S.M.;
RT "New mutations in acetylcholine receptor subunit genes reveal heterogeneity
RT in the slow-channel congenital myasthenic syndrome.";
RL Hum. Mol. Genet. 5:1217-1227(1996).
RN [8]
RP VARIANT CMS2C 449-GLU--GLU-451 DEL, AND CHARACTERIZATION OF VARIANT CMS2C
RP 449-GLU--GLU-451 DEL.
RX PubMed=10562302; DOI=10.1172/jci8179;
RA Quiram P.A., Ohno K., Milone M., Patterson M.C., Pruitt J.N. II,
RA Brengman J.M., Sine S.M., Engel A.G.;
RT "Mutation causing congenital myasthenia reveals acetylcholine receptor
RT beta/delta subunit interaction essential for assembly.";
RL J. Clin. Invest. 104:1403-1410(1999).
RN [9]
RP VARIANT CMS2A ALA-289, CHARACTERIZATION OF VARIANT CMS2A ALA-289, AND
RP FUNCTION.
RX PubMed=27375219; DOI=10.1002/humu.23043;
RA Shen X.M., Okuno T., Milone M., Otsuka K., Takahashi K., Komaki H.,
RA Giles E., Ohno K., Engel A.G.;
RT "Mutations causing slow-channel myasthenia reveal that a valine ring in the
RT channel pore of muscle AChR is optimized for stabilizing channel gating.";
RL Hum. Mutat. 37:1051-1059(2016).
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 {ECO:0000269|PubMed:27375219}.
CC -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC and gamma (in immature muscle) or epsilon (in mature muscle) chains.
CC The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon
CC subunits interacts with the alpha-conotoxin ImII (PubMed:15609996).
CC {ECO:0000269|PubMed:15609996}.
CC -!- INTERACTION:
CC P11230; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-724218, EBI-6425205;
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=P11230-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11230-2; Sequence=VSP_056675;
CC -!- DISEASE: Myasthenic syndrome, congenital, 2A, slow-channel (CMS2A)
CC [MIM:616313]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features are easy fatigability and
CC muscle weakness affecting the axial and limb muscles (with hypotonia in
CC early-onset forms), the ocular muscles (leading to ptosis and
CC ophthalmoplegia), and the facial and bulbar musculature (affecting
CC sucking and swallowing, and leading to dysphonia). The symptoms
CC fluctuate and worsen with physical effort. CMS2A is a slow-channel
CC myasthenic syndrome. It is caused by kinetic abnormalities of the AChR,
CC resulting in prolonged AChR channel opening episodes, prolonged
CC endplate currents, and depolarization block. This is associated with
CC calcium overload, which may contribute to subsequent degeneration of
CC the endplate and postsynaptic membrane. {ECO:0000269|PubMed:27375219,
CC ECO:0000269|PubMed:8651643, ECO:0000269|PubMed:8872460}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 2C, associated with
CC acetylcholine receptor deficiency (CMS2C) [MIM:616314]: A form of
CC congenital myasthenic syndrome, a group of disorders characterized by
CC failure of neuromuscular transmission, including pre-synaptic,
CC synaptic, and post-synaptic disorders that are not of autoimmune
CC origin. Clinical features are easy fatigability and muscle weakness
CC affecting the axial and limb muscles (with hypotonia in early-onset
CC forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and
CC the facial and bulbar musculature (affecting sucking and swallowing,
CC and leading to dysphonia). The symptoms fluctuate and worsen with
CC physical effort. CMS2C is an autosomal recessive disorder of
CC postsynaptic neuromuscular transmission, due to deficiency of AChR at
CC the endplate that results in low amplitude of the miniature endplate
CC potential and current. CMS2C is clinically characterized by early-onset
CC muscle weakness with variable severity. {ECO:0000269|PubMed:10562302}.
CC Note=The disease is caused by variants affecting the gene represented
CC 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. Beta-1/CHRNB1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X14830; CAA32939.1; -; mRNA.
DR EMBL; AK298938; BAH12907.1; -; mRNA.
DR EMBL; AC113189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011371; AAH11371.1; -; mRNA.
DR EMBL; BC023553; AAH23553.1; -; mRNA.
DR CCDS; CCDS11106.1; -. [P11230-1]
DR PIR; S04607; S04607.
DR RefSeq; NP_000738.2; NM_000747.2. [P11230-1]
DR AlphaFoldDB; P11230; -.
DR SMR; P11230; -.
DR BioGRID; 107562; 43.
DR ComplexPortal; CPX-2179; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR ComplexPortal; CPX-255; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR IntAct; P11230; 2.
DR STRING; 9606.ENSP00000304290; -.
DR BindingDB; P11230; -.
DR ChEMBL; CHEMBL1907588; -.
DR ChEMBL; CHEMBL3885508; -.
DR ChEMBL; CHEMBL4106145; -.
DR DrugCentral; P11230; -.
DR TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; P11230; 1 site.
DR iPTMnet; P11230; -.
DR PhosphoSitePlus; P11230; -.
DR BioMuta; CHRNB1; -.
DR DMDM; 21903373; -.
DR EPD; P11230; -.
DR jPOST; P11230; -.
DR MassIVE; P11230; -.
DR PaxDb; P11230; -.
DR PeptideAtlas; P11230; -.
DR PRIDE; P11230; -.
DR ProteomicsDB; 52725; -. [P11230-1]
DR ProteomicsDB; 6694; -.
DR Antibodypedia; 992; 267 antibodies from 35 providers.
DR DNASU; 1140; -.
DR Ensembl; ENST00000306071.7; ENSP00000304290.2; ENSG00000170175.11. [P11230-1]
DR Ensembl; ENST00000536404.6; ENSP00000439209.2; ENSG00000170175.11. [P11230-2]
DR Ensembl; ENST00000639692.2; ENSP00000492221.1; ENSG00000283946.2. [P11230-1]
DR Ensembl; ENST00000639993.1; ENSP00000491113.1; ENSG00000283946.2. [P11230-2]
DR GeneID; 1140; -.
DR KEGG; hsa:1140; -.
DR MANE-Select; ENST00000306071.7; ENSP00000304290.2; NM_000747.3; NP_000738.2.
DR UCSC; uc002ghb.4; human. [P11230-1]
DR CTD; 1140; -.
DR DisGeNET; 1140; -.
DR GeneCards; CHRNB1; -.
DR GeneReviews; CHRNB1; -.
DR HGNC; HGNC:1961; CHRNB1.
DR HPA; ENSG00000170175; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; CHRNB1; -.
DR MIM; 100710; gene.
DR MIM; 616313; phenotype.
DR MIM; 616314; phenotype.
DR neXtProt; NX_P11230; -.
DR OpenTargets; ENSG00000170175; -.
DR Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR PharmGKB; PA26494; -.
DR VEuPathDB; HostDB:ENSG00000170175; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158661; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P11230; -.
DR OMA; PCILITV; -.
DR OrthoDB; 776653at2759; -.
DR PhylomeDB; P11230; -.
DR TreeFam; TF315605; -.
DR PathwayCommons; P11230; -.
DR SignaLink; P11230; -.
DR BioGRID-ORCS; 1140; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; CHRNB1; human.
DR GeneWiki; CHRNB1; -.
DR GenomeRNAi; 1140; -.
DR Pharos; P11230; Tclin.
DR PRO; PR:P11230; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P11230; protein.
DR Bgee; ENSG00000170175; Expressed in gastrocnemius and 98 other tissues.
DR ExpressionAtlas; P11230; baseline and differential.
DR Genevisible; P11230; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IMP:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IMP:UniProtKB.
DR GO; GO:0042166; F:acetylcholine binding; ISS:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0015267; F:channel activity; IMP:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
DR GO; GO:0006812; P:cation transport; IMP:UniProtKB.
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:0055001; P:muscle cell development; IMP:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IMP:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR GO; GO:0001941; P:postsynaptic membrane organization; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:UniProtKB.
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 Alternative splicing; Cell membrane; Congenital myasthenic syndrome;
KW Disease variant; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT CHAIN 24..501
FT /note="Acetylcholine receptor subunit beta"
FT /id="PRO_0000000315"
FT TOPO_DOM 24..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 390
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056675"
FT VARIANT 32
FT /note="E -> G (in dbSNP:rs17856697)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048169"
FT VARIANT 124
FT /note="D -> Y (in dbSNP:rs17856698)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_070842"
FT VARIANT 285
FT /note="L -> M (in CMS2A; dbSNP:rs137852811)"
FT /evidence="ECO:0000269|PubMed:8651643"
FT /id="VAR_000287"
FT VARIANT 289
FT /note="V -> A (in CMS2A; slow-channel mutation; increases
FT gating equilibrium constant by 33-fold, owing to increased
FT opening rate and decreased closing rate; no effect on the
FT choline dissociation rate constant)"
FT /evidence="ECO:0000269|PubMed:27375219"
FT /id="VAR_077363"
FT VARIANT 289
FT /note="V -> M (in CMS2A; dbSNP:rs137852810)"
FT /evidence="ECO:0000269|PubMed:8872460"
FT /id="VAR_000288"
FT VARIANT 449..451
FT /note="Missing (in CMS2C; impairs AChR assembly by
FT disrupting a specific interaction between beta and delta
FT subunits)"
FT /evidence="ECO:0000269|PubMed:10562302"
FT /id="VAR_017494"
FT CONFLICT 15
FT /note="A -> P (in Ref. 1; CAA32939)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="I -> N (in Ref. 1; CAA32939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 56698 MW; 365CBFA795A51394 CRC64;
MTPGALLMLL GALGAPLAPG VRGSEAEGRL REKLFSGYDS SVRPAREVGD RVRVSVGLIL
AQLISLNEKD EEMSTKVYLD LEWTDYRLSW DPAEHDGIDS LRITAESVWL PDVVLLNNND
GNFDVALDIS VVVSSDGSVR WQPPGIYRSS CSIQVTYFPF DWQNCTMVFS SYSYDSSEVS
LQTGLGPDGQ GHQEIHIHEG TFIENGQWEI IHKPSRLIQP PGDPRGGREG QRQEVIFYLI
IRRKPLFYLV NVIAPCILIT LLAIFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE
TSLSVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMPLWVRQIF IHKLPLYLRL
KRPKPERDLM PEPPHCSSPG SGWGRGTDEY FIRKPPSDFL FPKPNRFQPE LSAPDLRRFI
DGPNRAVALL PELREVVSSI SYIARQLQEQ EDHDALKEDW QFVAMVVDRL FLWTFIIFTS
VGTLVIFLDA TYHLPPPDPF P
