RAPSN_HUMAN
ID RAPSN_HUMAN Reviewed; 412 AA.
AC Q13702; Q8TDF3; Q9BTD9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=43 kDa receptor-associated protein of the synapse;
DE Short=RAPsyn;
DE AltName: Full=43 kDa postsynaptic protein;
DE AltName: Full=Acetylcholine receptor-associated 43 kDa protein;
DE AltName: Full=RING finger protein 205;
GN Name=RAPSN; Synonyms=RNF205;
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=Muscle;
RX PubMed=8812503; DOI=10.1006/geno.1996.0409;
RA Buckel A., Beeson D., James M., Vincent A.;
RT "Cloning of cDNA encoding human rapsyn and mapping of the RAPSN gene locus
RT to chromosome 11p11.2-p11.1.";
RL Genomics 35:613-616(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS CMS11 PRO-14 AND
RP LYS-88.
RX PubMed=11791205; DOI=10.1086/339465;
RA Ohno K., Engel A.G., Shen X.-M., Selcen D., Brengman J., Harper C.M.,
RA Tsujino A., Milone M.;
RT "Rapsyn mutations in humans cause endplate acetylcholine-receptor
RT deficiency and myasthenic syndrome.";
RL Am. J. Hum. Genet. 70:875-885(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-8.
RC TISSUE=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 UBIQUITINATION BY THE BCR(KLHL8) COMPLEX.
RX PubMed=19158078; DOI=10.1074/jbc.m808230200;
RA Nam S., Min K., Hwang H., Lee H.O., Lee J.H., Yoon J., Lee H., Park S.,
RA Lee J.;
RT "Control of rapsyn stability by the CUL-3-containing E3 ligase complex.";
RL J. Biol. Chem. 284:8195-8206(2009).
RN [6]
RP VARIANTS CMS11 PRO-14 AND LYS-88.
RX PubMed=12730725; DOI=10.1007/s10038-003-0005-7;
RA Dunne V., Maselli R.A.;
RT "Identification of pathogenic mutations in the human rapsyn gene.";
RL J. Hum. Genet. 48:204-207(2003).
RN [7]
RP VARIANTS CMS11 PRO-14 AND LYS-88.
RX PubMed=12929188; DOI=10.1002/mus.10433;
RA Maselli R.A., Dunne V., Pascual-Pascual S.I., Bowe C., Agius M., Frank R.,
RA Wollmann R.L.;
RT "Rapsyn mutations in myasthenic syndrome due to impaired receptor
RT clustering.";
RL Muscle Nerve 28:293-301(2003).
RN [8]
RP VARIANT CMS11 LYS-88.
RX PubMed=12796535; DOI=10.1212/01.wnl.0000072262.14931.80;
RA Mueller J.S., Mildner G., Mueller-Felber W., Schara U., Krampfl K.,
RA Petersen B., Petrova S., Stucka R., Mortier W., Bufler J., Kurlemann G.,
RA Huebner A., Merlini L., Lochmuller H., Abicht A.;
RT "Rapsyn N88K is a frequent cause of congenital myasthenic syndromes in
RT European patients.";
RL Neurology 60:1805-1810(2003).
RN [9]
RP VARIANT CMS11 LYS-88.
RX PubMed=14504330; DOI=10.1212/01.wnl.0000085865.55513.ae;
RA Burke G., Cossins J., Maxwell S., Owens G., Vincent A., Robb S.,
RA Nicolle M., Hilton-Jones D., Newsom-Davis J., Palace J., Beeson D.;
RT "Rapsyn mutations in hereditary myasthenia: distinct early- and late-onset
RT phenotypes.";
RL Neurology 61:826-828(2003).
RN [10]
RP VARIANT CMS11 LYS-88.
RX PubMed=15036330; DOI=10.1016/j.nmd.2003.11.004;
RA Banwell B.L., Ohno K., Sieb J.P., Engel A.G.;
RT "Novel truncating RAPSN mutations causing congenital myasthenic syndrome
RT responsive to 3,4-diaminopyridine.";
RL Neuromuscul. Disord. 14:202-207(2004).
RN [11]
RP VARIANT CMS11 LYS-88.
RX PubMed=15328566; DOI=10.1055/s-2004-820993;
RA Ioos C., Barois A., Richard P., Eymard B., Hantai D.,
RA Estournet-Mathiaud B.;
RT "Congenital myasthenic syndrome due to rapsyn deficiency: three cases with
RT arthrogryposis and bulbar symptoms.";
RL Neuropediatrics 35:246-249(2004).
RN [12]
RP VARIANTS CMS11 CYS-164 AND PRO-283, AND CHARACTERIZATION OF VARIANTS CMS11
RP CYS-164 AND PRO-283.
RX PubMed=16931511; DOI=10.1212/01.wnl.0000233837.79459.40;
RA Mueller J.S., Baumeister S.K., Rasic V.M., Krause S., Todorovic S.,
RA Kugler K., Mueller-Felber W., Abicht A., Lochmueller H.;
RT "Impaired receptor clustering in congenital myasthenic syndrome with novel
RT RAPSN mutations.";
RL Neurology 67:1159-1164(2006).
RN [13]
RP VARIANTS CMS11 MET-45 AND LYS-162, AND CHARACTERIZATION OF VARIANTS CMS11
RP MET-45 AND LYS-162.
RX PubMed=17594401; DOI=10.1111/j.1399-0004.2007.00824.x;
RA Maselli R.A., Dris H., Schnier J., Cockrell J.L., Wollmann R.L.;
RT "Congenital myasthenic syndrome caused by two non-N88K rapsyn mutations.";
RL Clin. Genet. 72:63-65(2007).
RN [14]
RP INVOLVEMENT IN FADS2.
RX PubMed=18179903; DOI=10.1016/j.ajhg.2007.09.016;
RA Vogt J., Harrison B.J., Spearman H., Cossins J., Vermeer S., ten Cate L.N.,
RA Morgan N.V., Beeson D., Maher E.R.;
RT "Mutation analysis of CHRNA1, CHRNB1, CHRND, and RAPSN genes in multiple
RT pterygium syndrome/fetal akinesia patients.";
RL Am. J. Hum. Genet. 82:222-227(2008).
RN [15]
RP VARIANTS FADS2 SER-139 AND VAL-189.
RX PubMed=18252226; DOI=10.1016/j.ajhg.2007.11.006;
RA Michalk A., Stricker S., Becker J., Rupps R., Pantzar T., Miertus J.,
RA Botta G., Naretto V.G., Janetzki C., Yaqoob N., Ott C.-E., Seelow D.,
RA Wieczorek D., Fiebig B., Wirth B., Hoopmann M., Walther M., Koerber F.,
RA Blankenburg M., Mundlos S., Heller R., Hoffmann K.;
RT "Acetylcholine receptor pathway mutations explain various fetal akinesia
RT deformation sequence disorders.";
RL Am. J. Hum. Genet. 82:464-476(2008).
CC -!- FUNCTION: Postsynaptic protein required for clustering of nicotinic
CC acetylcholine receptors (nAChRs) at the neuromuscular junction. It may
CC link the receptor to the underlying postsynaptic cytoskeleton, possibly
CC by direct association with actin or spectrin.
CC -!- INTERACTION:
CC Q13702-2; P54253: ATXN1; NbExp=6; IntAct=EBI-22012855, EBI-930964;
CC Q13702-2; P42858: HTT; NbExp=18; IntAct=EBI-22012855, EBI-466029;
CC Q13702-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-22012855, EBI-748974;
CC Q13702-2; P50454: SERPINH1; NbExp=3; IntAct=EBI-22012855, EBI-350723;
CC Q13702-2; P37840: SNCA; NbExp=3; IntAct=EBI-22012855, EBI-985879;
CC Q13702-2; P37173: TGFBR2; NbExp=3; IntAct=EBI-22012855, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Postsynaptic cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic
CC surface of postsynaptic membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13702-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13702-2; Sequence=VSP_005533;
CC -!- DOMAIN: A cysteine-rich region homologous to part of the regulatory
CC domain of protein kinase C may be important in interactions of this
CC protein with the lipid bilayer.
CC -!- PTM: Ubiquitinated by the BCR(KLHL8) complex, leading to its
CC degradation. {ECO:0000269|PubMed:19158078}.
CC -!- DISEASE: Myasthenic syndrome, congenital, 11, associated with
CC acetylcholine receptor deficiency (CMS11) [MIM:616326]: 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. CMS11 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. {ECO:0000269|PubMed:11791205,
CC ECO:0000269|PubMed:12730725, ECO:0000269|PubMed:12796535,
CC ECO:0000269|PubMed:12929188, ECO:0000269|PubMed:14504330,
CC ECO:0000269|PubMed:15036330, ECO:0000269|PubMed:15328566,
CC ECO:0000269|PubMed:16931511, ECO:0000269|PubMed:17594401}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Fetal akinesia deformation sequence 2 (FADS2) [MIM:618388]: A
CC clinically and genetically heterogeneous group of disorders with
CC congenital malformations related to impaired fetal movement. Clinical
CC features include fetal akinesia, intrauterine growth retardation,
CC polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial
CC abnormalities, and cryptorchidism. FADS2 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:18179903, ECO:0000269|PubMed:18252226}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the RAPsyn family. {ECO:0000305}.
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DR EMBL; Z33905; CAA83954.1; -; mRNA.
DR EMBL; AF449218; AAL86639.1; -; mRNA.
DR EMBL; CH471064; EAW67914.1; -; Genomic_DNA.
DR EMBL; BC004196; AAH04196.1; -; mRNA.
DR CCDS; CCDS7936.1; -. [Q13702-1]
DR CCDS; CCDS7937.1; -. [Q13702-2]
DR PIR; S45064; S45064.
DR RefSeq; NP_005046.2; NM_005055.4. [Q13702-1]
DR RefSeq; NP_116034.2; NM_032645.4. [Q13702-2]
DR AlphaFoldDB; Q13702; -.
DR SMR; Q13702; -.
DR BioGRID; 111848; 20.
DR IntAct; Q13702; 10.
DR STRING; 9606.ENSP00000298854; -.
DR ChEMBL; CHEMBL2163166; -.
DR iPTMnet; Q13702; -.
DR PhosphoSitePlus; Q13702; -.
DR BioMuta; RAPSN; -.
DR DMDM; 145559521; -.
DR PaxDb; Q13702; -.
DR PeptideAtlas; Q13702; -.
DR PRIDE; Q13702; -.
DR ProteomicsDB; 59664; -. [Q13702-1]
DR ProteomicsDB; 59665; -. [Q13702-2]
DR Antibodypedia; 13774; 175 antibodies from 34 providers.
DR DNASU; 5913; -.
DR Ensembl; ENST00000298854.7; ENSP00000298854.2; ENSG00000165917.10. [Q13702-1]
DR Ensembl; ENST00000352508.7; ENSP00000298853.3; ENSG00000165917.10. [Q13702-2]
DR GeneID; 5913; -.
DR KEGG; hsa:5913; -.
DR MANE-Select; ENST00000298854.7; ENSP00000298854.2; NM_005055.5; NP_005046.2.
DR UCSC; uc001nfi.2; human. [Q13702-1]
DR CTD; 5913; -.
DR DisGeNET; 5913; -.
DR GeneCards; RAPSN; -.
DR GeneReviews; RAPSN; -.
DR HGNC; HGNC:9863; RAPSN.
DR HPA; ENSG00000165917; Group enriched (skeletal muscle, tongue).
DR MalaCards; RAPSN; -.
DR MIM; 601592; gene.
DR MIM; 616326; phenotype.
DR MIM; 618388; phenotype.
DR neXtProt; NX_Q13702; -.
DR OpenTargets; ENSG00000165917; -.
DR Orphanet; 994; Fetal akinesia deformation sequence.
DR Orphanet; 33108; Lethal multiple pterygium syndrome.
DR Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR PharmGKB; PA34224; -.
DR VEuPathDB; HostDB:ENSG00000165917; -.
DR eggNOG; KOG1941; Eukaryota.
DR GeneTree; ENSGT00390000016785; -.
DR HOGENOM; CLU_030911_0_0_1; -.
DR InParanoid; Q13702; -.
DR OMA; ALRCSHI; -.
DR OrthoDB; 396881at2759; -.
DR PhylomeDB; Q13702; -.
DR TreeFam; TF328344; -.
DR PathwayCommons; Q13702; -.
DR SignaLink; Q13702; -.
DR BioGRID-ORCS; 5913; 16 hits in 1111 CRISPR screens.
DR GeneWiki; RAPSN; -.
DR GenomeRNAi; 5913; -.
DR Pharos; Q13702; Tbio.
DR PRO; PR:Q13702; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13702; protein.
DR Bgee; ENSG00000165917; Expressed in hindlimb stylopod muscle and 97 other tissues.
DR ExpressionAtlas; Q13702; baseline and differential.
DR Genevisible; Q13702; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:1903540; P:establishment of protein localization to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2000673; P:positive regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:1901626; P:regulation of postsynaptic membrane organization; IEA:Ensembl.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IGI:MGI.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001237; Postsynaptic.
DR InterPro; IPR018293; Postsynaptic_CS.
DR InterPro; IPR019568; Rapsyn_myristoylation/link_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR041617; TPR_MalT.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF10579; Rapsyn_N; 1.
DR Pfam; PF17874; TPR_MalT; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR PRINTS; PR00217; POSTSYNAPTIC.
DR SMART; SM00184; RING; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS00405; 43_KD_POSTSYNAPTIC; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Congenital myasthenic syndrome;
KW Cytoplasm; Cytoskeleton; Disease variant; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Synapse; TPR repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..412
FT /note="43 kDa receptor-associated protein of the synapse"
FT /id="PRO_0000167591"
FT REPEAT 6..39
FT /note="TPR 1"
FT REPEAT 83..116
FT /note="TPR 2"
FT REPEAT 123..156
FT /note="TPR 3"
FT REPEAT 163..196
FT /note="TPR 4"
FT REPEAT 206..239
FT /note="TPR 5"
FT REPEAT 246..279
FT /note="TPR 6"
FT REPEAT 286..319
FT /note="TPR 7"
FT ZN_FING 363..403
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 264..322
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005533"
FT VARIANT 8
FT /note="Q -> K (in dbSNP:rs11556408)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_043897"
FT VARIANT 14
FT /note="L -> P (in CMS11; dbSNP:rs104894300)"
FT /evidence="ECO:0000269|PubMed:11791205,
FT ECO:0000269|PubMed:12730725, ECO:0000269|PubMed:12929188"
FT /id="VAR_021216"
FT VARIANT 45
FT /note="V -> M (in CMS11; reduced coclustering with
FT acetylcholine receptor; dbSNP:rs121909254)"
FT /evidence="ECO:0000269|PubMed:17594401"
FT /id="VAR_043898"
FT VARIANT 81
FT /note="F -> L (in dbSNP:rs57878668)"
FT /id="VAR_062142"
FT VARIANT 88
FT /note="N -> K (in CMS11; dbSNP:rs104894299)"
FT /evidence="ECO:0000269|PubMed:11791205,
FT ECO:0000269|PubMed:12730725, ECO:0000269|PubMed:12796535,
FT ECO:0000269|PubMed:12929188, ECO:0000269|PubMed:14504330,
FT ECO:0000269|PubMed:15036330, ECO:0000269|PubMed:15328566"
FT /id="VAR_021217"
FT VARIANT 139
FT /note="F -> S (in FADS2; dbSNP:rs121909256)"
FT /evidence="ECO:0000269|PubMed:18252226"
FT /id="VAR_043899"
FT VARIANT 162
FT /note="E -> K (in CMS11; reduced coclustering with
FT acetylcholine receptor; dbSNP:rs121909255)"
FT /evidence="ECO:0000269|PubMed:17594401"
FT /id="VAR_043900"
FT VARIANT 164
FT /note="R -> C (in CMS11; reduced coclustering with
FT acetylcholine receptor; dbSNP:rs104894294)"
FT /evidence="ECO:0000269|PubMed:16931511"
FT /id="VAR_043901"
FT VARIANT 189
FT /note="A -> V (in FADS2; dbSNP:rs121909257)"
FT /evidence="ECO:0000269|PubMed:18252226"
FT /id="VAR_043902"
FT VARIANT 283
FT /note="L -> P (in CMS11; reduced coclustering with
FT acetylcholine receptor; dbSNP:rs104894293)"
FT /evidence="ECO:0000269|PubMed:16931511"
FT /id="VAR_043903"
FT CONFLICT 112
FT /note="L -> V (in Ref. 1; CAA83954)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> T (in Ref. 1; CAA83954)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="R -> Q (in Ref. 1; CAA83954)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="G -> A (in Ref. 1; CAA83954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46328 MW; D17AC566700F5AAF CRC64;
MGQDQTKQQI EKGLQLYQSN QTEKALQVWT KVLEKSSDLM GRFRVLGCLV TAHSEMGRYK
EMLKFAVVQI DTARELEDAD FLLESYLNLA RSNEKLCEFH KTISYCKTCL GLPGTRAGAQ
LGGQVSLSMG NAFLGLSVFQ KALESFEKAL RYAHNNDDAM LECRVCCSLG SFYAQVKDYE
KALFFPCKAA ELVNNYGKGW SLKYRAMSQY HMAVAYRLLG RLGSAMECCE ESMKIALQHG
DRPLQALCLL CFADIHRSRG DLETAFPRYD SAMSIMTEIG NRLGQVQALL GVAKCWVARK
ALDKALDAIE RAQDLAEEVG NKLSQLKLHC LSESIYRSKG LQRELRAHVV RFHECVEETE
LYCGLCGESI GEKNSRLQAL PCSHIFHLRC LQNNGTRSCP NCRRSSMKPG FV
