SPTN4_HUMAN
ID SPTN4_HUMAN Reviewed; 2564 AA.
AC Q9H254; E9PGQ5; Q9H1K7; Q9H1K8; Q9H1K9; Q9H253; Q9H3G8; Q9HCD0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Spectrin beta chain, non-erythrocytic 4;
DE AltName: Full=Beta-IV spectrin;
DE AltName: Full=Spectrin, non-erythroid beta chain 3;
GN Name=SPTBN4; Synonyms=KIAA1642, SPTBN3;
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] (ISOFORMS 1 AND 5), AND VARIANT SER-1331.
RX PubMed=11294830; DOI=10.1074/jbc.m009307200;
RA Tse W.T., Tang J., Jin O., Korsgren C., John K.M., Kung A.L., Gwynn B.,
RA Peters L.L., Lux S.E.;
RT "A new spectrin, beta-IV, has a major truncated isoform that associates
RT with promyelocytic leukemia protein nuclear bodies and the nuclear
RT matrix.";
RL J. Biol. Chem. 276:23974-23985(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=11086001; DOI=10.1083/jcb.151.5.985;
RA Berghs S., Aggujaro D., Dirkx R. Jr., Maksimova E., Stabach P.,
RA Hermel J.-M., Zhang J.-P., Philbrick W., Slepnev V., Ort T., Solimena M.;
RT "BetaIV spectrin, a new spectrin localized at axon initial segments and
RT nodes of Ranvier in the central and peripheral nervous system.";
RL J. Cell Biol. 151:985-1002(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 386-2382 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP INVOLVEMENT IN NEDHND, TISSUE SPECIFICITY, AND VARIANT NEDHND
RP 533-GLN--LYS-2564.
RX PubMed=28540413; DOI=10.1007/s00439-017-1814-7;
RA Knierim E., Gill E., Seifert F., Morales-Gonzalez S., Unudurthi S.D.,
RA Hund T.J., Stenzel W., Schuelke M.;
RT "A recessive mutation in beta-IV-spectrin (SPTBN4) associates with
RT congenital myopathy, neuropathy, and central deafness.";
RL Hum. Genet. 136:903-910(2017).
CC -!- INTERACTION:
CC Q9H254; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-308543, EBI-529989;
CC Q9H254; Q16849: PTPRN; NbExp=2; IntAct=EBI-308543, EBI-728153;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cell cortex {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H254-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H254-2; Sequence=VSP_000725, VSP_000726;
CC Name=3;
CC IsoId=Q9H254-3; Sequence=VSP_000723, VSP_000724;
CC Name=4;
CC IsoId=Q9H254-4; Sequence=VSP_000727, VSP_000728;
CC Name=5;
CC IsoId=Q9H254-5; Sequence=VSP_046383, VSP_046384, VSP_046385;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle at the sarcolemma and
CC in the muscle capillaries (at protein level) (PubMed:28540413).
CC Abundantly expressed in brain and pancreatic islets (PubMed:11086001).
CC {ECO:0000269|PubMed:11086001, ECO:0000269|PubMed:28540413}.
CC -!- DISEASE: Neurodevelopmental disorder with hypotonia, neuropathy, and
CC deafness (NEDHND) [MIM:617519]: An autosomal recessive disorder
CC characterized by congenital myopathy with hypotonia and muscle weakness
CC manifesting after birth and progressing to generalized muscle atrophy,
CC central deafness with absent brainstem-evoked potentials, and a
CC combined axonal and demyelinating motor neuropathy.
CC {ECO:0000269|PubMed:28540413}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
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DR EMBL; AF311855; AAG42473.1; -; mRNA.
DR EMBL; AF311856; AAG42474.1; -; mRNA.
DR EMBL; AF082075; AAG38874.1; -; mRNA.
DR EMBL; AY004226; AAF93171.1; -; mRNA.
DR EMBL; AY004226; AAF93172.1; -; mRNA.
DR EMBL; AY004227; AAF93173.1; -; mRNA.
DR EMBL; AC020929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB046862; BAB13468.1; -; mRNA.
DR CCDS; CCDS12559.1; -. [Q9H254-1]
DR CCDS; CCDS42569.1; -. [Q9H254-5]
DR RefSeq; NP_066022.2; NM_020971.2. [Q9H254-1]
DR RefSeq; NP_079489.2; NM_025213.2. [Q9H254-5]
DR RefSeq; XP_016882538.1; XM_017027049.1. [Q9H254-1]
DR AlphaFoldDB; Q9H254; -.
DR SMR; Q9H254; -.
DR BioGRID; 121751; 55.
DR IntAct; Q9H254; 22.
DR MINT; Q9H254; -.
DR STRING; 9606.ENSP00000263373; -.
DR GlyGen; Q9H254; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H254; -.
DR PhosphoSitePlus; Q9H254; -.
DR BioMuta; SPTBN4; -.
DR DMDM; 17368942; -.
DR EPD; Q9H254; -.
DR jPOST; Q9H254; -.
DR MassIVE; Q9H254; -.
DR MaxQB; Q9H254; -.
DR PaxDb; Q9H254; -.
DR PeptideAtlas; Q9H254; -.
DR PRIDE; Q9H254; -.
DR ProteomicsDB; 20368; -.
DR ProteomicsDB; 80498; -. [Q9H254-1]
DR ProteomicsDB; 80499; -. [Q9H254-2]
DR ProteomicsDB; 80500; -. [Q9H254-3]
DR ProteomicsDB; 80501; -. [Q9H254-4]
DR ABCD; Q9H254; 2 sequenced antibodies.
DR Antibodypedia; 48036; 177 antibodies from 22 providers.
DR DNASU; 57731; -.
DR Ensembl; ENST00000352632.7; ENSP00000263373.2; ENSG00000160460.17. [Q9H254-1]
DR Ensembl; ENST00000392023.1; ENSP00000375877.1; ENSG00000160460.17. [Q9H254-5]
DR Ensembl; ENST00000598249.6; ENSP00000469242.1; ENSG00000160460.17. [Q9H254-1]
DR GeneID; 57731; -.
DR KEGG; hsa:57731; -.
DR MANE-Select; ENST00000598249.6; ENSP00000469242.1; NM_020971.3; NP_066022.2.
DR UCSC; uc002ony.4; human. [Q9H254-1]
DR CTD; 57731; -.
DR DisGeNET; 57731; -.
DR GeneCards; SPTBN4; -.
DR GeneReviews; SPTBN4; -.
DR HGNC; HGNC:14896; SPTBN4.
DR HPA; ENSG00000160460; Group enriched (brain, pituitary gland).
DR MalaCards; SPTBN4; -.
DR MIM; 606214; gene.
DR MIM; 617519; phenotype.
DR neXtProt; NX_Q9H254; -.
DR OpenTargets; ENSG00000160460; -.
DR PharmGKB; PA37918; -.
DR VEuPathDB; HostDB:ENSG00000160460; -.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000156343; -.
DR HOGENOM; CLU_000146_0_1_1; -.
DR InParanoid; Q9H254; -.
DR OMA; SPECGQH; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; Q9H254; -.
DR TreeFam; TF313446; -.
DR PathwayCommons; Q9H254; -.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; Q9H254; -.
DR BioGRID-ORCS; 57731; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; SPTBN4; human.
DR GeneWiki; SPTBN4; -.
DR GenomeRNAi; 57731; -.
DR Pharos; Q9H254; Tbio.
DR PRO; PR:Q9H254; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H254; protein.
DR Bgee; ENSG00000160460; Expressed in right hemisphere of cerebellum and 151 other tissues.
DR ExpressionAtlas; Q9H254; baseline and differential.
DR Genevisible; Q9H254; HS.
DR GO; GO:0005884; C:actin filament; ISS:ARUK-UCL.
DR GO; GO:0043203; C:axon hillock; ISS:BHF-UCL.
DR GO; GO:0043194; C:axon initial segment; ISS:ARUK-UCL.
DR GO; GO:0070852; C:cell body fiber; ISS:BHF-UCL.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0008091; C:spectrin; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; IDA:UniProtKB.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; TAS:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; ISS:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007628; P:adult walking behavior; ISS:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; ISS:BHF-UCL.
DR GO; GO:0061337; P:cardiac conduction; ISS:BHF-UCL.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISS:BHF-UCL.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISS:BHF-UCL.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0010459; P:negative regulation of heart rate; ISS:BHF-UCL.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; ISS:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0007605; P:sensory perception of sound; ISS:BHF-UCL.
DR GO; GO:0019226; P:transmission of nerve impulse; ISS:BHF-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 7.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00435; Spectrin; 14.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00033; CH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00150; SPEC; 16.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Alternative splicing; Cytoplasm;
KW Cytoskeleton; Deafness; Disease variant; Neuropathy; Reference proteome;
KW Repeat.
FT CHAIN 1..2564
FT /note="Spectrin beta chain, non-erythrocytic 4"
FT /id="PRO_0000073465"
FT DOMAIN 61..165
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 180..285
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 311..418
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 430..533
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 536..641
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 774..879
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 884..982
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 1089..1196
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 1306..1407
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1412..1512
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1515..1617
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1623..1725
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1728..1830
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1835..1935
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1944..2046
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 2049..2123
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT DOMAIN 2418..2527
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..282
FT /note="Actin-binding"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2208..2439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2533..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2228..2314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2422..2436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1324
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11294830"
FT /id="VSP_046383"
FT VAR_SEQ 1..1257
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11086001"
FT /id="VSP_000723"
FT VAR_SEQ 1258..1286
FT /note="AVQAAEGLLRQGNIYGEQAQEAVTRLLEK -> MPHYPSCSSAPSLGTPIPP
FT QIQQLEARHR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11086001"
FT /id="VSP_000724"
FT VAR_SEQ 1287..1309
FT /note="NQENQLRAQQWMQKLHDQLELQH -> CLIIHPALLHPPWEPPYLPRSSS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11086001"
FT /id="VSP_000725"
FT VAR_SEQ 1310..2564
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11086001"
FT /id="VSP_000726"
FT VAR_SEQ 1973..2002
FT /note="DVSSVEVLMNYHQGLKTELEARVPELTTCQ -> CPSSLLGLPASPWWPTPA
FT TPSPLTAPFSME (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11294830"
FT /id="VSP_046384"
FT VAR_SEQ 2003..2564
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11294830"
FT /id="VSP_046385"
FT VAR_SEQ 2113..2154
FT /note="IEKIKAEQSKQPPTPLLGRKFFGDPTELAAKAAPLLRPGGYE -> PRREDH
FT LNPGVQDQPWQHTEKPSLPKPKANKEKTARRDGTCL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11086001"
FT /id="VSP_000727"
FT VAR_SEQ 2155..2564
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11086001"
FT /id="VSP_000728"
FT VARIANT 533..2564
FT /note="Missing (in NEDHND; decreased protein abundance in
FT patient cells homozygous for the mutation)"
FT /evidence="ECO:0000269|PubMed:28540413"
FT /id="VAR_079212"
FT VARIANT 1331
FT /note="G -> S (in dbSNP:rs814501)"
FT /evidence="ECO:0000269|PubMed:11294830"
FT /id="VAR_048632"
FT CONFLICT 604..608
FT /note="Missing (in Ref. 2; AAG38874/AAF93171)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="L -> S (in Ref. 2; AAG38874/AAF93171/AAF93173)"
FT /evidence="ECO:0000305"
FT CONFLICT 1189
FT /note="E -> K (in Ref. 2; AAG38874/AAF93171/AAF93173)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="E -> K (in Ref. 2; AAG38874/AAF93171/AAF93173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2564 AA; 288985 MW; 52CDE7D11D601ECC CRC64;
MAQVPGEVDN MEGLPAPNNN PAARWESPDR GWEREQPAAS TAAASLFECS RIKALADERE
AVQKKTFTKW VNSHLARVGC HIGDLYVDLR DGFVLTRLLE VLSGEQLPRP TRGRMRIHSL
ENVDKALQFL KEQRVHLENV GSHDIVDGNH RLTLGLVWTI ILRFQIQVIK IETEDNRETR
SAKDALLLWC QMKTAGYPEV NIQNFTTSWR DGLAFNALIH RHRPDLVDFS KLTKSNANYN
LQRAFRTAEQ HLGLARLLDP EDVNMEAPDE KSIITYVVSF YHYFSKMKAL AVEGKRIGKV
LDQVLEVGKI IERYEELAAE LLAWIHRTVG LISNQKFANS LSGVQQQLQA FTAYCTLEKP
VKFQEKGNLE VLLFSIQSKL RACNRRLFVP REGCGIWDID KAWGELEKAE HEREAALRAE
LIRQEKLELL AQRFDHKVAM RESWLNENQR LVSQDNFGYE LPAVEAAMKK HEAIEADIAA
YEERVQGVAE LAQALAAEGY YDIRRVAAQR DSVLRQWALL TGLVGARRTR LEQNLALQKV
FQEMVYMVDW MEEMQAQLLS RECGQHLVEA DDLLQKHGLL EGDIAAQSER VEALNAAALR
FSQLQGYQPC DPQVICNRVN HVHGCLAELQ EQAARRRAEL EASRSLWALL QELEEAESWA
RDKERLLEAA GGGGAAGAAG AAGTAGGAHD LSSTARLLAQ HKILQGELGG RRALLQQALR
CGEELVAAGG AVGPGADTVH LVGLAERAAS ARRRWQRLEE AAARRERRLQ EARALHQFGA
DLDGLLDWLR DAYRLAAAGD FGHDEASSRR LARQHRALTG EVEAHRGPVS GLRRQLATLG
GASGAGPLVV ALQVRVVEAE QLFAEVTEVA ALRRQWLRDA LAVYRMFGEV HACELWIGEK
EQWLLSMRVP DSLDDVEVVQ HRFESLDQEM NSLMGRVLDV NHTVQELVEG GHPSSDEVRS
CQDHLNSRWN RIVELVEQRK EEMSAVLLVE NHVLEVAEVR AQVREKRRAV ESAPRAGGAL
QWRLSGLEAA LQALEPRQAA LLEEAALLAE RFPAQAARLH QGAEELGAEW GALASAAQAC
GEAVAAAGRL QRFLHDLDAF LDWLVRAQEA AGGSEGPLPN SLEEADALLA RHAALKEEVD
QREEDYARIV AASEALLAAD GAELGPGLAL DEWLPHLELG WHKLLGLWEA RREALVQAHI
YQLFLRDLRQ ALVVLRNQEM ALSGAELPGT VESVEEALKQ HRDFLTTMEL SQQKMQVAVQ
AAEGLLRQGN IYGEQAQEAV TRLLEKNQEN QLRAQQWMQK LHDQLELQHF LRDCHELDGW
IHEKMLMARD GTREDNHKLH KRWLRHQAFM AELAQNKEWL EKIEREGQQL MQEKPELAAS
VRKKLGEIRQ CWAELESTTQ AKARQLFEAS KADQLVQSFA ELDKKLLHME SQLQDVDPGG
DLATVNSQLK KLQSMESQVE EWYREVGELQ AQTAALPLEP ASKELVGERQ NAVGERLVRL
LEPLQERRRL LLASKELHQV AHDLDDELAW VQERLPLAMQ TERGNGLQAV QQHIKKNQGL
RREIQAHGPR LEEVLERAGA LASLRSPEAE AVRRGLEQLQ SAWAGLREAA ERRQQVLDAA
FQVEQYYFDV AEVEAWLGEQ ELLMMSEDKG KDEQSTLQLL KKHLQLEQGV ENYEESIAQL
SRQCRALLEM GHPDSEQISR RQSQVDRLYV ALKELGEERR VALEQQYWLY QLSRQVSELE
HWIAEKEVVA GSPELGQDFE HVSVLQEKFS EFASETGMAG RERLAAVNQM VDELIECGHT
AAATMAEWKD GLNEAWAELL ELMGTRAQLL AASRELHKFF SDARELQGQI EEKRRRLPRL
TTPPEPRPSA SSMQRTLRAF EHDLQLLVSQ VRQLQEGAAQ LRTVYAGEHA EAIASREQEV
LQGWKELLSA CEDARLHVSS TADALRFHSQ VRDLLSWMDG IASQIGAADK PRDVSSVEVL
MNYHQGLKTE LEARVPELTT CQELGRSLLL NKSAMADEIQ AQLDKLGTRK EEVSEKWDRH
WEWLQQMLEV HQFAQEAVVA DAWLTAQEPL LQSRELGSSV DEVEQLIRRH EAFRKAAAAW
EERFSSLRRL TTIEKIKAEQ SKQPPTPLLG RKFFGDPTEL AAKAAPLLRP GGYERGLEPL
ARRASDTLSA EVRTRVGYVR QELKPERLQP RIDRLPEIPG RVEPAALPAA PEDAAETPAT
PAAAEQVRPR PERQESADRA EELPRRRRPE RQESVDQSEE AARRRRPERQ ESAEHEAAHS
LTLGRYEQME RRRERRERRL ERQESSEQEM PIRGDLVKGK ATLADIVEQL QEKEAGPGLP
AGPSLPQPRE LPPGRLPNGL ELPERTPRPD RPRARDRPKP RRRPRPREGG EGGGSRRSRS
APAQGGSAPA PPPPPTHTVQ HEGFLLRKRE LDANRKSSNR SWVSLYCVLS KGELGFYKDS
KGPASGSTHG GEPLLSLHKA TSEVASDYKK KKHVFKLQTQ DGSEFLLQAK DEEEMNGWLE
AVASSVAEHA EIARWGQTLP TTSSTDEGNP KREGGDRRAS GRRK
