NFAC4_RAT
ID NFAC4_RAT Reviewed; 901 AA.
AC D3Z9H7; A0A0G2K0L1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 4;
DE Short=NF-ATc4;
DE Short=NFATc4;
DE AltName: Full=T-cell transcription factor NFAT3;
DE Short=NF-AT3 {ECO:0000303|PubMed:9568714};
GN Name=Nfatc4; Synonyms=Nfat3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=9568714; DOI=10.1016/s0092-8674(00)81573-1;
RA Molkentin J.D., Lu J.-R., Antos C.L., Markham B., Richardson J.,
RA Robbins J., Grant S.R., Olson E.N.;
RT "A calcineurin-dependent transcriptional pathway for cardiac hypertrophy.";
RL Cell 93:215-228(1998).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12370307; DOI=10.1128/mcb.22.21.7603-7613.2002;
RA Wilkins B.J., De Windt L.J., Bueno O.F., Braz J.C., Glascock B.J.,
RA Kimball T.F., Molkentin J.D.;
RT "Targeted disruption of NFATc3, but not NFATc4, reveals an intrinsic defect
RT in calcineurin-mediated cardiac hypertrophic growth.";
RL Mol. Cell. Biol. 22:7603-7613(2002).
RN [5]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=19026640; DOI=10.1016/j.febslet.2008.11.009;
RA Fan Y., Xie P., Zhang T., Zhang H., Gu D., She M., Li H.;
RT "Regulation of the stability and transcriptional activity of NFATc4 by
RT ubiquitination.";
RL FEBS Lett. 582:4008-4014(2008).
CC -!- FUNCTION: Ca(2+)-regulated transcription factor that is involved in
CC several processes, including the development and function of the
CC immune, cardiovascular, musculoskeletal, and nervous systems. Involved
CC in T-cell activation, stimulating the transcription of cytokine genes,
CC including that of IL2 and IL4 (PubMed:12370307). Along with NFATC3,
CC involved in embryonic heart development. Involved in mitochondrial
CC energy metabolism required for cardiac morphogenesis and function.
CC Transactivates many genes involved in heart physiology. Along with
CC GATA4, binds to and activates NPPB/BNP promoter (PubMed:9568714).
CC Activates NPPA/ANP/ANF and MYH7/beta-MHC transcription
CC (PubMed:19026640). Binds to and transactivates AGTR2 gene promoter.
CC Involved in the regulation of adult hippocampal neurogenesis. Involved
CC in BDNF-driven pro-survival signaling in hippocampal adult-born
CC neurons. Involved in the formation of long-term spatial memory and
CC long-term potentiation. In cochlear nucleus neurons, may play a role in
CC deafferentation-induced apoptosis during a developmental critical
CC period when auditory neurons depend on afferent input for survival (By
CC similarity). Binds to and activates the BACE1/Beta-secretase 1
CC promoter, hence may regulate the proteolytic processing of the amyloid
CC precursor protein (APP). Plays a role in adipocyte differentiation. May
CC be involved in myoblast differentiation into myotubes (By similarity).
CC Binds the consensus DNA sequence 5'-GGAAAAT-3' (By similarity). In the
CC presence of CREBBP, activates TNF transcription. Binds to PPARG gene
CC promoter and regulates its activity (By similarity). Binds to PPARG and
CC REG3G gene promoters (By similarity). {ECO:0000250|UniProtKB:Q14934,
CC ECO:0000250|UniProtKB:Q8K120, ECO:0000269|PubMed:12370307,
CC ECO:0000269|PubMed:19026640, ECO:0000269|PubMed:9568714}.
CC -!- SUBUNIT: Member of the multicomponent NFATC transcription complex that
CC consists of at least two components, a pre-existing cytoplasmic
CC component NFATC2 and an inducible nuclear component NFATC1. Other NFAT
CC proteins, such as NFATC4, NFATC3, or members of the activating protein-
CC 1 (AP-1) family and MAF can also bind the complex. NFAT proteins can
CC bind DNA as monomers or dimers. Interacts with CREBBP; this interaction
CC potentiates transcription activation (By similarity). Interacts with
CC MAPK8/JNK1 and MAPK9/JNK2 (By similarity). Interacts with GATA4 (via
CC the second Zn finger) (By similarity). Interacts (via N-terminus) with
CC IRAK1 (via C-terminus). Interacts with RPS6KA3. Interacts with HOMER1,
CC HOMER2 and HOMER3; this interaction competes with calcineurin/PPP3CA-
CC binding and hence prevents NFATC4 dephosphorylation and activation (By
CC similarity). Interacts with ESR1 and ESR2; this interaction decreases
CC NFATC4 transcriptional activity. Interacts with MTOR and MAPK7/ERK5 (By
CC similarity). Interacts with TRIM17; this interaction prevents NFATC3
CC nuclear localization (By similarity). {ECO:0000250|UniProtKB:Q14934,
CC ECO:0000250|UniProtKB:Q8K120}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K120}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K120}. Note=When hyperphosphorylated,
CC localizes in the cytosol. When intracellular Ca(2+) levels increase,
CC dephosphorylation by calcineurin/PPP3CA leads to translocation into the
CC nucleus. MAPK7/ERK5 and MTOR regulate NFATC4 nuclear export through
CC phosphorylation at Ser-168 and Ser-170. {ECO:0000250|UniProtKB:Q14934}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D3Z9H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D3Z9H7-2; Sequence=VSP_060060, VSP_060061;
CC -!- TISSUE SPECIFICITY: Expressed in heart (at protein level).
CC {ECO:0000269|PubMed:12370307}.
CC -!- DOMAIN: Rel similarity domain (RSD) or Rel homology domain (RHD) allows
CC DNA-binding and cooperative interactions with AP-1 factors.
CC {ECO:0000250|UniProtKB:O95644}.
CC -!- PTM: Phosphorylated by NFATC-kinases; dephosphorylated by
CC calcineurin/PPP3CA. Phosphorylated on Ser-168 and Ser-170 by MTOR,
CC IRAK1, MAPK7/ERK5 and MAPK14/p38, on Ser-213 and Ser-217 by MAPK8 and
CC MAPK9, and on Ser-289 and Ser-344 by RPS6KA3 (By similarity).
CC Phosphorylated by GSK3B; this phosphorylation markedly increases NFATC4
CC ubiquitination (PubMed:19026640). Phosphorylation by MAPK8/JNK1,
CC MAPK9/JNK2 and RPS6KA3 may stimulate NFATC4 transcriptional activity.
CC Phosphorylation at Ser-168 and Ser-170 is stimulated by UV irradiation
CC (By similarity). {ECO:0000250|UniProtKB:Q14934,
CC ECO:0000250|UniProtKB:Q8K120, ECO:0000269|PubMed:19026640}.
CC -!- PTM: Ubiquitinated, leading to degradation by the proteasome.
CC Ubiquitination may be stimulated by GSK3B-dependent phosphorylation.
CC Polyubiquitin linkage mainly occurs through 'Lys-48'.
CC {ECO:0000269|PubMed:19026640}.
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DR EMBL; AC116083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474049; EDM14287.1; -; Genomic_DNA.
DR RefSeq; NP_001100734.1; NM_001107264.1. [D3Z9H7-1]
DR AlphaFoldDB; D3Z9H7; -.
DR SMR; D3Z9H7; -.
DR STRING; 10116.ENSRNOP00000027789; -.
DR iPTMnet; D3Z9H7; -.
DR PhosphoSitePlus; D3Z9H7; -.
DR PaxDb; D3Z9H7; -.
DR PeptideAtlas; D3Z9H7; -.
DR Ensembl; ENSRNOT00000027789; ENSRNOP00000027789; ENSRNOG00000020482. [D3Z9H7-1]
DR Ensembl; ENSRNOT00000089584; ENSRNOP00000071490; ENSRNOG00000020482. [D3Z9H7-2]
DR GeneID; 305897; -.
DR KEGG; rno:305897; -.
DR CTD; 4776; -.
DR RGD; 1310749; Nfatc4.
DR eggNOG; ENOG502RIHQ; Eukaryota.
DR GeneTree; ENSGT00940000160923; -.
DR HOGENOM; CLU_010185_2_0_1; -.
DR InParanoid; D3Z9H7; -.
DR OMA; PTEGYNE; -.
DR OrthoDB; 95502at2759; -.
DR TreeFam; TF326480; -.
DR PRO; PR:D3Z9H7; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000020482; Expressed in pancreas and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:0045333; P:cellular respiration; ISO:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; ISO:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0035562; P:negative regulation of chromatin binding; ISO:RGD.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:2000297; P:negative regulation of synapse maturation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR12533; PTHR12533; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR01789; NUCFACTORATC.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..901
FT /note="Nuclear factor of activated T-cells, cytoplasmic 4"
FT /id="PRO_0000446288"
FT REPEAT 213..229
FT /note="SP 1"
FT /evidence="ECO:0000255"
FT REPEAT 277..293
FT /note="SP 2; approximate"
FT /evidence="ECO:0000255"
FT DOMAIN 401..582
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT DOMAIN 586..683
FT /note="IPT/TIG"
FT /evidence="ECO:0000255"
FT DNA_BIND 430..437
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..119
FT /note="Calcineurin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT REGION 203..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..293
FT /note="2 approximate SP repeats"
FT /evidence="ECO:0000255"
FT REGION 697..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 268..270
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 672..674
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 57..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K120"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K120"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K120"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14934"
FT VAR_SEQ 880..890
FT /note="VSEIIGRDLSG -> GGCGTGGCECE (in isoform 2)"
FT /id="VSP_060060"
FT VAR_SEQ 891..901
FT /note="Missing (in isoform 2)"
FT /id="VSP_060061"
SQ SEQUENCE 901 AA; 95764 MW; 97EBE1022C88D2A5 CRC64;
MGAASCEDEE LEFKLVFGEE KEAPPLGPGG PGEELDSEDA PPCCRLALGE PLPYGAAPIG
IPRPPPPRPG MHSPPPRPAP SPGTWESQPP RSVRLGGPGG TAGGTGGGRV LECPSIRITS
ISPTPDPPTS LEDAPETWGD GSPRDYPPPE GFGGYREAGG QGGGAFFSPS PGSSSLSSWS
FFSDASDEAA LYAACDEVES ELNEAASRFG LSSPLPSPRA SPRPWTPEDP WSLYGPSSGG
RAPEDSWLLL SAPGPIPASP RPASPCGKRR YSSSGTPSSA SPALSRRGSL GEEGPEPPPP
PPLPLVRDPS SSGPFDYVGA PPTESVPQKT RRTSSEQAVA LPRSEEPASC NGKLPSGTED
SVAAPGALRK EMAGMDYLAV PSPLAWSKAR IGGHSPIFRT SALPPLDWPL PSQYEQLELR
IEVQPRAHHR AHYETEGSRG AVKAAPGGHP VVKLLGYNEK PLTLQMFIGT ADERSLRPHA
FYQVHRITGK MVATASYEAV VSGTKVLEMT LLPENNMAAN IDCAGILKLR NSDIELRKGE
TDIGRKNTRV RLVFRVHVPQ GGGKVVSVQA ASVPIECSQR SAQELPQVEA YSPSACSVRG
GEELVLTGSN FLPDSKVVFI ERGPDGKLQW EEEAAVNRLQ SSEVTLTLTI PEYSNKRVSR
PVQVYFYVSN GRRKRSPTQS FKFLPVIFKE EPLPDSSLRG FPSTSGPPFG PDMDFSPPRP
PYPSYPHEDP AYETPYLSEG FGYSTPALYP QTGPPPSYRS GLRMFPETGG TTGCARLPSV
SFLPRPFPGD QYGGQGSSFP LGLPFSPPAP FRPPLPSSPP LEDPFNPQSA VHPLPAEGYN
EVGPGYTPGE GASEQEKSRG GYGSGFRDNV PIQGITLEEV SEIIGRDLSG FPARPGEEPP
A
