E2AK4_RAT
ID E2AK4_RAT Reviewed; 1649 AA.
AC D4A7V9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=eIF-2-alpha kinase GCN2 {ECO:0000250|UniProtKB:Q9QZ05};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9QZ05};
DE AltName: Full=Eukaryotic translation initiation factor 2-alpha kinase 4 {ECO:0000312|RGD:1311439};
DE AltName: Full=GCN2-like protein;
GN Name=Eif2ak4 {ECO:0000312|RGD:1311439}; Synonyms=Gcn2;
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 POSSIBLE FUNCTION.
RX PubMed=15051816; DOI=10.1093/jn/134.4.717;
RA Gietzen D.W., Ross C.M., Hao S., Sharp J.W.;
RT "Phosphorylation of eIF2alpha is involved in the signaling of indispensable
RT amino acid deficiency in the anterior piriform cortex of the brain in
RT rats.";
RL J. Nutr. 134:717-723(2004).
RN [3]
RP FUNCTION.
RX PubMed=15774759; DOI=10.1126/science.1104882;
RA Hao S., Sharp J.W., Ross-Inta C.M., McDaniel B.J., Anthony T.G., Wek R.C.,
RA Cavener D.R., McGrath B.C., Rudell J.B., Koehnle T.J., Gietzen D.W.;
RT "Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform
RT cortex.";
RL Science 307:1776-1778(2005).
CC -!- FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates
CC the alpha subunit of eukaryotic translation initiation factor 2
CC (EIF2S1/eIF-2-alpha) in response to low amino acid availability (By
CC similarity). Plays a role as an activator of the integrated stress
CC response (ISR) required for adaptation to amino acid starvation (By
CC similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress
CC converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor,
CC leading to a global attenuation of cap-dependent translation, and thus
CC to a reduced overall utilization of amino acids, while concomitantly
CC initiating the preferential translation of ISR-specific mRNAs, such as
CC the transcriptional activator ATF4, and hence allowing ATF4-mediated
CC reprogramming of amino acid biosynthetic gene expression to alleviate
CC nutrient depletion (By similarity). Required for the translational
CC induction of protein kinase PRKCH following amino acid starvation (By
CC similarity). Binds uncharged tRNAs (By similarity). Involved in cell
CC cycle arrest by promoting cyclin D1 mRNA translation repression after
CC the unfolded protein response pathway (UPR) activation or cell cycle
CC inhibitor CDKN1A/p21 mRNA translation activation in response to amino
CC acid deprivation (By similarity). Plays a role in the consolidation of
CC synaptic plasticity, learning as well as formation of long-term memory
CC (By similarity). Plays a role in neurite outgrowth inhibition (By
CC similarity). Plays a role in feeding behavior to maintain amino acid
CC homeostasis; contributes to the innate aversion toward diets of
CC imbalanced amino acid composition (PubMed:15051816, PubMed:15774759).
CC Plays a proapoptotic role in response to glucose deprivation (By
CC similarity). Promotes global cellular protein synthesis repression in
CC response to UV irradiation independently of the stress-activated
CC protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK
CC signaling pathways (By similarity). Plays a role in the antiviral
CC response against alphavirus infection; impairs early viral mRNA
CC translation of the incoming genomic virus RNA, thus preventing
CC alphavirus replication (By similarity). {ECO:0000250|UniProtKB:P15442,
CC ECO:0000250|UniProtKB:Q9P2K8, ECO:0000250|UniProtKB:Q9QZ05,
CC ECO:0000269|PubMed:15051816, ECO:0000269|PubMed:15774759}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9QZ05};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9QZ05};
CC -!- SUBUNIT: Homodimer; homodimerization is important for kinase activation
CC by uncharged tRNAs. Interacts with GCN1; this interaction stimulates
CC EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety
CC of stress conditions, such as amino acid depletion, UV-C irradiation,
CC proteasome inhibitor treatment and glucose deprivation. Interacts with
CC DNAJC3; this interaction inhibits EIF2AK4/GCN2 kinase activity during
CC endoplasmic reticulum (ER), hypothermic and amino acid-starving stress
CC conditions. {ECO:0000250|UniProtKB:P15442,
CC ECO:0000250|UniProtKB:Q9QZ05}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZ05}.
CC -!- DOMAIN: The histidyl-tRNA synthetase-like region and protein kinase
CC domains are necessary for eIF-2-alpha kinase activity and eIF-2-alpha-
CC mediated translational control. The histidyl-tRNA synthetase-like
CC domain is necessary for binding to uncharged tRNAs. Kinase domain 1 is
CC a degenerate kinase domain. {ECO:0000250|UniProtKB:Q9QZ05}.
CC -!- PTM: Autophosphorylated; autophosphorylation on Thr-899 is increased
CC upon amino acid starvation and in UV irradiation cells and inhibited in
CC presence of IMPACT. {ECO:0000250|UniProtKB:Q9QZ05}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AABR07053494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07053495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D4A7V9; -.
DR SMR; D4A7V9; -.
DR STRING; 10116.ENSRNOP00000009222; -.
DR jPOST; D4A7V9; -.
DR PaxDb; D4A7V9; -.
DR PeptideAtlas; D4A7V9; -.
DR PRIDE; D4A7V9; -.
DR RGD; 1311439; Eif2ak4.
DR VEuPathDB; HostDB:ENSRNOG00000006027; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_1_0_1; -.
DR InParanoid; D4A7V9; -.
DR OMA; GSEMIYE; -.
DR TreeFam; TF101512; -.
DR PRO; PR:D4A7V9; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006027; Expressed in stomach and 20 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR GO; GO:0070417; P:cellular response to cold; ISO:RGD.
DR GO; GO:1990253; P:cellular response to leucine starvation; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0036492; P:eiF2alpha phosphorylation in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0140469; P:GCN2-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISS:UniProtKB.
DR GO; GO:0032792; P:negative regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0032057; P:negative regulation of translational initiation in response to stress; ISO:RGD.
DR GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; ISO:RGD.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0071264; P:positive regulation of translational initiation in response to starvation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR GO; GO:0060259; P:regulation of feeding behavior; ISO:RGD.
DR GO; GO:0010998; P:regulation of translational initiation by eIF2 alpha phosphorylation; ISS:UniProtKB.
DR GO; GO:0043558; P:regulation of translational initiation in response to stress; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0002286; P:T cell activation involved in immune response; ISO:RGD.
DR GO; GO:0019081; P:viral translation; ISS:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF54495; SSF54495; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; ATP-binding; Cell cycle; Coiled coil; Cytoplasm;
KW Differentiation; Growth arrest; Kinase; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Translation regulation; tRNA-binding.
FT CHAIN 1..1649
FT /note="eIF-2-alpha kinase GCN2"
FT /id="PRO_0000435425"
FT DOMAIN 25..137
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT DOMAIN 296..539
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 590..1001
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1493
FT /note="Histidyl-tRNA synthetase-like"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ05"
FT COILED 146..205
FT /evidence="ECO:0000255"
FT COMPBIAS 706..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 847
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 596..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2K8"
FT MOD_RES 667
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2K8"
FT MOD_RES 870
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2K8"
FT MOD_RES 899
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ05"
FT MOD_RES 904
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1259
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2K8"
SQ SEQUENCE 1649 AA; 186724 MW; 75D093684454115F CRC64;
MAGGRGAAGR GPAEPQESYS QRQDHELQAL EAIYGSDFQD LRPDARGRVR EPPEINLVLY
PQGLAGEEVY VQVELRVKCP PTYPDVVPEI ELKNTKGLSN ESVNLLKSHL EELAKKQCGE
VMIFELAHHV QSFLSEHNKP PPKSFHEEML ERQAQEKQQR LLEARQKEEQ EQREILHEIQ
KRKEEIKEEK KRKEMAKQER LEITSLTNQD HASKRDPAGH RAAAFLHGGS PDFVGNGKAR
AHSSGRSRRE RQYSVCSGEA SPGSCDILYF CVGSADQLMV HKGKCVGSDE QLGKVVYNAL
ETATGSFVLL YEWVLQWQKK MGPCLTSQEK EKIDKCKKQI QGAETEFSSL VKLSHPNIVR
YFAMNSREEK DSIVVDILAE HISGISLAAH LSHSGPVPMH QLRKYTAQLL AGLDYLHRNS
VVHKVLSTAS VLVDAEGTVK ITDYSISKRL ADICKEDVFE QTRVRFSDSA LPYKTGKKGD
VWRLGLLLLS LSQGQECEEY PVTIPSDLPA DFQDFLKKCV CLDDKERWSP QQLLKHSFIN
PQPKMPLVEQ SPEDSGGQDY IETIIPSNQL PSAAFFTETQ RQFSRYFIEF EELQLLGKGA
FGAVIKVQNK LDGCCYAVKR IPINPASRQF RRIKGEVTLL SRLHHENIVR YYNAWIERHE
RPAVPGTPPP DYIPQAQNSS ATGGKASGDT EELGSVEAAA PPPILSSSVE WSTSAERSNS
ARFPVTGQDS SSDEEDEDER DGVFSQSFLP ASDSDSDIIF DNEDENSKSQ NQDEDCNEKD
SRHEIEPSVT TEAVHYLYIQ MEYCEKSTLR DTIDQGLFRD TSRLWRLFRE ILDGLAYIHE
KGMIHRDLKP VNIFLDSDDH VKIGDFGLAT DHLAFNAEGK QDDQAGDHVI KSDPSGHLTG
MVGTALYVSP EVQGSTKSAY NQKVDLFSLG IILFEMSYHP MVTASERIFV LNQLRDPTSP
KFPDDFEDGE HTKQKSVISW LLNHDPAKRP TAMELLKSEL LPPPQMEESE LHEVLHHTLA
NTDGKAYRTM MSQLFCQHSS PAIDYTYDSD ILKGNFLIRT AKIQQLVCET IVRVFKRHGA
VQLCTPLLLP RNRQIYEHNE AALFMDHSGM LVMLPFDLRV PFARYVARNN ILNLKRYCIE
RVFRPRKLDR FHPKELLECA FDIVTSTANS SLPTAETIYT IYEVIQEFPA LQERNYSIYL
NHTMLLKAIL LHCGIPEDKL SQVYVILYDA VTEKLTRREV EAKFCNLSLS SNSLCRLYKF
IEQKGDLQDL TPTINSLIKQ KTGIAQLVKY SLKDLEEVVG LLKKLGVKLQ VSINLGLVYK
VQQHNGIIFQ FLAFSKRRQR VVPEILAAGG RYDLLIPKFR GPQALGPVPT AVGVSIAIDK
IFAAVLNMGE PVTVSSCDLL VVSAGQMSMS RAINLTQKLW TAGITAEIMY DWSQSQEELQ
EYCRHHEITY VALVSDKEGS HVKVKSFEKE RQTEKRVLES DLVDHVMQKL RTKVGDERNF
RDASDNLAVQ TLKGSFSNAS GLFEIHGTTV VPTVSVISPE KLSASTRRRH EIQVQTRLQT
TLANLHQKSS EIEILAVDLP KETILQFLSL EWDADEQAFN TTVKQLLSRL PKQRYLKLVC
DEIYNIKVEK KVSVLFLYSY RDDYYRILF
