PRAG1_MOUSE
ID PRAG1_MOUSE Reviewed; 1373 AA.
AC Q571I4; E9QLH9; Q8CB68;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Inactive tyrosine-protein kinase PRAG1 {ECO:0000305};
DE AltName: Full=Notch activation complex kinase {ECO:0000303|PubMed:25038227};
DE AltName: Full=PEAK1-related kinase-activating pseudokinase 1 {ECO:0000312|MGI:MGI:1196223};
DE AltName: Full=Sugen kinase 223;
DE AltName: Full=Tyrosine-protein kinase SgK223;
GN Name=Prag1 {ECO:0000312|MGI:MGI:1196223};
GN Synonyms=D8Ertd82e {ECO:0000312|MGI:MGI:1196223},
GN Nack {ECO:0000303|PubMed:25038227}, Sgk223;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-1373.
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 190-1373.
RC TISSUE=Spleen;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-1373.
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBUNIT, INTERACTION WITH NOTCH1,
RP INTERACTION WITH NOTCH1 AND MAML1, AND SUBCELLULAR LOCATION.
RX PubMed=25038227; DOI=10.1158/0008-5472.can-14-1547;
RA Weaver K.L., Alves-Guerra M.C., Jin K., Wang Z., Han X., Ranganathan P.,
RA Zhu X., DaSilva T., Liu W., Ratti F., Demarest R.M., Tzimas C., Rice M.,
RA Vasquez-Del Carpio R., Dahmane N., Robbins D.J., Capobianco A.J.;
RT "NACK is an integral component of the Notch transcriptional activation
RT complex and is critical for development and tumorigenesis.";
RL Cancer Res. 74:4741-4751(2014).
CC -!- FUNCTION: Catalytically inactive protein kinase that acts as a scaffold
CC protein (By similarity). Functions as an effector of the small GTPase
CC RND2, which stimulates RhoA activity and inhibits NGF-induced neurite
CC outgrowth (By similarity). Promotes Src family kinase (SFK) signaling
CC by regulating the subcellular localization of CSK, a negative regulator
CC of these kinases, leading to the regulation of cell morphology and
CC motility by a CSK-dependent mechanism (By similarity). Acts as a
CC critical coactivator of Notch signaling (PubMed:25038227).
CC {ECO:0000250|UniProtKB:D3ZMK9, ECO:0000269|PubMed:25038227}.
CC -!- SUBUNIT: Homodimer (By similarity). Dimerization leads to the catalytic
CC activation of CSK (By similarity). Interacts (via C-terminus) with RND2
CC (By similarity). Interacts with CSK (via SH2 domain) in a Tyr-391
CC phosphorylation-dependent manner; this interaction potentiates kinase
CC activity of CSK (By similarity). Interacts with NOTCH1 intracellular
CC domain (N1ICD) (PubMed:25038227). Forms a complex with PRAG1, N1ICD and
CC MAML1, in a MAML1-dependent manner (PubMed:25038227).
CC {ECO:0000250|UniProtKB:D3ZMK9, ECO:0000269|PubMed:25038227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3ZMK9}. Nucleus
CC {ECO:0000269|PubMed:25038227}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q86YV5}. Note=Colocalized with NOTCH1 in the
CC nucleus (PubMed:25038227).
CC -!- DOMAIN: The dimerization region encompasses helices both from the
CC N- and C-terminal of the protein kinase domain.
CC {ECO:0000250|UniProtKB:D3ZMK9}.
CC -!- PTM: Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is
CC a primary site of phosphorylation. {ECO:0000250|UniProtKB:D3ZMK9}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice shown complete embryonic lethality
CC (PubMed:25038227). {ECO:0000269|PubMed:25038227}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Despite of the presence of a putative ATP-binding motif, this
CC protein does not bind ATP, suggesting that it has no protein kinase
CC activity. {ECO:0000250|UniProtKB:D3ZMK9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89024.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC29528.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90130.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC121858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK036672; BAC29528.1; ALT_INIT; mRNA.
DR EMBL; AK220205; BAD90130.1; ALT_INIT; mRNA.
DR EMBL; BC089024; AAH89024.1; ALT_INIT; mRNA.
DR CCDS; CCDS22247.2; -.
DR RefSeq; NP_766499.2; NM_172911.3.
DR RefSeq; XP_011240439.1; XM_011242137.1.
DR AlphaFoldDB; Q571I4; -.
DR SMR; Q571I4; -.
DR BioGRID; 232647; 7.
DR IntAct; Q571I4; 2.
DR STRING; 10090.ENSMUSP00000106118; -.
DR iPTMnet; Q571I4; -.
DR PhosphoSitePlus; Q571I4; -.
DR EPD; Q571I4; -.
DR jPOST; Q571I4; -.
DR MaxQB; Q571I4; -.
DR PaxDb; Q571I4; -.
DR PeptideAtlas; Q571I4; -.
DR PRIDE; Q571I4; -.
DR ProteomicsDB; 289882; -.
DR ProteomicsDB; 310231; -.
DR Antibodypedia; 73468; 129 antibodies from 28 providers.
DR DNASU; 244418; -.
DR Ensembl; ENSMUST00000110492; ENSMUSP00000106118; ENSMUSG00000050271.
DR GeneID; 244418; -.
DR KEGG; mmu:244418; -.
DR CTD; 157285; -.
DR MGI; MGI:1196223; Prag1.
DR VEuPathDB; HostDB:ENSMUSG00000050271; -.
DR eggNOG; ENOG502QVUZ; Eukaryota.
DR GeneTree; ENSGT00940000157066; -.
DR HOGENOM; CLU_005467_0_0_1; -.
DR InParanoid; Q571I4; -.
DR OMA; FKGNGHW; -.
DR OrthoDB; 49921at2759; -.
DR PhylomeDB; Q571I4; -.
DR TreeFam; TF331193; -.
DR BioGRID-ORCS; 244418; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Prag1; mouse.
DR PRO; PR:Q571I4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q571I4; protein.
DR Bgee; ENSMUSG00000050271; Expressed in dorsal pancreas and 191 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1373
FT /note="Inactive tyrosine-protein kinase PRAG1"
FT /id="PRO_0000263009"
FT DOMAIN 945..1296
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..954
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT REGION 1041..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1373
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT COMPBIAS 311..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9,
FT ECO:0007744|PubMed:15592455"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT CONFLICT 154..156
FT /note="LEA -> PGG (in Ref. 2; BAC29528)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="LA -> VD (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="D -> Y (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> C (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="G -> S (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="T -> I (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="V -> M (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="A -> V (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="G -> E (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="S -> I (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160
FT /note="A -> V (in Ref. 3; BAD90130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1373 AA; 147945 MW; E24B9CA499EA9BB5 CRC64;
MSACSDFVEH IWKPGSCKNC FCLRSDHQPT AGHPKARANS LPAGTRLPAR PENCRLDDEG
VNGLAYSKPT IAVKPTMMTS ETSDLWTEAS LSAEVPKVNW RRTPGKLLLP KQEDEPIVYL
GSFRGLQKPA SPLACTDGNS RCPPAYTMVG LHNLEARVDR NTAFQPVSFQ EEKAGREELP
SAHESFRQKL AAFAGMTSSC PKGPRPCTSP QPLRESLPSE DDSDQRCSPS GDSEGGEYCS
ILDCCPESKD AVHSTEGSGR RGGDCSPTCR EQGPRTRPTE EEKQGLSFPR ECCGQGSTAN
PPRLGPKKPS LNSEAASSSD GLSCGSSRSG ASSPFAPHLE NDYCSLVKEP ASGKQQDLSG
HFLTSGKCVG QAAELQPASL LRDPVQPEPI YAESAKRKKA APGPPRPEPK KEQVPAGHSQ
GQVWTGDTWI QKTPPSWSQD REGANPAPQV ATTITVIAAH PEEDHRTIYL SSPDSAVGVQ
WPRGPSNQDL QAGEEEPLVA QGLTSRESHP HNVTENTAKE KPAIPPKLSK SSPGGSPVSP
APPLTDHSDG NTGGSSVGPQ LLSRVPANLT SSCHTNGVAT AGDSAKCPPP ATSSSVLDQR
RPRYQTGAWS RQCRIEEEEE VGQELSQSWG RELENGTADH SNSSTWHRLH PIDGTSGQNS
KTNSGMSKSA SFAFEFPKDR GRLEAFSPPP PPPKSRHLLK MNKSSSDLEK VSQSSAESLS
PSFRGAHVSF TTGSTDSLAS DSRPCSDGGP SYEPTHSPTI SGKKLFAPVP FPSGSTEDVS
PGGGPAQPPP LPQKKIVSRA ASSPDGFFWT QGSPKPRTAS PKLNLSHSET NVCAHDEPPF
NCSLNSGNRS HHVFSSSEPL GKAFKGNAPW APALGLANSK GGCGSPSLQC RAATSTSSSQ
LSVSSQASSS STQLQLHSLL SSISSKEGTY AKLGGLYTQS LARLVTKCED LFMGGQKKEL
RFNENYWSLF KLTCNKPCCD SGDAIYYCAT CSEDPGSIYA VKICKTPEPK SASYCSPSVP
VHFNIQQDCG HFVASVPSSM LASPDTSSKD TAPAVSPQPP AQEQDCVVVI TREVPHQTAS
DFVRDSMASH RAEPEVYERR VCFLLLQLCN GLEHLKEHGI IHRDLCLENL LLAHCNPQSS
PGPSATPTVP TTTSRCPSAA PAATTACQGG PGEKQLPRLI ISNFLKAKQK PGGTTNLQQK
KSQARLAPEI VSASQYRKFD EFQTGILIYE LLHQPNPFEV RAQLRERDYR REDLPPLPTL
SLYSPGLQQL AHLLLEADPI KRIRIGEAKR VLQCLLWGPR RELVEQPCTS EEVLCNTLHN
WIDMKRALMM MKFAEKAVDR RRGVELEDWL CCQYLASAEP GALLQSLKLL QLL
