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 24-JAN-2024, entry version 135. 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}, Nack GN {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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 8. DR IntAct; Q571I4; 2. DR STRING; 10090.ENSMUSP00000106118; -. DR GlyGen; Q571I4; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q571I4; -. DR PhosphoSitePlus; Q571I4; -. DR EPD; Q571I4; -. DR jPOST; Q571I4; -. DR MaxQB; Q571I4; -. DR PaxDb; 10090-ENSMUSP00000106118; -. DR PeptideAtlas; Q571I4; -. DR ProteomicsDB; 289882; -. DR ProteomicsDB; 310231; -. DR Antibodypedia; 73468; 150 antibodies from 28 providers. DR DNASU; 244418; -. DR Ensembl; ENSMUST00000110492.2; ENSMUSP00000106118.2; ENSMUSG00000050271.13. DR GeneID; 244418; -. DR KEGG; mmu:244418; -. DR AGR; MGI:1196223; -. 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; DLKMSAC; -. DR OrthoDB; 2914135at2759; -. DR PhylomeDB; Q571I4; -. DR TreeFam; TF331193; -. DR Reactome; R-MMU-9696270; RND2 GTPase cycle. DR BioGRID-ORCS; 244418; 1 hit in 75 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 193 other cell types or 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: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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR22972:SF3; INACTIVE TYROSINE-PROTEIN KINASE PRAG1; 1. DR PANTHER; PTHR22972; SERINE/THREONINE PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //