PRAG1_RAT
ID PRAG1_RAT Reviewed; 1368 AA.
AC D3ZMK9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Inactive tyrosine-protein kinase PRAG1 {ECO:0000305};
DE AltName: Full=PEAK1-related kinase-activating pseudokinase 1;
DE AltName: Full=Pragma of Rnd2 {ECO:0000303|PubMed:16481321};
GN Name=Prag1 {ECO:0000312|RGD:1311793};
GN Synonyms=Pragmin {ECO:0000303|PubMed:16481321};
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, FUNCTION, AND INTERACTION WITH RND2.
RX PubMed=16481321; DOI=10.1074/jbc.m511314200;
RA Tanaka H., Katoh H., Negishi M.;
RT "Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity.";
RL J. Biol. Chem. 281:10355-10364(2006).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-391, MUTAGENESIS OF TYR-391,
RP AND INTERACTION WITH CSK.
RX PubMed=21873224; DOI=10.1073/pnas.1107740108;
RA Safari F., Murata-Kamiya N., Saito Y., Hatakeyama M.;
RT "Mammalian Pragmin regulates Src family kinases via the Glu-Pro-Ile-Tyr-Ala
RT (EPIYA) motif that is exploited by bacterial effectors.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:14938-14943(2011).
RN [5]
RP INTERACTION WITH CSK, PHOSPHORYLATION AT TYR-391; TYR-238 AND TYR-343,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=27116701; DOI=10.1111/cas.12962;
RA Senda Y., Murata-Kamiya N., Hatakeyama M.;
RT "C-terminal Src kinase-mediated EPIYA phosphorylation of Pragmin creates a
RT feed-forward C-terminal Src kinase activation loop that promotes cell
RT motility.";
RL Cancer Sci. 107:972-980(2016).
RN [6] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7] {ECO:0007744|PDB:6EWX}
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 906-1368, MUTAGENESIS OF TYR-391;
RP LEU-939; ASP-978; TYR-981; LYS-997; GLN-1021; ALA-1329; TYR-1349 AND
RP LEU-1362, SUBUNIT, INTERACTION WITH CSK, PHOSPHORYLATION AT TYR-391,
RP DOMAIN, LACK OF ATP-BINDING, AND FUNCTION.
RX PubMed=29503074; DOI=10.1016/j.str.2018.01.017;
RA Lecointre C., Simon V., Kerneur C., Allemand F., Fournet A., Montarras I.,
RA Pons J.L., Gelin M., Brignatz C., Urbach S., Labesse G., Roche S.;
RT "Dimerization of the Pragmin pseudo-kinase regulates protein tyrosine
RT phosphorylation.";
RL Structure 26:545-554(2018).
CC -!- FUNCTION: Catalytically inactive protein kinase that acts as a scaffold
CC protein (PubMed:29503074). Functions as an effector of the small GTPase
CC RND2, which stimulates RhoA activity and inhibits NGF-induced neurite
CC outgrowth (PubMed:16481321). Promotes Src family kinase (SFK) signallig
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 (PubMed:27116701,
CC PubMed:21873224). Acts as a critical coactivator of Notch signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q571I4,
CC ECO:0000269|PubMed:16481321, ECO:0000269|PubMed:21873224,
CC ECO:0000269|PubMed:27116701, ECO:0000269|PubMed:29503074}.
CC -!- SUBUNIT: Homodimer (PubMed:29503074). Dimerization leads to the
CC catalytic activation of CSK (PubMed:29503074). Interacts (via C-
CC terminus) with RND2 (PubMed:16481321). Interacts with CSK (via SH2
CC domain) in a Tyr-391 phosphorylation-dependent manner; this interaction
CC potentiates kinase activity of CSK (PubMed:29503074, PubMed:21873224,
CC PubMed:27116701). Interacts with NOTCH1 intracellular domain (N1ICD)
CC (By similarity). Forms a complex with N1ICD and MAML1, in a MAML1-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:Q571I4,
CC ECO:0000269|PubMed:16481321, ECO:0000269|PubMed:21873224,
CC ECO:0000269|PubMed:27116701, ECO:0000269|PubMed:29503074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21873224,
CC ECO:0000269|PubMed:27116701}. Nucleus {ECO:0000250|UniProtKB:Q571I4}.
CC Cell junction, focal adhesion {ECO:0000269|PubMed:27116701}.
CC Note=Colocalized with NOTCH1 in the nucleus.
CC {ECO:0000250|UniProtKB:Q571I4}.
CC -!- TISSUE SPECIFICITY: Highly-expressed in brain, including cortical and
CC hippocampal pyramidal neurons, as well as in kidney, spleen, colon and
CC small intestine (PubMed:16481321). {ECO:0000269|PubMed:16481321}.
CC -!- DOMAIN: The dimerization region encompasses helices both from the
CC N- and C-terminal of the protein kinase domain.
CC {ECO:0000269|PubMed:29503074}.
CC -!- PTM: Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is
CC a primary site of phosphorylation. {ECO:0000269|PubMed:27116701}.
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 (PubMed:29503074). {ECO:0000269|PubMed:29503074}.
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DR EMBL; AABR07026025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07026026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473970; EDM09203.1; -; Genomic_DNA.
DR RefSeq; NP_001100785.1; NM_001107315.1.
DR RefSeq; XP_017455620.1; XM_017600131.1.
DR RefSeq; XP_017455621.1; XM_017600132.1.
DR PDB; 6EWX; X-ray; 2.77 A; A/B=906-1368.
DR PDBsum; 6EWX; -.
DR AlphaFoldDB; D3ZMK9; -.
DR SMR; D3ZMK9; -.
DR ELM; D3ZMK9; -.
DR IntAct; D3ZMK9; 2.
DR STRING; 10116.ENSRNOP00000015166; -.
DR iPTMnet; D3ZMK9; -.
DR PhosphoSitePlus; D3ZMK9; -.
DR PaxDb; D3ZMK9; -.
DR PRIDE; D3ZMK9; -.
DR Ensembl; ENSRNOT00000015166; ENSRNOP00000015166; ENSRNOG00000011407.
DR GeneID; 306506; -.
DR KEGG; rno:306506; -.
DR CTD; 157285; -.
DR RGD; 1311793; Prag1.
DR eggNOG; ENOG502QVUZ; Eukaryota.
DR GeneTree; ENSGT00940000157066; -.
DR HOGENOM; CLU_005467_0_0_1; -.
DR InParanoid; D3ZMK9; -.
DR OMA; FKGNGHW; -.
DR OrthoDB; 49921at2759; -.
DR PhylomeDB; D3ZMK9; -.
DR TreeFam; TF331193; -.
DR PRO; PR:D3ZMK9; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Proteomes; UP000234681; Chromosome 16.
DR Bgee; ENSRNOG00000011407; Expressed in cerebellum and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS: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 3D-structure; Cell junction; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1368
FT /note="Inactive tyrosine-protein kinase PRAG1"
FT /id="PRO_0000444634"
FT DOMAIN 940..1291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 200..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..949
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:29503074"
FT REGION 1134..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1368
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:29503074"
FT COMPBIAS 311..330
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 411..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000269|PubMed:27116701"
FT MOD_RES 343
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000269|PubMed:27116701"
FT MOD_RES 391
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000269|PubMed:21873224,
FT ECO:0000269|PubMed:27116701, ECO:0000269|PubMed:29503074"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YV5"
FT MUTAGEN 391
FT /note="Y->A: Does not affect cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:21873224"
FT MUTAGEN 391
FT /note="Y->F: Decreases the interaction with CSK."
FT /evidence="ECO:0000269|PubMed:21873224,
FT ECO:0000269|PubMed:29503074"
FT MUTAGEN 939
FT /note="L->E: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 978
FT /note="D->N: No ATP-binding activity."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 981
FT /note="Y->F: No ATP-binding activity."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 997
FT /note="K->A: Does not affect PRAG1-CSK complex formation.
FT Does not affect PRAG1-induced protein tyrosine
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 1021
FT /note="Q->E: No ATP-binding activity."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 1329
FT /note="A->E: Strong reduction of homodimerization; Does not
FT affect PRAG1-CSK complex formation. Reduces CSK
FT activation."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 1349
FT /note="Y->E: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:29503074"
FT MUTAGEN 1362
FT /note="L->E: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:29503074"
FT HELIX 921..946
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 962..964
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 977..989
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 994..999
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 1026..1031
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1033..1035
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 1059..1068
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 1070..1073
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1074..1080
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1082..1087
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1089..1112
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 1124..1128
FT /evidence="ECO:0007829|PDB:6EWX"
FT STRAND 1173..1176
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1203..1206
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1209..1211
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1214..1226
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1258..1269
FT /evidence="ECO:0007829|PDB:6EWX"
FT TURN 1274..1276
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1280..1292
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1296..1300
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1306..1332
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1341..1352
FT /evidence="ECO:0007829|PDB:6EWX"
FT HELIX 1355..1364
FT /evidence="ECO:0007829|PDB:6EWX"
SQ SEQUENCE 1368 AA; 147716 MW; 31BF773387FD28B7 CRC64;
MSACSDFVEH IWKPGSCKNC FCLRSDHQLT AGHPKARASS LPAGARLPAR PEICRLEDEG
VNGLAYSKPT IAVKPTMMTS ETADLWTEAS LSAEVPKVNW RRTPGKLLLQ KQEDGPIVYL
GSFRGMQKAA GPLACTDSNS RCPPAYTMVG LHNLEARVDR NTALQPVNFQ EEKAGREELP
SAQESFRQKL AAFTGMTSSC LKGPRPCTSP QPLRESLPSE DDSDQRCSPS GDSEGGEYCS
ILDCRPESRD AVHNTEGSGR RRGDCSPICW EQGTCTRPTE EEKQALNFPR ECCGQGSTAN
PPHLGPKKPS LNSEAASSSD GLSCGSSRSG ANSPFAPHLE NDYCSLVKEP TSVKQQDSGC
HLVNSGKYVG QAVDLQPPAL PREAVQPEPI YAESAKRKKA APVPQRPEPK KEQVSSGQVW
TGDTWSQKTP SGWSQEREGP NAAPQVATTI TVIAAHPEED HRTIYLSSPD SAVGVQWPRG
SLNQDLHGSG EEPLVVQGLS SRESHPHNMT ENSSKEKPAI PPKLSKSSPG GSPVSPAAPP
LTDHSDGNTS GSSVGSQPSS RVPTNLTSSC QTNGVAAGDP AKCPPQANSS VLDQRRPRYQ
TGAWSRQCRI EEEEEVGQEL LSQSWGRELE NGIADHSNSS TWHRLHPIDG ASGQNGKTNS
GMSKSASFAF EFPKDRGRLE SFSPPPPPPK SRHLLKMNKS SSDLEKVSQS SAESLSPSFR
GAHVSFTTGS TDSLASDSRT CSDGGPSCEA THSPTISGKK LFAPVPFPSG STEDVSPSGP
AQPPPLPQKK IVSRAASSPD GFFWTQGSPK PRTASPKLNL SHSETNVCAH DEPPLSYSLN
SGNHPHHVFS SSEPLEKAFK GSVPWAPALG PANSKGGCGS PNLQGRAATS TSSSQLSVSS
QASTGSSQLQ LHSLLSSISS KEGTYAKLGG LYTQSLARLV TKCEDLFMGG LKTELRFDEN
SWSLFKLICN KPCCDSGDAI YYGATCSKDP DSIYAVKICK TPEPKSASYC SPSVPVHFNI
QQDCGHFVAS VPSSMLAFPD TSSKDPAPAA PSHTPAQEQD CVVVITREVP HQTASDFVRD
SVASHRAEPE VYERRVCFLL LQLCNGLEHL KEHGIIHRDL CLENLLLVHC NPQSSPGPSA
NPSVPTTTSR CPSAAPAATT ACQGGPGEKH LPRLIISNFL KAKQKPGGTT NLQQKKSQAR
LAPEIVSASQ YRKFDEFQTG ILIYELLHQP NPFEVRAQLR ERDYRREDLP PLPTLSLYSP
GLQQLAHLLL EADPIKRIRI GEAKRVLQCL LWGPRRELVE QPCPSEEVLC NTLHNWIDMK
RALMMMKFAE KAVERRRGVE LEDWLCCQYL ASAEPGALLQ SLKLLQLL
