NPR1_YEAST
ID NPR1_YEAST Reviewed; 790 AA.
AC P22211; D6W103;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Nitrogen permease reactivator protein;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase NPR1;
GN Name=NPR1; OrderedLocusNames=YNL183C; ORFNames=N1631;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sigma 1278B;
RX PubMed=2125693; DOI=10.1007/bf00633845;
RA Vandenbol M., Jauniaux J.-C., Grenson M.;
RT "The Saccharomyces cerevisiae NPR1 gene required for the activity of
RT ammonia-sensitive amino acid permeases encodes a protein kinase
RT homologue.";
RL Mol. Gen. Genet. 222:393-399(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 45-60; 63-120; 123-147; 255-269; 273-296; 315-362 AND
RP 368-403, PHOSPHORYLATION AT SER-47; SER-85; SER-90; SER-100; SER-111;
RP SER-116; SER-125; SER-137; SER-141; SER-257; SER-259; SER-260; SER-288;
RP SER-292; SER-317; SER-320; SER-328; SER-336; SER-353; SER-356; SER-357 AND
RP SER-385, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-47;
RP SER-257 AND SER-357.
RX PubMed=18980262; DOI=10.1002/rcm.3790;
RA Gander S., Bonenfant D., Altermatt P., Martin D.E., Hauri S., Moes S.,
RA Hall M.N., Jenoe P.;
RT "Identification of the rapamycin-sensitive phosphorylation sites within the
RT Ser/Thr-rich domain of the yeast Npr1 protein kinase.";
RL Rapid Commun. Mass Spectrom. 22:3743-3753(2008).
RN [5]
RP FUNCTION.
RX PubMed=6343084; DOI=10.1111/j.1432-1033.1983.tb07439.x;
RA Grenson M.;
RT "Study of the positive control of the general amino-acid permease and other
RT ammonia-sensitive uptake systems by the product of the NPR1 gene in the
RT yeast Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 133:141-144(1983).
RN [6]
RP FUNCTION.
RX PubMed=9843498; DOI=10.1093/emboj/17.23.6924;
RA Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.;
RT "The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits
RT turnover of the tryptophan permease.";
RL EMBO J. 17:6924-6931(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11500493; DOI=10.1074/jbc.m102944200;
RA De Craene J.-O., Soetens O., Andre B.;
RT "The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast
RT Gap1 permease.";
RL J. Biol. Chem. 276:43939-43948(2001).
RN [8]
RP INTERACTION WITH TIP41.
RX PubMed=11741537; DOI=10.1016/s1097-2765(01)00386-0;
RA Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
RT "TIP41 interacts with TAP42 and negatively regulates the TOR signaling
RT pathway.";
RL Mol. Cell 8:1017-1026(2001).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION.
RX PubMed=15247235; DOI=10.1074/jbc.m407372200;
RA Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B.,
RA Primig M., Hall M.N.;
RT "NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent
RT transcription in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:37512-37517(2004).
RN [11]
RP FUNCTION.
RX PubMed=16864574; DOI=10.1074/jbc.m605551200;
RA Feller A., Boeckstaens M., Marini A.-M., Dubois E.;
RT "Transduction of the nitrogen signal activating Gln3-mediated transcription
RT is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 281:28546-28554(2006).
RN [12]
RP FUNCTION.
RX PubMed=16864577; DOI=10.1074/jbc.m604171200;
RA Tate J.J., Rai R., Cooper T.G.;
RT "Ammonia-specific regulation of Gln3 localization in Saccharomyces
RT cerevisiae by protein kinase Npr1.";
RL J. Biol. Chem. 281:28460-28469(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-357, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP FUNCTION.
RX PubMed=17493133; DOI=10.1111/j.1365-2958.2007.05681.x;
RA Boeckstaens M., Andre B., Marini A.M.;
RT "The yeast ammonium transport protein Mep2 and its positive regulator, the
RT Npr1 kinase, play an important role in normal and pseudohyphal growth on
RT various nitrogen media through retrieval of excreted ammonium.";
RL Mol. Microbiol. 64:534-546(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-137; SER-141 AND
RP TYR-334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Nutrient-regulated protein kinase that promotes the activity
CC of at least 6 distinct transport systems for nitrogenous nutrients
CC under conditions of nitrogen catabolite derepression. Under poor
CC nitrogen growth conditions, required for post-Golgi sorting of the
CC general amino acid permease GAP1 and the three known ammonia permeases,
CC MEP1/2/3, to the plasma membrane. Contributes also to the stability and
CC the retention of GAP1 at the plasma membrane. Inversely, promotes the
CC degradation of tryptophan permease TAT2 under the same conditions.
CC Activity is regulated by the TOR signaling pathway via phosphatase
CC SIT4. Although thought to be involved in regulation of GLN3-dependent
CC transcription by nitrogen catabolite repression, this seems to be an
CC indirect effect from the reduced uptake of the nitrogen-repressing
CC compound. {ECO:0000269|PubMed:11500493, ECO:0000269|PubMed:15247235,
CC ECO:0000269|PubMed:16864574, ECO:0000269|PubMed:16864577,
CC ECO:0000269|PubMed:17493133, ECO:0000269|PubMed:6343084,
CC ECO:0000269|PubMed:9843498}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Dephosphorylation by SIT4 activates NPR1 kinase
CC activity.
CC -!- SUBUNIT: Interacts with TIP41. {ECO:0000269|PubMed:11741537}.
CC -!- INTERACTION:
CC P22211; P15442: GCN2; NbExp=2; IntAct=EBI-12207, EBI-330;
CC P22211; P06782: SNF1; NbExp=2; IntAct=EBI-12207, EBI-17516;
CC P22211; P35169: TOR1; NbExp=2; IntAct=EBI-12207, EBI-19374;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11500493}.
CC Note=Appears to be more concentrated in punctate structures reminiscent
CC of the Golgi or of an endosomal compartment.
CC -!- PTM: Hyperphosphorylated in nitrogen-rich growth medium. Nitrogen
CC limitation (or rapamycin treatment) leads to substantial, though not
CC complete dephosphorylation. Autophosphorylation plays only a minor role
CC and seems not to be regulated by the quality of the nitrogen source.
CC {ECO:0000269|PubMed:18980262}.
CC -!- MISCELLANEOUS: Present with 284 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X56084; CAA39564.1; -; Genomic_DNA.
DR EMBL; Z71459; CAA96076.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10369.1; -; Genomic_DNA.
DR PIR; S63138; S63138.
DR RefSeq; NP_014216.1; NM_001183021.1.
DR AlphaFoldDB; P22211; -.
DR SMR; P22211; -.
DR BioGRID; 35649; 165.
DR DIP; DIP-4327N; -.
DR IntAct; P22211; 54.
DR MINT; P22211; -.
DR STRING; 4932.YNL183C; -.
DR iPTMnet; P22211; -.
DR MaxQB; P22211; -.
DR PaxDb; P22211; -.
DR PRIDE; P22211; -.
DR EnsemblFungi; YNL183C_mRNA; YNL183C; YNL183C.
DR GeneID; 855538; -.
DR KEGG; sce:YNL183C; -.
DR SGD; S000005127; NPR1.
DR VEuPathDB; FungiDB:YNL183C; -.
DR eggNOG; KOG0590; Eukaryota.
DR GeneTree; ENSGT00940000176633; -.
DR HOGENOM; CLU_000288_82_4_1; -.
DR InParanoid; P22211; -.
DR OMA; LQVMEYC; -.
DR BioCyc; YEAST:G3O-33194-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P22211; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P22211; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045806; P:negative regulation of endocytosis; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:SGD.
DR GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..790
FT /note="Nitrogen permease reactivator protein"
FT /id="PRO_0000086445"
FT DOMAIN 438..742
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 561
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 444..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 47
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 257
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 334
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MOD_RES 357
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18980262,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18980262"
FT MUTAGEN 47
FT /note="S->A: Abolishes autophosphorylation; when associated
FT with A-257 and A-357."
FT /evidence="ECO:0000269|PubMed:18980262"
FT MUTAGEN 257
FT /note="S->A: Abolishes autophosphorylation; when associated
FT with A-47 and A-357."
FT /evidence="ECO:0000269|PubMed:18980262"
FT MUTAGEN 257
FT /note="S->D: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:18980262"
FT MUTAGEN 357
FT /note="S->A: Abolishes autophosphorylation; when associated
FT with A-47 and A-257."
FT /evidence="ECO:0000269|PubMed:18980262"
FT CONFLICT 154
FT /note="T -> A (in Ref. 1; CAA39564)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="S -> P (in Ref. 1; CAA39564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 85990 MW; 0ECFA33376740733 CRC64;
MSSLTRLLQE KRKNETSNSS PRTSADTLTT TPESQSLDLH SRNKSSSHIG SVSNSSSSDR
NRANVPVPGS VTTVTQIYSE EDSSSTAGSS LDDRNQFSSS FLNANFAHTA SFYGTSAQSR
DRFGSLINDQ GTAGLSSHGG SFAAQNRITS RLSTTSHTSG RAIPSLSSSI PYSVPNSNKD
NNSSNSNSSS LSSSWLETYA GGMPNNISAI DSNVISSPKV DSVEPRFVIS KQKLQKASMD
SNNANATQSR SISRSGSFSS QLGNFFFSKN SKESSNSNSA GMSFSANSNG PSPNIKNPNV
TNGSTPIPKP IRARQSSIYS ASRQPTGSYT DNFYGSPSSV HDHLPPSQSV PRSQHSSIGD
LKRFFKKSSN SNLSSNSNNV IPNGSPLSSG IAVPSHSHSS SHFAAGNNSY STSYNGNGDT
IYSHSHGGSG IPFSKRYIKT GADLGAGAGG SVKLAQRISD NKIFAVKEFR TKFENESKRD
YVKKITSEYC IGTTLNHPNI IETIEIVYEN DRILQVMEYC EYDLFAIVMS NKMSYEEICC
CFKQILTGVQ YLHSIGLAHR DLKLDNCVIN EKGIVKLIDF GAAVVFSYPF SKNLVEASGI
VGSDPYLAPE VCIFAKYDPR PVDIWSSAII FACMILKKFP WKIPKLRDNS FKLFCSGRDC
DSLSSLVTRT PDPPSYDESH STEKKKPESS SNNVSDPNNV NIGPQRLLHS LPEETQHIVG
RMIDLAPACR GNIEEIMEDP WIRSIDMCHL VEDGLSFKVV RGEDHHHTQV DQSEAHIAGL
EKKKKKQNNQ
