ID   RIM15_YEAST             Reviewed;        1770 AA.
AC   P43565; D6VTJ8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 231.
DE   RecName: Full=Serine/threonine-protein kinase RIM15;
DE            EC=2.7.11.1;
GN   Name=RIM15; Synonyms=TAK1; OrderedLocusNames=YFL033C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=9111339; DOI=10.1128/mcb.17.5.2688;
RA   Vidan S., Mitchell A.P.;
RT   "Stimulation of yeast meiotic gene expression by the glucose-repressible
RT   protein kinase Rim15p.";
RL   Mol. Cell. Biol. 17:2688-2697(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP   MUTAGENESIS OF LYS-823.
RX   PubMed=9744870; DOI=10.1101/gad.12.18.2943;
RA   Reinders A., Buerckert N., Boller T., Wiemken A., De Virgilio C.;
RT   "Saccharomyces cerevisiae cAMP-dependent protein kinase controls entry into
RT   stationary phase through the Rim15p protein kinase.";
RL   Genes Dev. 12:2943-2955(1998).
RN   [5]
RP   FUNCTION, PHOSPHORYLATION AT THR-1075, AND SUBCELLULAR LOCATION.
RX   PubMed=16308562; DOI=10.1038/sj.emboj.7600889;
RA   Wanke V., Pedruzzi I., Cameroni E., Dubouloz F., De Virgilio C.;
RT   "Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex.";
RL   EMBO J. 24:4271-4278(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733 AND SER-1764, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-476; THR-704 AND
RP   THR-747, AND 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704; SER-709; SER-733;
RP   SER-736; SER-737; SER-1044; SER-1048; SER-1064; SER-1421; SER-1531;
RP   SER-1538; SER-1542 AND SER-1565, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH IGO1.
RX   PubMed=20471941; DOI=10.1016/j.molcel.2010.02.039;
RA   Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S.,
RA   Devgan G., Snyder M., Broach J.R., De Virgilio C.;
RT   "Initiation of the TORC1-regulated G0 program requires Igo1/2, which
RT   license specific mRNAs to evade degradation via the 5'-3' mRNA decay
RT   pathway.";
RL   Mol. Cell 38:345-355(2010).
CC   -!- FUNCTION: Protein kinase that positively regulates proper entry into
CC       stationary phase of cells under nutrient starvation conditions.
CC       Involved in glycogen and trehalose accumulation, derepression of
CC       stress-induced genes, induction of thermotolerance and starvation
CC       resistance, and proper G1 cell cycle arrest. Also involved in the
CC       activation of a meiotic genes activation pathway. Phosphorylates IGO1
CC       and IGO2, both involved in the TORC1 control of gene expression and
CC       chronological life span. {ECO:0000269|PubMed:16308562,
CC       ECO:0000269|PubMed:20471941, ECO:0000269|PubMed:9744870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- ACTIVITY REGULATION: Kinase activity is inhibited by phosphorylation by
CC       cAMP-dependent protein kinase (PKA). {ECO:0000269|PubMed:9744870}.
CC   -!- SUBUNIT: Interacts with the cyclin-dependent kinase (CDK) PHO85 and
CC       IGO1. {ECO:0000269|PubMed:20471941}.
CC   -!- INTERACTION:
CC       P43565; P13186: KIN2; NbExp=2; IntAct=EBI-15150, EBI-9723;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16308562}. Nucleus
CC       {ECO:0000269|PubMed:16308562}.
CC   -!- PTM: Autophosphorylated. Phosphorylation by PKA strongly inhibits
CC       kinase activity. Phosphorylation by cyclin-CDK PHO80-PHO85 under
CC       favorable growth condition causes inactivation of RIM15 by promoting
CC       its export to the cytoplasm. {ECO:0000269|PubMed:16308562}.
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; D50617; BAA09206.1; -; Genomic_DNA.
DR   EMBL; U83459; AAB64088.1; -; Genomic_DNA.
DR   EMBL; AJ001030; CAA04486.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12408.1; -; Genomic_DNA.
DR   PIR; S56221; S56221.
DR   RefSeq; NP_116620.1; NM_001179933.1.
DR   AlphaFoldDB; P43565; -.
DR   SMR; P43565; -.
DR   BioGRID; 31114; 398.
DR   DIP; DIP-2510N; -.
DR   ELM; P43565; -.
DR   FunCoup; P43565; 370.
DR   IntAct; P43565; 18.
DR   MINT; P43565; -.
DR   STRING; 4932.YFL033C; -.
DR   CarbonylDB; P43565; -.
DR   GlyGen; P43565; 7 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; P43565; -.
DR   PaxDb; 4932-YFL033C; -.
DR   PeptideAtlas; P43565; -.
DR   EnsemblFungi; YFL033C_mRNA; YFL033C; YFL033C.
DR   GeneID; 850511; -.
DR   KEGG; sce:YFL033C; -.
DR   AGR; SGD:S000001861; -.
DR   SGD; S000001861; RIM15.
DR   VEuPathDB; FungiDB:YFL033C; -.
DR   eggNOG; KOG0605; Eukaryota.
DR   HOGENOM; CLU_000709_4_0_1; -.
DR   InParanoid; P43565; -.
DR   OMA; AKLYYAF; -.
DR   OrthoDB; 162894at2759; -.
DR   BioCyc; YEAST:G3O-30429-MONOMER; -.
DR   BRENDA; 2.7.11.1; 984.
DR   Reactome; R-SCE-2465910; MASTL Facilitates Mitotic Progression.
DR   BioGRID-ORCS; 850511; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P43565; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43565; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IDA:SGD.
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:0034605; P:cellular response to heat; IMP:SGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:SGD.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:SGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR   GO; GO:1903452; P:positive regulation of G1 to G0 transition; IMP:SGD.
DR   GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   FunFam; 1.10.510.10:FF:000340; Serine threonine protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:001008; Serine/threonine-protein kinase cek1; 1.
DR   FunFam; 3.40.50.2300:FF:000504; Serine/threonine-protein kinase RIM15; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR050236; Ser_Thr_kinase_AGC.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF1; SERINE_THREONINE-PROTEIN KINASE GREATWALL; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Meiosis; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..1770
FT                   /note="Serine/threonine-protein kinase RIM15"
FT                   /id="PRO_0000086605"
FT   DOMAIN          794..1254
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1255..1320
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   DOMAIN          1636..1750
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   REGION          334..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1378..1403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1448..1507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1519..1572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..358
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..632
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..692
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..980
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1031
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1378..1391
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1392..1401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1463..1481
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        918
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         800..808
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         823
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         704
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         709
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         736
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         737
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         747
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         1044
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1048
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1064
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1075
FT                   /note="Phosphothreonine; by PHO85"
FT                   /evidence="ECO:0000269|PubMed:16308562"
FT   MOD_RES         1421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1531
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1565
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1764
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MUTAGEN         823
FT                   /note="K->Y: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:9744870"
SQ   SEQUENCE   1770 AA;  196531 MW;  DC1064825000FAFF CRC64;
     MFNRSNTAGG SQAMKEGLGI NKLSPISSNS NPSSLTSSNY EKYLQLATEK NPCMILELEL
     DGKVRYGSPQ WNTITGVADD SGSSPTYIAD LILGSDQDKG VFQKATDMLL MNDDTSCTIT
     FKIKAADYEG SAGCDDESTI TTLEARGILI RDGHTQLPSH TMWIVKPRTN DWSDFYANED
     AQDDMVIQLS DNCDDIDIQL PEEFAKTLGF GAKIFVQYLK RIRLEMIIDE FNLPLPKMEL
     CRVCENFVPV WWLETHSQSC VCEHRTESLI QLLHDNLLEQ QAILANFTKD SEYKGSQIQV
     RSNNFLNQVL DSLRELCQDA IDINPSEMVP DLYHSLSTFP QDNGNNNNNN NNNNNNNNAL
     LDQFPIQKDT VSLNSYFQFS PRTNHNIQNV TSWQSRFFLN DDQDPGLALL IHDTLDLARK
     KVDAVLRLDN AMTYSLKIKN EVNNYVVQLI REQIEINKHA ILTHPMNLRS SSIFHSPLPQ
     IHSQQPEAEN LIYSSSTPLQ VQHDQCASFE APSKSHLEPI PFPVSSIEET PTANDIRHPS
     PLPRSCSNTV MKLPTPRRKL DSNGLFSDAY LNADIIPNPS IESTISIDRD NNTNSRGSSM
     KQYGIGEATD SRTSNSERPS SSSSRLGIRS RSITPRQKIE YSHVDNDDRT NEMLSRDKDS
     LQPQPSVDTT ITSSTQATTT GTKTNSNNST NSVLPKLMTS ISLTPRRGSP SFGNLASHSM
     QQTNSFKLIH DKSPISSPFT FSKDFLTPEQ HPSNIARTDS INNAMLTSPN MPLSPLLLAT
     NQTVKSPTPS IKDYDILKPI SKGAYGSVYL ARKKLTGDYF AIKVLRKSDM IAKNQVTNVK
     SERAIMMVQS DKPYVARLFA SFQNKDNLFL VMEYLPGGDL ATLIKMMGYL PDQWAKQYLT
     EIVVGVNDMH QNGIIHHDLK PENLLIDNAG HVKLTDFGLS RAGLIRRHKF VPHKSSLSIS
     STLPIDNPAN NFTMNNNNSN HSQLSTPDSF TSDHKQYNRS KKSSLGQQYE HSEYSSTSNS
     HSMTPTPSTN TVVYPSYYRG KDRSHGSSNI DLPASLRRSE SQLSFSLLDI SRSSTPPLAN
     PTNSNANNIM RRKSLTENKS FSNDLLSSDA IAATNTNINS NNNISLSPAP SDLALFYPDD
     SKQNKKFFGT PDYLAPETIE GKGEDNKQCD WWSVGCIFFE LLLGYPPFHA ETPDAVFKKI
     LSGVIQWPEF KNEEEEREFL TPEAKDLIEK LLVVDPAKRL GAKGIQEIKD HPYFKNVDWD
     HVYDEEASFV PTIDNPEDTD YFDLRGAELQ DFGDDIENDN ANILFGKHGI NTDVSELSAA
     NLSPPLNHKN ILSRKLSMSN TTNRSSNNSN SSVHDFGAHT PVNKLSIASV LESVPQETGY
     ITPNGTGTTT TSAKNSPNLK NLSLAIPPHM RDRRSSKLND SQTEFGSFNF RNLSALDKAN
     KDAINRLKSE HFSEQPGVHR RTSSASLMGS SSDGSVSTPG SNASNTTSGG KLKIHKPTIS
     GSPSTFGTFP KTFLRSDSFS TRSYSPERSI SIDSSTLSRK GSIIGDNQQT TANSSDSPTM
     TKFKSPLSPA NTTTVSSYFS RQRVLSKSFS QRTNSSDLSA EESDRLQAIS RVNSLRNRRR
     SGRKSSSTSE IGYHMDVLVC EPIPIHRYRV TKDLENLGCT VVSVGAGDEL VSRATSGVSF
     DLIMTALKLP KLGAIDIVQL LKQTNGANST TPIVAITNYF QEAATSRVFD DVLEKPVKLD
     ELKKLVAKYA LKKSQEDEEH TILSDSDETH
//