BCK1_YEAST
ID BCK1_YEAST Reviewed; 1478 AA.
AC Q01389; D6VW89; P32894;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Serine/threonine-protein kinase BCK1/SLK1/SSP31;
DE EC=2.7.11.1;
GN Name=BCK1; Synonyms=LAS3, SLK1, SSP31; OrderedLocusNames=YJL095W;
GN ORFNames=J0906;
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].
RX PubMed=1545797; DOI=10.1128/mcb.12.3.1162-1178.1992;
RA Costigan C., Gehrung S., Snyder M.;
RT "A synthetic lethal screen identifies SLK1, a novel protein kinase homolog
RT implicated in yeast cell morphogenesis and cell growth.";
RL Mol. Cell. Biol. 12:1162-1178(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840547; DOI=10.1016/0378-1119(91)90499-2;
RA Irie K., Araki H., Oshima Y.;
RT "A new protein kinase, SSP31, modulating the SMP3 gene-product involved in
RT plasmid maintenance in Saccharomyces cerevisiae.";
RL Gene 108:139-144(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-1119; ILE-1120;
RP GLY-1146 AND ALA-1174.
RC STRAIN=ATCC 204278 / EG123 / SM1058;
RX PubMed=1729597; DOI=10.1128/mcb.12.1.172-182.1992;
RA Lee K.S., Levin D.E.;
RT "Dominant mutations in a gene encoding a putative protein kinase (BCK1)
RT bypass the requirement for a Saccharomyces cerevisiae protein kinase C
RT homolog.";
RL Mol. Cell. Biol. 12:172-182(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871887; DOI=10.1002/yea.320101112;
RA Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S.,
RA Zimmermann F.K.;
RT "Sequence and function analysis of a 9.74 kb fragment of Saccharomyces
RT cerevisiae chromosome X including the BCK1 gene.";
RL Yeast 10:1481-1488(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 459-1173.
RA Cusick M.E.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747 AND SER-1058, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407; SER-411; SER-491;
RP SER-816; SER-1058 AND SER-1061, 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).
CC -!- FUNCTION: Serine/threonine protein kinase involved in a signal
CC transduction pathway that plays a role in yeast cell morphogenesis and
CC cell growth. This pathway seems to start by SMP3; then involve the
CC kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates
CC MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
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 -!- INTERACTION:
CC Q01389; Q00684: CDC14; NbExp=4; IntAct=EBI-3470, EBI-4192;
CC Q01389; P36006: MYO3; NbExp=6; IntAct=EBI-3470, EBI-11670;
CC Q01389; Q04439: MYO5; NbExp=6; IntAct=EBI-3470, EBI-11687;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 112 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA21179.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M84389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D10389; BAA01226.1; -; Genomic_DNA.
DR EMBL; X60227; CAA42788.1; -; Genomic_DNA.
DR EMBL; X77923; CAA54896.1; -; Genomic_DNA.
DR EMBL; Z49370; CAA89389.1; -; Genomic_DNA.
DR EMBL; Z49369; CAA89388.1; -; Genomic_DNA.
DR EMBL; M88604; AAA21179.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006943; DAA08705.1; -; Genomic_DNA.
DR PIR; S20117; S20117.
DR RefSeq; NP_012440.1; NM_001181528.1.
DR AlphaFoldDB; Q01389; -.
DR SMR; Q01389; -.
DR BioGRID; 33662; 829.
DR DIP; DIP-2223N; -.
DR IntAct; Q01389; 56.
DR MINT; Q01389; -.
DR STRING; 4932.YJL095W; -.
DR CarbonylDB; Q01389; -.
DR iPTMnet; Q01389; -.
DR MaxQB; Q01389; -.
DR PaxDb; Q01389; -.
DR PRIDE; Q01389; -.
DR EnsemblFungi; YJL095W_mRNA; YJL095W; YJL095W.
DR GeneID; 853350; -.
DR KEGG; sce:YJL095W; -.
DR SGD; S000003631; BCK1.
DR VEuPathDB; FungiDB:YJL095W; -.
DR eggNOG; KOG0198; Eukaryota.
DR GeneTree; ENSGT00980000202011; -.
DR HOGENOM; CLU_002516_0_0_1; -.
DR InParanoid; Q01389; -.
DR OMA; PWSNFEV; -.
DR BioCyc; YEAST:G3O-31550-MON; -.
DR PRO; PR:Q01389; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; Q01389; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IMP:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IGI:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:SGD.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0010447; P:response to acidic pH; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1478
FT /note="Serine/threonine-protein kinase BCK1/SLK1/SSP31"
FT /id="PRO_0000085662"
FT DOMAIN 1175..1440
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1303
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1181..1189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1134
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MUTAGEN 1119
FT /note="T->P: In BCK1-19; Dominant active."
FT /evidence="ECO:0000269|PubMed:1729597"
FT MUTAGEN 1120
FT /note="I->K: In BCK1-11; Dominant active."
FT /evidence="ECO:0000269|PubMed:1729597"
FT MUTAGEN 1120
FT /note="I->T: In BCK1-16; Dominant active."
FT /evidence="ECO:0000269|PubMed:1729597"
FT MUTAGEN 1146
FT /note="G->V: In BCK1-10; Dominant active."
FT /evidence="ECO:0000269|PubMed:1729597"
FT MUTAGEN 1174
FT /note="A->P: In BCK1-20; Dominant active."
FT /evidence="ECO:0000269|PubMed:1729597"
FT CONFLICT 59
FT /note="F -> I (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="E -> V (in Ref. 2; BAA01226)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> P (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="N -> I (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 703..714
FT /note="RYPQTPSYYYDR -> STPKPRVITMTE (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="S -> A (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="L -> V (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="A -> S (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="T -> N (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="T -> N (in Ref. 3; CAA42788)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="A -> R (in Ref. 7; AAA21179)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="A -> R (in Ref. 7; AAA21179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1478 AA; 164195 MW; D586C3A497A5BB33 CRC64;
MPFLRKIAGT AHTHSRSDSN SSVKFGHQPT SSVASTKSSS KSPRATSRKS IYDDIRSQFP
NLTPNSTSSQ FYESTPVIEQ SFNWTTDDHI SAGTLENPTS FTNSSYKNDN GPSSLSDSRK
SSGGNSVNSL SFDKLILSWD PTDPDEWTMH RVTSWFKFHD FPESWILFFK KHQLFGHRFI
KLLAYDNFAV YEKYLPQTKT ASYTRFQQLL KKTMTKNVTN SHIRQKSASK LKSSRSSSES
IKSKLKNSKS QEDISNSRST SESALSPTKS GPSKTDEKNF LHSTSTHQKT KSASSLYRRS
FISLRGSSSS NASSAKSPSN IKLSIPARPH SIIESNSTLT KSASPPASPS YPSIFRRHHK
SSSSESSLLN SLFGSGIGEE APTKPNPQGH SLSSENLAKG KSKHYETNVS SPLKQSSLPT
SDDKGNLWNK FKRKSQIGVP SPNTVAYVTS QETPSLKSNS STATLTVQTA DVNIPSPSSS
PPPIPKTANR SLEVISTEDT PKISSTTASF KETYPDCINP DKTVPVPVNN QKYSVKNFLL
DQKFYPLKKT GLNDSENKYI LVTKDNVSFV PLNLKSVAKL SSFKESALTK LGINHKNVTF
HMTDFDCDIG AAIPDDTLEF LKKSLFLNTS GKIYIKDQMK LQQKPKPAPL TSENNVPLKS
VKSKSSMRSG TSSLIASTDD VSIVTSSSDI TSFDEHASGS GRRYPQTPSY YYDRVSNTNP
TEELNYWNIK EVLSHEENAP KMVFKTSPKL ELNLPDKGSK LNIPTPITEN ESKSSFQVLR
KDEGTEIDFN HRRESPYTKP ELAPKREAPK PPANTSPQRT LSTSKQNKPI RLVRASTKIS
RSKRSKPLPP QLLSSPIEAS SSSPDSLTSS YTPASTHVLI PQPYKGANDV MRRLKTDQDS
TSTSPSLKMK QKVNRSNSTV STSNSIFYSP SPLLKRGNSK RVVSSTSAAD IFEENDITFA
DAPPMFDSDD SDDDSSSSDD IIWSKKKTAP ETNNENKKDE KSDNSSTHSD EIFYDSQTQD
KMERKMTFRP SPEVVYQNLE KFFPRANLDK PITEGIASPT SPKSLDSLLS PKNVASSRTE
PSTPSRPVPP DSSYEFIQDG LNGKNKPLNQ AKTPKRTKTI RTIAHEASLA RKNSVKLKRQ
NTKMWGTRMV EVTENHMVSI NKAKNSKGEY KEFAWMKGEM IGKGSFGAVY LCLNVTTGEM
MAVKQVEVPK YSSQNEAILS TVEALRSEVS TLKDLDHLNI VQYLGFENKN NIYSLFLEYV
AGGSVGSLIR MYGRFDEPLI KHLTTQVLKG LAYLHSKGIL HRDMKADNLL LDQDGICKIS
DFGISRKSKD IYSNSDMTMR GTVFWMAPEM VDTKQGYSAK VDIWSLGCIV LEMFAGKRPW
SNLEVVAAMF KIGKSKSAPP IPEDTLPLIS QIGRNFLDAC FEINPEKRPT ANELLSHPFS
EVNETFNFKS TRLAKFIKSN DKLNSSKLRI TSQENKTE
