PLO1_SCHPO
ID PLO1_SCHPO Reviewed; 683 AA.
AC P50528;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/threonine-protein kinase plo1;
DE EC=2.7.11.21;
GN Name=plo1; ORFNames=SPAC23C11.16;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=7744248; DOI=10.1101/gad.9.9.1059;
RA Ohkura H., Hagan I.M., Glover D.M.;
RT "The conserved Schizosaccharomyces pombe kinase plo1, required to form a
RT bipolar spindle, the actin ring, and septum, can drive septum formation in
RT G1 and G2 cells.";
RL Genes Dev. 9:1059-1073(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11676915; DOI=10.1016/s0960-9822(01)00478-x;
RA Krapp A., Schmidt S., Cano E., Simanis V.;
RT "S. pombe cdc11p, together with sid4p, provides an anchor for septation
RT initiation network proteins on the spindle pole body.";
RL Curr. Biol. 11:1559-1568(2001).
RN [4]
RP FUNCTION, INTERACTION WITH CUT12, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP SER-124; GLU-139 AND THR-197.
RX PubMed=12815070; DOI=10.1101/gad.256003;
RA MacIver F.H., Tanaka K., Robertson A.M., Hagan I.M.;
RT "Physical and functional interactions between polo kinase and the spindle
RT pole component Cut12 regulate mitotic commitment in S. pombe.";
RL Genes Dev. 17:1507-1523(2003).
RN [5]
RP FUNCTION, INTERACTION WITH ABP2; CUT23; DMF1; SCK1; SPAC1006.03C;
RP SPAC6B12.08; SPAC26H5.05 AND SUM1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-69; ASP-181; GLU-193; THR-197; LYS-251; ILE-252; SER-256; PHE-493;
RP TRP-497; VAL-498; GLY-505; 508-TYR--LEU-510; 519-PHE-ASN-520; VAL-533;
RP LEU-565; 572-TYR-MET-573; ARG-605 AND 625-ASP--LYS-627.
RX PubMed=12615979; DOI=10.1242/jcs.00314;
RA Reynolds N., Ohkura H.;
RT "Polo boxes form a single functional domain that mediates interactions with
RT multiple proteins in fission yeast polo kinase.";
RL J. Cell Sci. 116:1377-1387(2003).
RN [6]
RP INTERACTION WITH SID4.
RX PubMed=15062098; DOI=10.1016/j.cub.2004.03.036;
RA Morrell J.L., Tomlin G.C., Rajagopalan S., Venkatram S., Feoktistova A.S.,
RA Tasto J.J., Mehta S., Jennings J.L., Link A., Balasubramanian M.K.,
RA Gould K.L.;
RT "Sid4p-Cdc11p assembles the septation initiation network and its regulators
RT at the S. pombe SPB.";
RL Curr. Biol. 14:579-584(2004).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442 AND SER-585, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [9]
RP FUNCTION, INTERACTION WITH MOA1, AND SUBCELLULAR LOCATION.
RX PubMed=25533956; DOI=10.1038/nature14097;
RA Kim J., Ishiguro K., Nambu A., Akiyoshi B., Yokobayashi S., Kagami A.,
RA Ishiguro T., Pendas A.M., Takeda N., Sakakibara Y., Kitajima T.S.,
RA Tanno Y., Sakuno T., Watanabe Y.;
RT "Meikin is a conserved regulator of meiosis-I-specific kinetochore
RT function.";
RL Nature 517:466-471(2015).
CC -!- FUNCTION: Required to form a bipolar spindle, the actin ring and
CC septum. Functions upstream of the whole septum formation pathway,
CC including actin ring formation (regulated by late septation genes) and
CC septal material deposition (regulated by early septation genes).
CC Behaves as a 'septum-promoting factor', and could also be involved in
CC inducing other late events of cell division (PubMed:12615979,
CC PubMed:12815070, PubMed:7744248). Together with moa1, acts as a
CC regulator of kinetochore function during meiosis I: required both for
CC mono-orientation of kinetochores on sister chromosomes and protection
CC of centromeric cohesin from separase-mediated cleavage
CC (PubMed:25533956). {ECO:0000269|PubMed:12615979,
CC ECO:0000269|PubMed:12815070, ECO:0000269|PubMed:25533956,
CC ECO:0000269|PubMed:7744248}.
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=2.7.11.21;
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=2.7.11.21;
CC -!- SUBUNIT: Interacts with abp2, cut12, cut23, dmf1, sck1, sid4,
CC spac1006.03c, spac6b12.08, spac26h5.05 and sum1. Interacts with moa1
CC (PubMed:25533956). {ECO:0000269|PubMed:12615979,
CC ECO:0000269|PubMed:12815070, ECO:0000269|PubMed:15062098,
CC ECO:0000269|PubMed:25533956}.
CC -!- INTERACTION:
CC P50528; O59755: cut12; NbExp=3; IntAct=EBI-1112601, EBI-1112619;
CC P50528; O94556: cut23; NbExp=5; IntAct=EBI-1112601, EBI-1116472;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:25533956}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:11676915,
CC ECO:0000269|PubMed:12615979, ECO:0000269|PubMed:12815070,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X85758; CAA59766.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11167.1; -; Genomic_DNA.
DR PIR; T38254; T38254.
DR RefSeq; NP_593647.1; NM_001019078.2.
DR AlphaFoldDB; P50528; -.
DR SMR; P50528; -.
DR BioGRID; 278444; 56.
DR DIP; DIP-35381N; -.
DR IntAct; P50528; 16.
DR MINT; P50528; -.
DR STRING; 4896.SPAC23C11.16.1; -.
DR iPTMnet; P50528; -.
DR MaxQB; P50528; -.
DR PaxDb; P50528; -.
DR PRIDE; P50528; -.
DR EnsemblFungi; SPAC23C11.16.1; SPAC23C11.16.1:pep; SPAC23C11.16.
DR GeneID; 2541957; -.
DR KEGG; spo:SPAC23C11.16; -.
DR PomBase; SPAC23C11.16; plo1.
DR VEuPathDB; FungiDB:SPAC23C11.16; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_000288_46_2_1; -.
DR InParanoid; P50528; -.
DR OMA; LKHFERY; -.
DR PhylomeDB; P50528; -.
DR BRENDA; 2.7.11.21; 5613.
DR Reactome; R-SPO-156711; Polo-like kinase mediated events.
DR Reactome; R-SPO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-SPO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SPO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-SPO-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-SPO-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-SPO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:P50528; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
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:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:PomBase.
DR GO; GO:1990571; P:meiotic centromere clustering; IMP:PomBase.
DR GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IMP:PomBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IMP:PomBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IGI:PomBase.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IPI:PomBase.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:PomBase.
DR GO; GO:0140434; P:positive regulation of protein localization to meiotic spindle pole body; IMP:PomBase.
DR GO; GO:0031031; P:positive regulation of septation initiation signaling; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IBA:GO_Central.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_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 Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
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; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Kinase; Kinetochore; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..683
FT /note="Serine/threonine-protein kinase plo1"
FT /id="PRO_0000086572"
FT DOMAIN 41..296
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 500..567
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 604..670
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 317..683
FT /note="Localization to the spindle poly body"
FT REGION 322..683
FT /note="Interaction with cut12"
FT REGION 375..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 69
FT /note="K->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 69
FT /note="K->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 124
FT /note="S->D: Enhances kinase activity; when associated with
FT D-197."
FT /evidence="ECO:0000269|PubMed:12815070"
FT MUTAGEN 139
FT /note="E->K: In ts allele plo1.ts2. Impairs kinase activity
FT at both 25 and 36 degrees Celsius and impairs association
FT with the spindle pole body and bipolar spindle formation."
FT /evidence="ECO:0000269|PubMed:12815070"
FT MUTAGEN 181
FT /note="D->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 193
FT /note="E->G: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 197
FT /note="T->D: Enhances kinase activity; when associated with
FT D-124."
FT /evidence="ECO:0000269|PubMed:12615979,
FT ECO:0000269|PubMed:12815070"
FT MUTAGEN 197
FT /note="T->V: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979,
FT ECO:0000269|PubMed:12815070"
FT MUTAGEN 251
FT /note="K->E: Loss of function and impairs interaction with
FT spac6b12.08."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 252
FT /note="I->T: Loss of function and impairs interaction with
FT spac6b12.08."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 256
FT /note="S->P: Loss of function and impairs interaction with
FT spac6b12.08."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 493
FT /note="F->L: Loss of function and impairs interaction with
FT cut23 and spac6b12.08."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 497
FT /note="W->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 498
FT /note="V->A: Loss of function and impairs interaction with
FT dmf1, spac1006.03c and spac6b12.08."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 505
FT /note="G->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 508..510
FT /note="YQL->AAA: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 519..520
FT /note="FN->AA: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 533
FT /note="V->A: Loss of function and impairs interaction with
FT cut23, dmf1 and spac6b12.08."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 565
FT /note="L->F: Loss of function and impairs interaction with
FT cut23."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 572..573
FT /note="YM->AA: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 605
FT /note="R->P: Loss of function and impairs interaction with
FT cut23."
FT /evidence="ECO:0000269|PubMed:12615979"
FT MUTAGEN 625..627
FT /note="DHR->AAA: Loss of function."
FT /evidence="ECO:0000269|PubMed:12615979"
SQ SEQUENCE 683 AA; 77302 MW; F11CD0EF9B913917 CRC64;
MASVAIKEPK TAITPKKKSK ASRLCFTPPT NLHNNKKNIF YTRYDCIGEG GFARCFRVKD
NYGNIYAAKV IAKRSLQNDK TKLKLFGEIK VHQSMSHPNI VGFIDCFEDS TNIYLILELC
EHKSLMELLR KRKQLTEPEV RYLMMQILGA LKYMHKKRVI HRDLKLGNIM LDESNNVKIG
DFGLAALLMD DEERKMTICG TPNYIAPEIL FNSKEGHSFE VDLWSAGVVM YALLIGKPPF
QDKEVKTIYR KIKANSYSFP SNVDISAEAK DLISSLLTHD PSIRPSIDDI VDHEFFHTGY
MASTLPDEIL HSMPIWPSSQ SKSSFQRNLD FVASASGVGF GNSAGVEKNK PYALRTDEVD
NDRILPSVLS PRDRVNPVMK IGPETKPVPS KLSTALHAAR KSTDGSLGSR VKVLREESQS
FVPTKSAVTE QVEPIQLIRS LSANTVSRLS KVGNMKSDIW ISVKKTALKI GMALEAHTHA
LTSEDADSEP VLFITKWVDY SNKYGLGYQL SDESVGVHFN DDTSLLFSAD EEVVEYALHP
KDTEIKPYIY PASKVPESIR SKLQLLKHFK SYMGQNLSKA VQDESFEKPK NSTSNTMLFM
QHYLRTRQAI MFRLSNGIFQ FNFLDHRKVV ISSTARKIIV LDKERERVEL PLQEASAFSE
DLRSRLKYIR ETLESWASKM EVS
