AIR2_CAEEL
ID AIR2_CAEEL Reviewed; 305 AA.
AC O01427;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Aurora/IPL1-related protein kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase aurora-B;
GN Name=air-2 {ECO:0000312|WormBase:B0207.4};
GN Synonyms=stu-7 {ECO:0000312|WormBase:B0207.4};
GN ORFNames=B0207.4 {ECO:0000312|WormBase:B0207.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9852156; DOI=10.1083/jcb.143.6.1635;
RA Schumacher J.M., Golden A., Donovan P.J.;
RT "AIR-2: an Aurora/Ipl1-related protein kinase associated with chromosomes
RT and midbody microtubules is required for polar body extrusion and
RT cytokinesis in Caenorhabditis elegans embryos.";
RL J. Cell Biol. 143:1635-1646(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=10354474; DOI=10.1016/s0925-4773(99)00020-9;
RA Woollard A., Hodgkin J.;
RT "Stu-7/air-2 is a C. elegans aurora homologue essential for chromosome
RT segregation during embryonic and post-embryonic development.";
RL Mech. Dev. 82:95-108(1999).
RN [4]
RP FUNCTION.
RX PubMed=10975519; DOI=10.1016/s0092-8674(00)00034-9;
RA Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
RA Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M.,
RA Allis C.D.;
RT "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase
RT and Glc7/PP1 phosphatase in budding yeast and nematodes.";
RL Cell 102:279-291(2000).
RN [5]
RP FUNCTION, AND INTERACTION WITH ZEN-4.
RX PubMed=11050384; DOI=10.1016/s0960-9822(00)00715-6;
RA Severson A.F., Hamill D.R., Carter J.C., Schumacher J., Bowerman B.;
RT "The aurora-related kinase AIR-2 recruits ZEN-4/CeMKLP1 to the mitotic
RT spindle at metaphase and is required for cytokinesis.";
RL Curr. Biol. 10:1162-1171(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH ICP-1.
RX PubMed=11050385; DOI=10.1016/s0960-9822(00)00721-1;
RA Kaitna S., Mendoza M., Jantsch-Plunger V., Glotzer M.;
RT "Incenp and an aurora-like kinase form a complex essential for chromosome
RT segregation and efficient completion of cytokinesis.";
RL Curr. Biol. 10:1172-1181(2000).
RN [7]
RP FUNCTION.
RX PubMed=10983970; DOI=10.1016/s1097-2765(00)00023-x;
RA Speliotes E.K., Uren A., Vaux D., Horvitz H.R.;
RT "The survivin-like C. elegans BIR-1 protein acts with the Aurora-like
RT kinase AIR-2 to affect chromosomes and the spindle midzone.";
RL Mol. Cell 6:211-223(2000).
RN [8]
RP FUNCTION.
RX PubMed=12015116; DOI=10.1016/s0960-9822(02)00820-5;
RA Kaitna S., Pasierbek P., Jantsch M., Loidl J., Glotzer M.;
RT "The aurora B kinase AIR-2 regulates kinetochores during mitosis and is
RT required for separation of homologous Chromosomes during meiosis.";
RL Curr. Biol. 12:798-812(2002).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11914278; DOI=10.1101/gad.968302;
RA Hagstrom K.A., Holmes V.F., Cozzarelli N.R., Meyer B.J.;
RT "C. elegans condensin promotes mitotic chromosome architecture, centromere
RT organization, and sister chromatid segregation during mitosis and
RT meiosis.";
RL Genes Dev. 16:729-742(2002).
RN [10]
RP FUNCTION.
RX PubMed=11940606; DOI=10.1083/jcb.200110045;
RA Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R.;
RT "The aurora kinase AIR-2 functions in the release of chromosome cohesion in
RT Caenorhabditis elegans meiosis.";
RL J. Cell Biol. 157:219-229(2002).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12213836; DOI=10.1083/jcb.200202054;
RA Gruneberg U., Glotzer M., Gartner A., Nigg E.A.;
RT "The CeCDC-14 phosphatase is required for cytokinesis in the Caenorhabditis
RT elegans embryo.";
RL J. Cell Biol. 158:901-914(2002).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE CHROMOSOMAL PASSENGER COMPLEX, AND
RP INTERACTION WITH ICP-1; CSC-1 AND BIR-1.
RX PubMed=12707312; DOI=10.1083/jcb.200207117;
RA Romano A., Guse A., Krascenicova I., Schnabel H., Schnabel R., Glotzer M.;
RT "CSC-1: a subunit of the Aurora B kinase complex that binds to the
RT survivin-like protein BIR-1 and the incenp-like protein ICP-1.";
RL J. Cell Biol. 161:229-236(2003).
RN [13]
RP FUNCTION.
RX PubMed=15854913; DOI=10.1016/j.cub.2005.03.041;
RA Guse A., Mishima M., Glotzer M.;
RT "Phosphorylation of ZEN-4/MKLP1 by aurora B regulates completion of
RT cytokinesis.";
RL Curr. Biol. 15:778-786(2005).
RN [14]
RP FUNCTION, AND INTERACTION WITH TLK-1.
RX PubMed=15916946; DOI=10.1016/j.cub.2005.04.019;
RA Han Z., Riefler G.M., Saam J.R., Mango S.E., Schumacher J.M.;
RT "The C. elegans Tousled-like kinase contributes to chromosome segregation
RT as a substrate and regulator of the Aurora B kinase.";
RL Curr. Biol. 15:894-904(2005).
RN [15]
RP INTERACTION WITH BMK-1.
RX PubMed=15548597; DOI=10.1091/mbc.e04-08-0682;
RA Bishop J.D., Han Z., Schumacher J.M.;
RT "The Caenorhabditis elegans Aurora B kinase AIR-2 phosphorylates and is
RT required for the localization of a BimC kinesin to meiotic and mitotic
RT spindles.";
RL Mol. Biol. Cell 16:742-756(2005).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-265.
RX PubMed=18923084; DOI=10.1101/gad.1691208;
RA de Carvalho C.E., Zaaijer S., Smolikov S., Gu Y., Schumacher J.M.,
RA Colaiacovo M.P.;
RT "LAB-1 antagonizes the Aurora B kinase in C. elegans.";
RL Genes Dev. 22:2869-2885(2008).
RN [17]
RP FUNCTION.
RX PubMed=20729837; DOI=10.1038/ncb2093;
RA Dumont J., Oegema K., Desai A.;
RT "A kinetochore-independent mechanism drives anaphase chromosome separation
RT during acentrosomal meiosis.";
RL Nat. Cell Biol. 12:894-901(2010).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23684975; DOI=10.1016/j.cub.2013.04.028;
RA Bembenek J.N., Verbrugghe K.J., Khanikar J., Csankovszki G., Chan R.C.;
RT "Condensin and the spindle midzone prevent cytokinesis failure induced by
RT chromatin bridges in C. elegans embryos.";
RL Curr. Biol. 23:937-946(2013).
RN [19]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-155 AND LYS-168.
RX PubMed=25475837; DOI=10.1038/ncomms6485;
RA Pelisch F., Sonneville R., Pourkarimi E., Agostinho A., Blow J.J.,
RA Gartner A., Hay R.T.;
RT "Dynamic SUMO modification regulates mitotic chromosome assembly and cell
RT cycle progression in Caenorhabditis elegans.";
RL Nat. Commun. 5:5485-5485(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase component of the chromosomal
CC passenger complex (CPC), a complex that acts as a key regulator of
CC chromosome segregation and cytokinesis (PubMed:12707312,
CC PubMed:11050385, PubMed:10983970, PubMed:9852156, PubMed:10354474,
CC PubMed:10975519, PubMed:11050384). The CPC complex has essential
CC functions at the centromere in ensuring correct chromosome alignment
CC and segregation (PubMed:12707312, PubMed:10983970). Required for
CC histone H3 phosphorylation during segregation of homologous chromosomes
CC in meiosis and mitosis (PubMed:18923084). Required for histone H3 'Ser-
CC 10' phosphorylation (PubMed:9852156, PubMed:10354474, PubMed:10975519,
CC PubMed:11050384, PubMed:11050385, PubMed:10983970, PubMed:12015116,
CC PubMed:11940606). Phosphorylates tlk-1 at 'Ser-634', which enhances its
CC activity (PubMed:15916946). Phosphorylates zen-4 at 'Ser-
CC 680'(PubMed:15854913). Required for the recruitment of bub-1 to the
CC ring-shaped domain between chromosomes during meiotic anaphase I
CC (PubMed:20729837). Also required for the localization of the condensin
CC I complex subunit smc-4 to mitotic chromosomes (PubMed:11914278). Acts
CC at the spindle midzone and the midbody to prevent cleavage furrow
CC regression upon chromatin obstructions during cytokinesis
CC (PubMed:12213836, PubMed:23684975). {ECO:0000269|PubMed:10354474,
CC ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:10983970,
CC ECO:0000269|PubMed:11050384, ECO:0000269|PubMed:11050385,
CC ECO:0000269|PubMed:11914278, ECO:0000269|PubMed:11940606,
CC ECO:0000269|PubMed:12015116, ECO:0000269|PubMed:12213836,
CC ECO:0000269|PubMed:12707312, ECO:0000269|PubMed:15854913,
CC ECO:0000269|PubMed:15916946, ECO:0000269|PubMed:18923084,
CC ECO:0000269|PubMed:20729837, ECO:0000269|PubMed:23684975,
CC ECO:0000269|PubMed:9852156}.
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 -!- SUBUNIT: Component of the CPC complex which consists of icp-1; csc-1;
CC bir-1 and air-2 (PubMed:12707312). Within the complex, interacts with
CC icp-1; csc-1 and bir-1 (PubMed:12707312, PubMed:11050385). Interacts
CC with zen-4 (PubMed:11050384). Interacts with tlk-1 and bmk-1
CC (PubMed:15548597, PubMed:15916946). {ECO:0000269|PubMed:11050384,
CC ECO:0000269|PubMed:11050385, ECO:0000269|PubMed:12707312,
CC ECO:0000269|PubMed:15548597, ECO:0000269|PubMed:15916946}.
CC -!- INTERACTION:
CC O01427; G5EE37: icp-1; NbExp=4; IntAct=EBI-312947, EBI-312981;
CC O01427; O17583: lin-10; NbExp=2; IntAct=EBI-312947, EBI-313389;
CC O01427; P34314: tlk-1; NbExp=3; IntAct=EBI-312947, EBI-3890382;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9852156}. Chromosome {ECO:0000269|PubMed:18923084,
CC ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837,
CC ECO:0000269|PubMed:9852156}. Midbody {ECO:0000269|PubMed:23684975,
CC ECO:0000269|PubMed:9852156}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. Note=Meiotic
CC and mitotic chromosomes (PubMed:9852156, PubMed:18923084). During each
CC division, relocates to the midbody microtubules (PubMed:9852156,
CC PubMed:23684975). Localizes on chromosomes during metaphase and on the
CC central spindle during anaphase (PubMed:25475837, PubMed:23684975).
CC Localization to homologous chromosomes during segregation is dependent
CC on lab-1 (PubMed:18923084). {ECO:0000269|PubMed:18923084,
CC ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837,
CC ECO:0000269|PubMed:9852156}.
CC -!- DEVELOPMENTAL STAGE: Present during gametogenesis and throughout
CC embryogenesis (at protein level). {ECO:0000269|PubMed:9852156}.
CC -!- PTM: Phosphorylated. Increased phosphorylation upon chromatin
CC obstructions at anaphase. {ECO:0000269|PubMed:23684975}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts the localization
CC of the condensin subunit smc-4 to mitotic chromosomes
CC (PubMed:11914278). RNAi-mediated knockdown causes failure in mitotic
CC chromosome segregation and cytokinesis, leading to aneuploidy
CC (PubMed:11914278, PubMed:12213836). {ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:12213836}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF071207; AAC70945.1; -; mRNA.
DR EMBL; BX284601; CCD61317.1; -; Genomic_DNA.
DR PIR; B87790; B87790.
DR PIR; T43221; T43221.
DR RefSeq; NP_491714.1; NM_059313.5.
DR AlphaFoldDB; O01427; -.
DR SMR; O01427; -.
DR BioGRID; 37722; 18.
DR ComplexPortal; CPX-3461; Chromosomal passenger complex.
DR DIP; DIP-25477N; -.
DR IntAct; O01427; 7.
DR MINT; O01427; -.
DR STRING; 6239.B0207.4; -.
DR EPD; O01427; -.
DR PaxDb; O01427; -.
DR PeptideAtlas; O01427; -.
DR EnsemblMetazoa; B0207.4.1; B0207.4.1; WBGene00000099.
DR EnsemblMetazoa; B0207.4.2; B0207.4.2; WBGene00000099.
DR GeneID; 172268; -.
DR KEGG; cel:CELE_B0207.4; -.
DR UCSC; B0207.4; c. elegans.
DR CTD; 172268; -.
DR WormBase; B0207.4; CE24761; WBGene00000099; air-2.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000158980; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; O01427; -.
DR OMA; PYGRQTT; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; O01427; -.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR SignaLink; O01427; -.
DR PRO; PR:O01427; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000099; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:ComplexPortal.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IDA:WormBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IDA:WormBase.
DR GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IPI:WormBase.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; IPI:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IMP:WormBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
DR GO; GO:0045184; P:establishment of protein localization; IMP:WormBase.
DR GO; GO:0051257; P:meiotic spindle midzone assembly; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:WormBase.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0031991; P:regulation of actomyosin contractile ring contraction; IMP:WormBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR InterPro; IPR030616; Aur.
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 PANTHER; PTHR24350; PTHR24350; 1.
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; Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Developmental protein;
KW Kinase; Meiosis; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..305
FT /note="Aurora/IPL1-related protein kinase 2"
FT /id="PRO_0000268640"
FT DOMAIN 30..280
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 36..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 155
FT /note="K->R: Reduced in vitro sumo-1 conjugation."
FT /evidence="ECO:0000269|PubMed:25475837"
FT MUTAGEN 168
FT /note="K->R: Reduced in vitro sumo-1 conjugation."
FT /evidence="ECO:0000269|PubMed:25475837"
FT MUTAGEN 265
FT /note="P->L: In or207; temperature sensitive. At 15 degrees
FT Celsius, there are no observed changed in meiosis or
FT mitosis. At 20 or 25 degrees Celsius, meiosis appears
FT normal, embryos are not viable and eggs do not complete the
FT first embryonic division due to defects in chromosome
FT segregation and cytokinesis. In these embryos,
FT phosphorylation of histone H3 is abrogated, but this is not
FT abrogated in germ line nuclei. Embryonic viability is
FT increased in a lab-1 tm1791 mutant background and 17% of
FT embryos complete embryogenesis and reach adulthood as
FT fertile animals. Moreover, the phosphorylation of histone
FT H3 defect is rescued in 30% of these embryos."
FT /evidence="ECO:0000269|PubMed:18923084"
SQ SEQUENCE 305 AA; 34749 MW; 1635EB60D2E14011 CRC64;
MENKPPVINL PEKETVNTPQ KGGKFTINDF EIGRPLGKGK FGSVYLARTK TGHFHVAIKV
LFKSQLISGG VEHQLEREIE IQSHLNHPNI IKLYTYFWDA KKIYLVLEYA PGGEMYKQLT
VSKRFSEPTA AKYMYEIADA LSYCHRKNVI HRDIKPENLL IGSQGELKIG DFGWSVHAPS
NKRQTMCGTM DYLPPEMVNG ADHSDAVDLW AIGVLCYEFL VGKPPFEHED QSKTYAAIKA
ARFTYPDSVK KGARDLIGRL LVVDPKARCT LEQVKEHYWI QGMMEAKIRA EKQQKIEKEA
SLRNH
