NAT10_MOUSE
ID NAT10_MOUSE Reviewed; 1024 AA.
AC Q8K224; Q3UE04; Q6ZPJ7; Q80VD3; Q8BW78;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=RNA cytidine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=N-acetyltransferase 10 {ECO:0000255|HAMAP-Rule:MF_03211};
GN Name=Nat10 {ECO:0000255|HAMAP-Rule:MF_03211}; Synonyms=Kiaa1709;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1005.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-1024.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=29703891; DOI=10.1038/s41467-018-03770-3;
RG Sanger Mouse Genetics Project;
RA Balmus G., Larrieu D., Barros A.C., Collins C., Abrudan M., Demir M.,
RA Geisler N.J., Lelliott C.J., White J.K., Karp N.A., Atkinson J., Kirton A.,
RA Jacobsen M., Clift D., Rodriguez R., Adams D.J., Jackson S.P.;
RT "Targeting of NAT10 enhances healthspan in a mouse model of human
RT accelerated aging syndrome.";
RL Nat. Commun. 9:1700-1700(2018).
CC -!- FUNCTION: RNA cytidine acetyltransferase that catalyzes the formation
CC of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and
CC tRNAs. Catalyzes ac4C modification of a broad range of mRNAs, enhancing
CC mRNA stability and translation. mRNA ac4C modification is frequently
CC present within wobble cytidine sites and promotes translation
CC efficiency. Mediates the formation of ac4C at position 1842 in 18S rRNA
CC (By similarity). May also catalyze the formation of ac4C at position
CC 1337 in 18S rRNA (By similarity). Required for early nucleolar
CC cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA
CC synthesis (By similarity). Catalyzes the formation of ac4C in serine
CC and leucine tRNAs (By similarity). Requires the tRNA-binding adapter
CC protein THUMPD1 for full tRNA acetyltransferase activity but not for
CC 18S rRNA acetylation. In addition to RNA acetyltransferase activity,
CC also able to acetylate lysine residues of proteins, such as histones,
CC microtubules, p53/TP53 and MDM2, in vitro. The relevance of the protein
CC lysine acetyltransferase activity is however unsure in vivo. Activates
CC telomerase activity by stimulating the transcription of TERT, and may
CC also regulate telomerase function by affecting the balance of
CC telomerase subunit assembly, disassembly, and localization (By
CC similarity). Involved in the regulation of centrosome duplication by
CC acetylating CENATAC during mitosis, promoting SASS6 proteasome
CC degradation (By similarity). {ECO:0000250|UniProtKB:P53914,
CC ECO:0000250|UniProtKB:Q9H0A0, ECO:0000255|HAMAP-Rule:MF_03211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + an
CC N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate;
CC Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA-COMP:13576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-
CC acetylcytidine in tRNA + CoA + H(+) + phosphate;
CC Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:13671,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in mRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-
CC acetylcytidine in mRNA + CoA + H(+) + phosphate;
CC Xref=Rhea:RHEA:58480, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15146,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9H0A0};
CC -!- SUBUNIT: Interacts with THUMPD1. Interacts with SUN1 (via N-terminus).
CC Also interacts with TERT. {ECO:0000255|HAMAP-Rule:MF_03211}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03211}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality before 14.5 dpc
CC (PubMed:29703891). Heterozygous mice are healthy and show enhanced
CC healthspan in a Hutchinson-Gilford progeria syndrome (HGPS) mouse
CC model; molecular mechanisms explaining the relation between Nat10
CC activity and nuclear architecture defects in HGPS mouse models are
CC however unclear (PubMed:29703891). {ECO:0000269|PubMed:29703891}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX537331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034516; AAH34516.1; -; mRNA.
DR EMBL; BC047436; AAH47436.1; -; mRNA.
DR EMBL; AK054029; BAC35626.1; -; mRNA.
DR EMBL; AK149825; BAE29107.1; -; mRNA.
DR EMBL; AK129427; BAC98237.1; -; Transcribed_RNA.
DR CCDS; CCDS16480.1; -.
DR RefSeq; NP_694766.1; NM_153126.2.
DR AlphaFoldDB; Q8K224; -.
DR SMR; Q8K224; -.
DR BioGRID; 221159; 8.
DR IntAct; Q8K224; 4.
DR MINT; Q8K224; -.
DR STRING; 10090.ENSMUSP00000028608; -.
DR iPTMnet; Q8K224; -.
DR PhosphoSitePlus; Q8K224; -.
DR EPD; Q8K224; -.
DR MaxQB; Q8K224; -.
DR PaxDb; Q8K224; -.
DR PeptideAtlas; Q8K224; -.
DR PRIDE; Q8K224; -.
DR ProteomicsDB; 252777; -.
DR Antibodypedia; 25804; 228 antibodies from 35 providers.
DR DNASU; 98956; -.
DR Ensembl; ENSMUST00000028608; ENSMUSP00000028608; ENSMUSG00000027185.
DR GeneID; 98956; -.
DR KEGG; mmu:98956; -.
DR UCSC; uc008liy.1; mouse.
DR CTD; 55226; -.
DR MGI; MGI:2138939; Nat10.
DR VEuPathDB; HostDB:ENSMUSG00000027185; -.
DR eggNOG; KOG2036; Eukaryota.
DR GeneTree; ENSGT00390000009140; -.
DR HOGENOM; CLU_004652_0_0_1; -.
DR InParanoid; Q8K224; -.
DR OMA; QDEEFAG; -.
DR OrthoDB; 296129at2759; -.
DR PhylomeDB; Q8K224; -.
DR TreeFam; TF300601; -.
DR BioGRID-ORCS; 98956; 28 hits in 78 CRISPR screens.
DR ChiTaRS; Nat10; mouse.
DR PRO; PR:Q8K224; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K224; protein.
DR Bgee; ENSMUSG00000027185; Expressed in spermatocyte and 234 other tissues.
DR ExpressionAtlas; Q8K224; baseline and differential.
DR Genevisible; Q8K224; MM.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0106162; F:mRNA N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISO:MGI.
DR GO; GO:1990883; F:rRNA cytidine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:1904812; P:rRNA acetylation involved in maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03211; RNA_acetyltr_Nat10; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR007807; Helicase_dom.
DR InterPro; IPR033688; NAT10.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032672; TmcA/NAT10/Kre33.
DR InterPro; IPR013562; TmcA_N.
DR InterPro; IPR027992; tRNA_bind_dom.
DR PANTHER; PTHR10925; PTHR10925; 1.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 1.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF13725; tRNA_bind_2; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; ATP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; rRNA processing; Transferase;
KW tRNA processing.
FT CHAIN 1..1024
FT /note="RNA cytidine acetyltransferase"
FT /id="PRO_0000327480"
FT DOMAIN 558..753
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 702..1024
FT /note="Required for localization to the nucleolus and
FT midbody"
FT /evidence="ECO:0000250|UniProtKB:Q9H0A0"
FT REGION 990..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1024
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 629..631
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 636..642
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 725
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0A0"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0A0"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0A0"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0A0"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0A0"
FT CONFLICT 75..81
FT /note="QLQKKIK -> FSHNKIM (in Ref. 3; BAC35626)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="N -> Y (in Ref. 3; BAC35626)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="P -> S (in Ref. 3; BAE29107)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="D -> G (in Ref. 3; BAE29107)"
FT /evidence="ECO:0000305"
FT CONFLICT 865..904
FT /note="ALLLGIGLQHKSVDQLEKEIELPSGQLMGLFNRIIRKVVK -> VGHLGLHG
FT GQGRTVELL (in Ref. 4; BAC98237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1024 AA; 115419 MW; BB4DE75F6686C894 CRC64;
MNRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK ARPSVLWCYK
KELGFSSHRK KRMRQLQKKI KSGTLNLKQD DPFELFVAAT NIRYCYYNET HKILGNTFGM
CVLQDFEALT PNLLARTVET VEGGGLVVIL LRTMNSLKQL YTMTMDVHSR YRTEAHQDVV
GRFNERFILS LASCKKCLVI DDQLDILPIS SHVASIEALP PQAPDENLSP AALELLELKE
SLQDTQPVGV LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIVQSLNPE FNKAVIRVNV
FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS LLGPYLVFMA STINGYEGTG
RSLSLKLIQQ LRQQSAQSQV STTAENKTTT TARLASARTL HEVSLQESIR YAPGDAVEKW
LNDLLCLDCL NITRIVSGCP LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN
SPNDLQMLSD APAHHLFCLL PPVPPTQNAL PEVLAVVQVC LEGEISRQSI LNSLSRGKKA
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM YYEGKFPCLE
EKVLETPQEI RTVSSEAVSL LEEVITPRKD LPPLLLKLNE RPAERLDYLG VSYGLTPRLL
KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK TLADEDEAEQ GAWLAAFWKD FRRRFLALLS
YQFSTFSPAL SLNIIQNRNV AKSALPALGR EHLEALFLPY DLKRLEMYSR NMVDYHLIMD
LIPAISRLYF LNQLGDLSLS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR
KVVKLFNDVQ EKAIEEQMVA VKDVVMEPTM KTLSDDLDEA AKEFQEKHKK EVGKLKDMDL
SQYVIRGDDE EWNEVLSKAG QNASIVSLKS DKKRKLETKQ EPKQSKKLKK RDNNRKDMKL
KRKK
