ID FIRRM_HUMAN Reviewed; 853 AA. AC Q9NSG2; A6NFP1; B3KU42; Q3KNQ1; Q9H8L5; Q9NVJ0; DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 152. DE RecName: Full=FIGNL1-interacting regulator of recombination and mitosis {ECO:0000312|HGNC:HGNC:25565}; DE AltName: Full=FIDGETIN-like-1 interacting protein {ECO:0000303|PubMed:29608566}; DE Short=FLIP {ECO:0000303|PubMed:29608566}; DE AltName: Full=POLO1-associating protein {ECO:0000303|PubMed:34260926}; GN Name=FIRRM {ECO:0000312|HGNC:HGNC:25565}; GN Synonyms=APOLO1 {ECO:0000303|PubMed:34260926}, C1orf112; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Rhodes S., Huckle E.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain, Placenta, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Testis; 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 [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-792, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] RP SUBUNIT, AND INTERACTION WITH FIGL1. RX PubMed=29608566; DOI=10.1371/journal.pgen.1007317; RA Fernandes J.B., Duhamel M., Seguela-Arnaud M., Froger N., Girard C., RA Choinard S., Solier V., De Winne N., De Jaeger G., Gevaert K., Andrey P., RA Grelon M., Guerois R., Kumar R., Mercier R.; RT "FIGL1 and its novel partner FLIP form a conserved complex that regulates RT homologous recombination."; RL PLoS Genet. 14:e1007317-e1007317(2018). RN [10] RP FUNCTION, INTERACTION WITH PLK1 AND PPP1CC, SUBCELLULAR LOCATION, RP PHOSPHORYLATION AT SER-43 AND SER-744, AND MUTAGENESIS OF SER-43 AND RP SER-744. RX PubMed=34260926; DOI=10.1016/j.celrep.2021.109343; RA Xu L., Ali M., Duan W., Yuan X., Garba F., Mullen M., Sun B., Poser I., RA Duan H., Lu J., Tian R., Ge Y., Chu L., Pan W., Wang D., Hyman A., RA Green H., Li L., Dou Z., Liu D., Liu X., Yao X.; RT "Feedback control of PLK1 by Apolo1 ensures accurate chromosome RT segregation."; RL Cell Rep. 36:109343-109343(2021). CC -!- FUNCTION: Regulates PLK1 kinase activity at kinetochores and promotes CC faithful chromosome segregation in prometaphase by bridging kinase and CC phosphatase activities (PubMed:34260926). Phosphorylation of FIRRM by CC PLK1 negatively regulates its interaction with the phosphatase, PPP1CC, CC thus creating a negative feedback loop for maintaining proper PLK1 CC kinase activity during mitosis (PubMed:34260926). In complex with FIGL1 CC may regulate homologous recombination (PubMed:29608566). CC {ECO:0000269|PubMed:29608566, ECO:0000269|PubMed:34260926}. CC -!- SUBUNIT: Interacts (via its N-terminal region) with PLK1; controls PLK1 CC kinase activity (PubMed:34260926). Interacts (via the KVVXF motif) with CC PPP1CC; controls PLK1 kinase activity (PubMed:34260926). Interacts with CC FIGNL1; may regulate homologous recombination (PubMed:29608566). CC {ECO:0000269|PubMed:29608566, ECO:0000269|PubMed:34260926}. CC -!- INTERACTION: CC Q9NSG2; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-11128910, EBI-10181968; CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore CC {ECO:0000269|PubMed:34260926}. Nucleus {ECO:0000269|PubMed:34260926}. CC Chromosome, centromere {ECO:0000269|PubMed:34260926}. Midbody CC {ECO:0000269|PubMed:34260926}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:34260926}. Note=Exhibits cell-cycle-dependent CC distribution during mitosis. Detected in the nucleus in interphase. CC Colocalizes with PLK1 to the centromeres in a nearby prometaphase CC cells. Relocates to the central spindle in anaphase and to the midbody CC in telophase cells. {ECO:0000269|PubMed:34260926}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9NSG2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NSG2-2; Sequence=VSP_023445; CC Name=3; CC IsoId=Q9NSG2-3; Sequence=VSP_023444; CC -!- PTM: Phosphorylation at Ser-43 by PLK1 strengthens FIRRM-PLK1 CC interaction (PubMed:34260926). Phosphorylation at Ser-744 by PLK1 CC negatively regulates its interaction with PPP1CC (PubMed:34260926). CC {ECO:0000269|PubMed:34260926}. 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; AL354614; CAB89727.1; -; mRNA. DR EMBL; AK001568; BAA91761.1; -; mRNA. DR EMBL; AK023532; BAB14600.1; -; mRNA. DR EMBL; AK096493; BAG53304.1; -; mRNA. DR EMBL; AL021940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031297; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90863.1; -; Genomic_DNA. DR EMBL; BC091516; AAH91516.1; -; mRNA. DR EMBL; BC107168; AAI07169.1; -; mRNA. DR EMBL; BC107169; AAI07170.1; -; mRNA. DR CCDS; CCDS1285.1; -. [Q9NSG2-1] DR CCDS; CCDS86030.1; -. [Q9NSG2-3] DR RefSeq; NP_001306976.1; NM_001320047.1. [Q9NSG2-1] DR RefSeq; NP_001306977.1; NM_001320048.1. [Q9NSG2-2] DR RefSeq; NP_001306979.1; NM_001320050.1. DR RefSeq; NP_001306980.1; NM_001320051.1. DR RefSeq; NP_060656.2; NM_018186.3. DR RefSeq; XP_011508037.1; XM_011509735.2. DR RefSeq; XP_016857213.1; XM_017001724.1. DR RefSeq; XP_016857214.1; XM_017001725.1. DR AlphaFoldDB; Q9NSG2; -. DR BioGRID; 120851; 60. DR IntAct; Q9NSG2; 22. DR STRING; 9606.ENSP00000286031; -. DR iPTMnet; Q9NSG2; -. DR PhosphoSitePlus; Q9NSG2; -. DR BioMuta; C1orf112; -. DR DMDM; 74761679; -. DR EPD; Q9NSG2; -. DR jPOST; Q9NSG2; -. DR MassIVE; Q9NSG2; -. DR MaxQB; Q9NSG2; -. DR PaxDb; 9606-ENSP00000286031; -. DR PeptideAtlas; Q9NSG2; -. DR ProteomicsDB; 82548; -. [Q9NSG2-1] DR ProteomicsDB; 82549; -. [Q9NSG2-2] DR ProteomicsDB; 82550; -. [Q9NSG2-3] DR Pumba; Q9NSG2; -. DR Antibodypedia; 20545; 92 antibodies from 14 providers. DR DNASU; 55732; -. DR Ensembl; ENST00000286031.10; ENSP00000286031.6; ENSG00000000460.17. [Q9NSG2-1] DR Ensembl; ENST00000359326.9; ENSP00000352276.4; ENSG00000000460.17. [Q9NSG2-1] DR Ensembl; ENST00000413811.3; ENSP00000389257.3; ENSG00000000460.17. [Q9NSG2-3] DR GeneID; 55732; -. DR KEGG; hsa:55732; -. DR MANE-Select; ENST00000359326.9; ENSP00000352276.4; NM_001320047.2; NP_001306976.1. DR UCSC; uc001ggp.4; human. [Q9NSG2-1] DR AGR; HGNC:25565; -. DR CTD; 55732; -. DR DisGeNET; 55732; -. DR GeneCards; FIRRM; -. DR HGNC; HGNC:25565; FIRRM. DR HPA; ENSG00000000460; Tissue enhanced (parathyroid). DR neXtProt; NX_Q9NSG2; -. DR OpenTargets; ENSG00000000460; -. DR PharmGKB; PA142672496; -. DR VEuPathDB; HostDB:ENSG00000000460; -. DR eggNOG; ENOG502QQPV; Eukaryota. DR GeneTree; ENSGT00390000004791; -. DR HOGENOM; CLU_335441_0_0_1; -. DR InParanoid; Q9NSG2; -. DR OMA; PCVQQTF; -. DR OrthoDB; 3152308at2759; -. DR PhylomeDB; Q9NSG2; -. DR TreeFam; TF328571; -. DR PathwayCommons; Q9NSG2; -. DR SignaLink; Q9NSG2; -. DR BioGRID-ORCS; 55732; 26 hits in 1130 CRISPR screens. DR ChiTaRS; C1orf112; human. DR GenomeRNAi; 55732; -. DR Pharos; Q9NSG2; Tdark. DR PRO; PR:Q9NSG2; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NSG2; Protein. DR Bgee; ENSG00000000460; Expressed in primordial germ cell in gonad and 105 other cell types or tissues. DR ExpressionAtlas; Q9NSG2; baseline and differential. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0045859; P:regulation of protein kinase activity; IMP:UniProtKB. DR InterPro; IPR027902; DUF4487. DR PANTHER; PTHR16071; CHROMOSOME 1 OPEN READING FRAME 112; 1. DR PANTHER; PTHR16071:SF2; CHROMOSOME 1 OPEN READING FRAME 112; 1. DR Pfam; PF14868; DUF4487; 1. DR Genevisible; Q9NSG2; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Centromere; Chromosome; Cytoplasm; KW Cytoskeleton; Kinetochore; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..853 FT /note="FIGNL1-interacting regulator of recombination and FT mitosis" FT /id="PRO_0000279461" FT MOD_RES 43 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:34260926, FT ECO:0007744|PubMed:23186163" FT MOD_RES 744 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:34260926" FT MOD_RES 792 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..323 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_023444" FT VAR_SEQ 1..135 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023445" FT VARIANT 481 FT /note="A -> S (in dbSNP:rs2272920)" FT /id="VAR_030906" FT MUTAGEN 43 FT /note="S->A: Decreased binding to PLK1." FT /evidence="ECO:0000269|PubMed:34260926" FT MUTAGEN 43 FT /note="S->D: Increased binding to PLK1." FT /evidence="ECO:0000269|PubMed:34260926" FT MUTAGEN 744 FT /note="S->A: Does not affect binding to PPP1CC. Rescues the FT mitotic defects seen in FIRRM-depleted cells." FT /evidence="ECO:0000269|PubMed:34260926" FT MUTAGEN 744 FT /note="S->D: Decreased binding to PPP1CC. Does not rescue FT the mitotic defects seen in FIRRM-depleted cells." FT /evidence="ECO:0000269|PubMed:34260926" FT CONFLICT 594 FT /note="D -> G (in Ref. 2; BAB14600)" FT /evidence="ECO:0000305" FT CONFLICT 655 FT /note="S -> L (in Ref. 2; BAA91761)" FT /evidence="ECO:0000305" SQ SEQUENCE 853 AA; 96554 MW; E7FCA875C87052B1 CRC64; MFLPHMNHLT LEQTFFSQVL PKTVKLFDDM MYELTSQARG LSSQNLEIQT TLRNILQTMV QLLGALTGCV QHICATQESI ILENIQSLPS SVLHIIKSTF VHCKNSESVY SGCLHLVSDL LQALFKEAYS LQKQLMELLD MVCMDPLVDD NDDILNMVIV IHSLLDICSV ISSMDHAFHA NTWKFIIKQS LKHQSIIKSQ LKHKDIITSL CEDILFSFHS CLQLAEQMTQ SDAQDNADYR LFQKTLKLCR FFANSLLHYA KEFLPFLSDS CCTLHQLYLQ IHSKFPPSLY ATRISKAHQE EIAGAFLVTL DPLISQLLTF QPFMQVVLDS KLDLPCELQF PQCLLLVVVM DKLPSQPKEV QTLWCTDSQV SETTTRISLL KAVFYSFEQC SGELSLPVHL QGLKSKGKAE VAVTLYQHVC VHLCTFITSF HPSLFAELDA ALLNAVLSAN MITSLLAMDA WCFLARYGTA ELCAHHVTIV AHLIKSCPGE CYQLINLSIL LKRLFFFMAP PHQLEFIQKF SPKEAENLPL WQHISFQALP PELREQTVHE VTTVGTAECR KWLSRSRTLG ELESLNTVLS ALLAVCNSAG EALDTGKQTA IIEVVSQLWA FLNIKQVADQ PYVQQTFSLL LPLLGFFIQT LDPKLILQAV TLQTSLLKLE LPDYVRLAML DFVSSLGKLF IPEAIQDRIL PNLSCMFALL LADRSWLLEQ HTLEAFTQFA EGTNHEEIVP QCLSSEETKN KVVSFLEKTG FVDETEAAKV ERVKQEKGIF WEPFANVTVE EAKRSSLQPY AKRARQEFPW EEEYRSALHT IAGALEATES LLQKGPAPAW LSMEMEALQE RMDKLKRYIH TLG //