ID RADX_HUMAN Reviewed; 855 AA. AC Q6NSI4; H7BY89; Q4G0L7; Q5JQS1; Q5JRF9; Q6PHY5; Q6PII9; Q6PJU8; Q9H7W5; AC Q9NWA6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 147. DE RecName: Full=RPA-related protein RADX {ECO:0000305}; DE AltName: Full=RPA-related and RAD51-antagonist, X-chromosome {ECO:0000303|PubMed:28735897}; GN Name=RADX {ECO:0000303|PubMed:28735897, ECO:0000312|HGNC:HGNC:25486}; GN Synonyms=CXorf57 {ECO:0000312|HGNC:HGNC:25486}; 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] (ISOFORMS 2 AND 3). RC TISSUE=Embryo; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-593. RC TISSUE=Brain, Choriocarcinoma, and Leiomyosarcoma; 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-240; ARG-248; RP 252-LYS--LYS-256; TRP-279; LYS-304; ARG-310 AND GLU-327. RX PubMed=28735897; DOI=10.1016/j.molcel.2017.06.023; RA Dungrawala H., Bhat K.P., Le Meur R., Chazin W.J., Ding X., Sharan S.K., RA Wessel S.R., Sathe A.A., Zhao R., Cortez D.; RT "RADX promotes genome stability and modulates chemosensitivity by RT regulating RAD51 at replication forks."; RL Mol. Cell 67:374-386(2017). CC -!- FUNCTION: Single-stranded DNA-binding protein recruited to replication CC forks to maintain genome stability (PubMed:28735897). Prevents fork CC collapse by antagonizing the accumulation of RAD51 at forks to ensure CC the proper balance of fork remodeling and protection without CC interfering with the capacity of cells to complete homologous CC recombination of double-strand breaks (PubMed:28735897). CC {ECO:0000269|PubMed:28735897}. CC -!- INTERACTION: CC Q6NSI4; P40692: MLH1; NbExp=9; IntAct=EBI-8634209, EBI-744248; CC Q6NSI4; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-8634209, EBI-744342; CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:28735897}. CC Note=Recruited to replication forks. {ECO:0000269|PubMed:28735897}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6NSI4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6NSI4-2; Sequence=VSP_021182, VSP_021183; CC Name=3; CC IsoId=Q6NSI4-3; Sequence=VSP_044983, VSP_044984; CC Name=4; CC IsoId=Q6NSI4-4; Sequence=VSP_044984; 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; AK001040; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK024253; BAB14859.1; -; mRNA. DR EMBL; AL590808; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL606833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471120; EAX02740.1; -; Genomic_DNA. DR EMBL; BC011483; AAH11483.1; -; mRNA. DR EMBL; BC033709; AAH33709.1; -; mRNA. DR EMBL; BC054032; AAH54032.1; ALT_SEQ; mRNA. DR EMBL; BC070110; AAH70110.1; -; mRNA. DR CCDS; CCDS14519.1; -. [Q6NSI4-1] DR CCDS; CCDS55470.1; -. [Q6NSI4-4] DR RefSeq; NP_001171711.1; NM_001184782.1. [Q6NSI4-4] DR RefSeq; NP_060485.4; NM_018015.5. [Q6NSI4-1] DR PDB; 8U5Y; EM; 3.01 A; A/B/C=1-855. DR PDBsum; 8U5Y; -. DR AlphaFoldDB; Q6NSI4; -. DR EMDB; EMD-41939; -. DR SMR; Q6NSI4; -. DR BioGRID; 120400; 48. DR IntAct; Q6NSI4; 14. DR MINT; Q6NSI4; -. DR STRING; 9606.ENSP00000361628; -. DR GlyGen; Q6NSI4; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q6NSI4; -. DR MetOSite; Q6NSI4; -. DR PhosphoSitePlus; Q6NSI4; -. DR BioMuta; CXorf57; -. DR DMDM; 117949773; -. DR EPD; Q6NSI4; -. DR MassIVE; Q6NSI4; -. DR MaxQB; Q6NSI4; -. DR PaxDb; 9606-ENSP00000361628; -. DR PeptideAtlas; Q6NSI4; -. DR ProteomicsDB; 43542; -. DR ProteomicsDB; 66630; -. [Q6NSI4-1] DR ProteomicsDB; 66631; -. [Q6NSI4-2] DR Pumba; Q6NSI4; -. DR Antibodypedia; 348; 32 antibodies from 10 providers. DR DNASU; 55086; -. DR Ensembl; ENST00000372544.6; ENSP00000361623.2; ENSG00000147231.14. [Q6NSI4-4] DR Ensembl; ENST00000372548.9; ENSP00000361628.4; ENSG00000147231.14. [Q6NSI4-1] DR Ensembl; ENST00000461251.5; ENSP00000432238.1; ENSG00000147231.14. [Q6NSI4-2] DR GeneID; 55086; -. DR KEGG; hsa:55086; -. DR MANE-Select; ENST00000372548.9; ENSP00000361628.4; NM_018015.6; NP_060485.4. DR UCSC; uc004emi.5; human. [Q6NSI4-1] DR AGR; HGNC:25486; -. DR CTD; 55086; -. DR GeneCards; RADX; -. DR HGNC; HGNC:25486; RADX. DR HPA; ENSG00000147231; Tissue enhanced (brain, pituitary gland). DR neXtProt; NX_Q6NSI4; -. DR OpenTargets; ENSG00000147231; -. DR PharmGKB; PA145149058; -. DR VEuPathDB; HostDB:ENSG00000147231; -. DR eggNOG; ENOG502QSE7; Eukaryota. DR GeneTree; ENSGT00390000005094; -. DR HOGENOM; CLU_016770_0_0_1; -. DR InParanoid; Q6NSI4; -. DR OMA; TGCHKGQ; -. DR OrthoDB; 5346238at2759; -. DR PhylomeDB; Q6NSI4; -. DR TreeFam; TF331019; -. DR PathwayCommons; Q6NSI4; -. DR SignaLink; Q6NSI4; -. DR BioGRID-ORCS; 55086; 30 hits in 757 CRISPR screens. DR ChiTaRS; CXorf57; human. DR GenomeRNAi; 55086; -. DR Pharos; Q6NSI4; Tdark. DR PRO; PR:Q6NSI4; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q6NSI4; Protein. DR Bgee; ENSG00000147231; Expressed in pituitary gland and 123 other cell types or tissues. DR ExpressionAtlas; Q6NSI4; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005657; C:replication fork; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR040893; RADX. DR PANTHER; PTHR14944; RPA-RELATED PROTEIN RADX; 1. DR PANTHER; PTHR14944:SF2; RPA-RELATED PROTEIN RADX; 1. DR Pfam; PF17659; DUF5521; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2. DR Genevisible; Q6NSI4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; DNA-binding; KW Reference proteome. FT CHAIN 1..855 FT /note="RPA-related protein RADX" FT /id="PRO_0000254127" FT DNA_BIND 228..331 FT /note="OB" FT /evidence="ECO:0000305|PubMed:28735897" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 570..608 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 570..592 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..225 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044983" FT VAR_SEQ 482..578 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044984" FT VAR_SEQ 525..567 FT /note="VESLLTAISEVRKEIEDLQYREQKRIAIQGIITAIKYIPHSSA -> GTNVI FT ASPSKYVYILYVWLMLFQLVIFILFFYGSDLKFSNIHR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_021182" FT VAR_SEQ 568..855 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_021183" FT VARIANT 593 FT /note="I -> M (in dbSNP:rs5962707)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_028816" FT MUTAGEN 240 FT /note="R->E: Decreased binding to single-stranded DNA; when FT associated with E-248; 252-E--E-256; A-279; E-304; E-310 FT and A-327." FT /evidence="ECO:0000269|PubMed:28735897" FT MUTAGEN 248 FT /note="R->E: Decreased binding to single-stranded DNA; when FT associated with E-240; 252-E--E-256; A-279; E-304; E-310 FT and A-327." FT /evidence="ECO:0000269|PubMed:28735897" FT MUTAGEN 252..256 FT /note="KPDKK->EPDEE: Decreased binding to single-stranded FT DNA; when associated with E-240; E-248; A-279; E-304; E-310 FT and A-327." FT /evidence="ECO:0000269|PubMed:28735897" FT MUTAGEN 279 FT /note="W->A: Decreased binding to single-stranded DNA; when FT associated with E-240; E-248; 252-E--E-256; E-304; E-310 FT and A-327." FT /evidence="ECO:0000269|PubMed:28735897" FT MUTAGEN 304 FT /note="K->E: Decreased binding to single-stranded DNA; when FT associated with E-240; E-248; 252-E--E-256; A-279; E-310 FT and A-327." FT /evidence="ECO:0000269|PubMed:28735897" FT MUTAGEN 310 FT /note="R->E: Decreased binding to single-stranded DNA; when FT associated with E-240; E-248; 252-E--E-256; A-279; E-304 FT and A-327." FT /evidence="ECO:0000269|PubMed:28735897" FT MUTAGEN 327 FT /note="E->A: Decreased binding to single-stranded DNA; when FT associated with E-240; E-248; 252-E--E-256; A-279; E-304 FT and E-310." FT /evidence="ECO:0000269|PubMed:28735897" FT CONFLICT 29 FT /note="V -> A (in Ref. 1; AK001040)" FT /evidence="ECO:0000305" FT CONFLICT 33 FT /note="V -> L (in Ref. 4; AAH70110)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="K -> E (in Ref. 4; AAH11483)" FT /evidence="ECO:0000305" FT CONFLICT 394 FT /note="E -> K (in Ref. 4; AAH54032)" FT /evidence="ECO:0000305" FT CONFLICT 674 FT /note="K -> N (in Ref. 1; BAB14859)" FT /evidence="ECO:0000305" SQ SEQUENCE 855 AA; 97554 MW; 31EE2E17E7D9BF47 CRC64; MSGESGQPEA GPSHAGLDWP NPERNRAGVP GGVIRRAGSQ GPRSWIQKVL EQIMDSPRQC VTPSEVVPVT VLAVQRYLLE DEPRDTVPKP PLYCYDVTIS DGVYQEKCYL DPSLNSLVYQ NILKVGIQMR ISRVSCLYNE KRIGQGILCI DNVHCGETSD SISLETPFRN RAHQEKPERP LRGGKSHYLA LWNNEDPYGD IWLTDKQPEE HNFSDTKIIS LSHLEMTWTN RRNFPALLVR ILHKSKLRYY GKPDKKMIEP YQTFLEVADS SGTVSVIMWN ALCPEWYKSL RVGLVLLLQD YSVKKSYPFR IQPVPVDPQI KLISTMEICL NLRDPPTNII IIPEKQVKPE WRLPKLNHRF TTRSELDDMP ENCICDVIGL LVFVGRVQRS KKKENREDFW SYRWIHIADG TSEQPFIVEL FSTSQPEIFE NIYPMAYFVC TQLKVVRNDN QVPKLLYLTT TNESGVFITG HRGQPYTYDA KVKNFIQWIR TKSDSGEQKN MVIGGYYPYP PVPETFSKYS SSIKVESLLT AISEVRKEIE DLQYREQKRI AIQGIITAIK YIPHSSATES ASASETLRNA NRPSTSQAAR VEIQERNGKR HQDDEPVNSQ YFQTTSTNLS LSNKIRILQG PHANPVAVPQ PGASVQTKGI KPGMPSIFNR RANINANLQG KARKTISDRW ESQLWREKKF GLIDHLHYSR VYPESIPRKF MFEHRKFLSD QYNSQPAKYV PPEGRPPKLD DFKSARSLGH FEVTILGLNH EIAIDVAFLP MYCPEDIRTS QIDTLLTSMN YSCAYPQDTT GNDRLPGPRA VAGDIIKAAT ELDRVHIVGI LDICNLGNNK VEVYLHKIYS PENTS //