RHG25_HUMAN
ID RHG25_HUMAN Reviewed; 645 AA.
AC P42331; A8K2Y1; B7Z498; E9PFQ7; G5E9G2; Q8IXQ2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Rho GTPase-activating protein 25;
DE AltName: Full=Rho-type GTPase-activating protein 25;
GN Name=ARHGAP25; Synonyms=KIAA0053;
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 3).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANTS
RP SER-555 AND THR-556.
RC TISSUE=Umbilical cord blood;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Blood;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP STRUCTURE BY NMR OF 47-151.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the pleckstrin homology domain of human KIAA0053
RT protein.";
RL Submitted (JUN-2004) to the PDB data bank.
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- INTERACTION:
CC P42331-2; P40227: CCT6A; NbExp=3; IntAct=EBI-21499901, EBI-356687;
CC P42331-2; Q6ZTQ4: CDHR3; NbExp=3; IntAct=EBI-21499901, EBI-12143631;
CC P42331-2; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-21499901, EBI-6447163;
CC P42331-2; P45880: VDAC2; NbExp=3; IntAct=EBI-21499901, EBI-354022;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P42331-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42331-2; Sequence=VSP_037345, VSP_010275, VSP_010276;
CC Name=3;
CC IsoId=P42331-3; Sequence=VSP_037345;
CC Name=4;
CC IsoId=P42331-4; Sequence=VSP_010275;
CC Name=5;
CC IsoId=P42331-5; Sequence=VSP_045391;
CC Name=6;
CC IsoId=P42331-6; Sequence=VSP_037345, VSP_010275;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06125.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D29642; BAA06125.2; ALT_INIT; mRNA.
DR EMBL; AK290396; BAF83085.1; -; mRNA.
DR EMBL; AK297056; BAH12484.1; -; mRNA.
DR EMBL; AC097495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99866.1; -; Genomic_DNA.
DR EMBL; BC039591; AAH39591.1; -; mRNA.
DR CCDS; CCDS33214.2; -. [P42331-4]
DR CCDS; CCDS46312.1; -. [P42331-3]
DR CCDS; CCDS54363.1; -. [P42331-5]
DR CCDS; CCDS54364.1; -. [P42331-6]
DR PIR; C59430; C59430.
DR RefSeq; NP_001007232.2; NM_001007231.2. [P42331-4]
DR RefSeq; NP_001159748.1; NM_001166276.1. [P42331-6]
DR RefSeq; NP_001159749.1; NM_001166277.1. [P42331-5]
DR RefSeq; NP_055697.1; NM_014882.2. [P42331-3]
DR RefSeq; XP_005264732.1; XM_005264675.2.
DR PDB; 1V89; NMR; -; A=47-151.
DR PDBsum; 1V89; -.
DR AlphaFoldDB; P42331; -.
DR SMR; P42331; -.
DR BioGRID; 115264; 48.
DR IntAct; P42331; 25.
DR MINT; P42331; -.
DR STRING; 9606.ENSP00000386911; -.
DR CarbonylDB; P42331; -.
DR GlyGen; P42331; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P42331; -.
DR PhosphoSitePlus; P42331; -.
DR BioMuta; ARHGAP25; -.
DR DMDM; 238054314; -.
DR EPD; P42331; -.
DR jPOST; P42331; -.
DR MassIVE; P42331; -.
DR MaxQB; P42331; -.
DR PaxDb; P42331; -.
DR PeptideAtlas; P42331; -.
DR PRIDE; P42331; -.
DR ProteomicsDB; 20155; -.
DR ProteomicsDB; 33928; -.
DR ProteomicsDB; 55505; -. [P42331-1]
DR ProteomicsDB; 55506; -. [P42331-2]
DR ProteomicsDB; 55507; -. [P42331-3]
DR ProteomicsDB; 55508; -. [P42331-4]
DR Antibodypedia; 30948; 430 antibodies from 27 providers.
DR DNASU; 9938; -.
DR Ensembl; ENST00000409030.7; ENSP00000386863.3; ENSG00000163219.12. [P42331-3]
DR Ensembl; ENST00000409202.8; ENSP00000386911.3; ENSG00000163219.12. [P42331-4]
DR Ensembl; ENST00000409220.5; ENSP00000386241.1; ENSG00000163219.12. [P42331-6]
DR Ensembl; ENST00000467265.5; ENSP00000420583.1; ENSG00000163219.12. [P42331-5]
DR Ensembl; ENST00000497079.5; ENSP00000417139.1; ENSG00000163219.12. [P42331-2]
DR GeneID; 9938; -.
DR KEGG; hsa:9938; -.
DR MANE-Select; ENST00000409202.8; ENSP00000386911.3; NM_001007231.3; NP_001007232.2. [P42331-4]
DR UCSC; uc002sev.4; human. [P42331-1]
DR CTD; 9938; -.
DR DisGeNET; 9938; -.
DR GeneCards; ARHGAP25; -.
DR HGNC; HGNC:28951; ARHGAP25.
DR HPA; ENSG00000163219; Tissue enhanced (lymphoid).
DR MIM; 610587; gene.
DR neXtProt; NX_P42331; -.
DR OpenTargets; ENSG00000163219; -.
DR PharmGKB; PA134941737; -.
DR VEuPathDB; HostDB:ENSG00000163219; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR HOGENOM; CLU_020795_1_0_1; -.
DR InParanoid; P42331; -.
DR OMA; NWDFNLR; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; P42331; -.
DR TreeFam; TF323577; -.
DR PathwayCommons; P42331; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; P42331; -.
DR BioGRID-ORCS; 9938; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; ARHGAP25; human.
DR EvolutionaryTrace; P42331; -.
DR GenomeRNAi; 9938; -.
DR Pharos; P42331; Tbio.
DR PRO; PR:P42331; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P42331; protein.
DR Bgee; ENSG00000163219; Expressed in granulocyte and 153 other tissues.
DR ExpressionAtlas; P42331; baseline and differential.
DR Genevisible; P42331; HS.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..645
FT /note="Rho GTPase-activating protein 25"
FT /id="PRO_0000056716"
FT DOMAIN 46..151
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 159..353
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 355..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 541..644
FT /evidence="ECO:0000255"
FT COMPBIAS 391..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYW1"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYW1"
FT VAR_SEQ 1..19
FT /note="MSLKLPRNWDFNLKVEAAK -> MSLGQSACLFLS (in isoform 2,
FT isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7584044"
FT /id="VSP_037345"
FT VAR_SEQ 117..155
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045391"
FT VAR_SEQ 155
FT /note="G -> GA (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010275"
FT VAR_SEQ 400..645
FT /note="TSDSDTTSPTGQQPSDAFPEDSSKVPREKPGDWKMQSRKRTQTLPNRKCFLT
FT SAFQGANSSKMEIFKNEFWSPSSEAKAGEGHRRTMSQDLRQLSDSQRTSTYDNVPSLPG
FT SPGEEASALSSQACDSKGDTLASPNSETGPGKKNSGEEEIDSLQRMVQELRKEIETQKQ
FT MYEEQIKNLEKENYDVWAKVVRLNEELEKEKKKSAALEISLRNMERSREDVEKRNKALE
FT EEVKEFVKSMKEPKTEA -> VRCREPSCFHWVLPLVQAIPCKACSRVAIWGVLGDAVA
FT VGAAATDSSEHTLKAWPLSKSSFYWHL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010276"
FT VARIANT 192
FT /note="R -> W (in dbSNP:rs3749130)"
FT /id="VAR_049142"
FT VARIANT 555
FT /note="R -> S (in dbSNP:rs4241344)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049143"
FT VARIANT 556
FT /note="M -> T (in dbSNP:rs10177248)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049144"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1V89"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1V89"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:1V89"
SQ SEQUENCE 645 AA; 73435 MW; 3D54323CA5571754 CRC64;
MSLKLPRNWD FNLKVEAAKI ARSRSVMTGE QMAAFHPSST PNPLERPIKM GWLKKQRSIV
KNWQQRYFVL RAQQLYYYKD EEDTKPQGCM YLPGCTIKEI ATNPEEAGKF VFEIIPASWD
QNRMGQDSYV LMASSQAEME EWVKFLRRVA GTPCGVFGQR LDETVAYEQK FGPHLVPILV
EKCAEFILEH GRNEEGIFRL PGQDNLVKQL RDAFDAGERP SFDRDTDVHT VASLLKLYLR
DLPEPVVPWS QYEGFLLCGQ LTNADEAKAQ QELMKQLSIL PRDNYSLLSY ICRFLHEIQL
NCAVNKMSVD NLATVIGVNL IRSKVEDPAV IMRGTPQIQR VMTMMIRDHE VLFPKSKDIP
LSPPAQKNDP KKAPVARSSV GWDATEDLRI SRTDSFSSMT SDSDTTSPTG QQPSDAFPED
SSKVPREKPG DWKMQSRKRT QTLPNRKCFL TSAFQGANSS KMEIFKNEFW SPSSEAKAGE
GHRRTMSQDL RQLSDSQRTS TYDNVPSLPG SPGEEASALS SQACDSKGDT LASPNSETGP
GKKNSGEEEI DSLQRMVQEL RKEIETQKQM YEEQIKNLEK ENYDVWAKVV RLNEELEKEK
KKSAALEISL RNMERSREDV EKRNKALEEE VKEFVKSMKE PKTEA
