ID RN207_HUMAN Reviewed; 634 AA. AC Q6ZRF8; A2VCM8; B4DFR6; Q5TGS6; Q6ZS63; Q96MP2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=RING finger protein 207; GN Name=RNF207; Synonyms=C1orf188; 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; 3 AND 4), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-634 (ISOFORM 1). RC TISSUE=Amygdala, Brain, Teratocarcinoma, and Thymus; 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=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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). 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 [4] RP ASSOCIATION WITH QT INTERVAL VARIANCE. RX PubMed=19305408; DOI=10.1038/ng.364; RA Newton-Cheh C., Eijgelsheim M., Rice K.M., de Bakker P.I., Yin X., RA Estrada K., Bis J.C., Marciante K., Rivadeneira F., Noseworthy P.A., RA Sotoodehnia N., Smith N.L., Rotter J.I., Kors J.A., Witteman J.C., RA Hofman A., Heckbert S.R., O'Donnell C.J., Uitterlinden A.G., Psaty B.M., RA Lumley T., Larson M.G., Stricker B.H.; RT "Common variants at ten loci influence QT interval duration in the QTGEN RT Study."; RL Nat. Genet. 41:399-406(2009). RN [5] RP ASSOCIATION WITH QT INTERVAL VARIANCE, AND VARIANTS SER-573 AND ALA-603. RX PubMed=19305409; DOI=10.1038/ng.362; RA Pfeufer A., Sanna S., Arking D.E., Muller M., Gateva V., Fuchsberger C., RA Ehret G.B., Orru M., Pattaro C., Kottgen A., Perz S., Usala G., RA Barbalic M., Li M., Putz B., Scuteri A., Prineas R.J., Sinner M.F., RA Gieger C., Najjar S.S., Kao W.H., Muhleisen T.W., Dei M., Happle C., RA Mohlenkamp S., Crisponi L., Erbel R., Jockel K.H., Naitza S., Steinbeck G., RA Marroni F., Hicks A.A., Lakatta E., Muller-Myhsok B., Pramstaller P.P., RA Wichmann H.E., Schlessinger D., Boerwinkle E., Meitinger T., Uda M., RA Coresh J., Kaab S., Abecasis G.R., Chakravarti A.; RT "Common variants at ten loci modulate the QT interval duration in the QTSCD RT Study."; RL Nat. Genet. 41:407-414(2009). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT ALA-603, RP INTERACTION WITH DNAJA1; HSPA1A; HSPA8 AND KCNH2, AUTOUBIQUITINATION, AND RP MUTAGENESIS OF CYS-25. RX PubMed=25281747; DOI=10.1074/jbc.m114.592295; RA Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E., RA Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.; RT "RING finger protein RNF207, a novel regulator of cardiac excitation."; RL J. Biol. Chem. 289:33730-33740(2014). CC -!- FUNCTION: Plays a role in cardiac repolarization possibly by CC stabilizing membrane expression of the potassium channel KCNH2/HERG, or CC by assisting its synthesis, folding or export from the endoplasmic CC reticulum, in a heat shock protein-dependent manner. CC {ECO:0000269|PubMed:25281747}. CC -!- SUBUNIT: Interacts with the core-glycosylated, but not the fully CC glycosylated form of KCNH2/HERG. Interacts with DNAJA1 and HSPA8. CC Interacts (via the C-terminus) with HSPA1A; this interaction additively CC increases KCNH2 expression. {ECO:0000269|PubMed:25281747}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25281747}. CC Note=Probably located in the endoplasmic reticulum and/or possibly the CC cis-Golgi apparatus. {ECO:0000269|PubMed:25281747}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6ZRF8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6ZRF8-2; Sequence=VSP_027863, VSP_027864; CC Name=3; CC IsoId=Q6ZRF8-3; Sequence=VSP_028439, VSP_028440, VSP_028441; CC Name=4; CC IsoId=Q6ZRF8-4; Sequence=VSP_028439, VSP_028442, VSP_028443; CC -!- POLYMORPHISM: Genetic variation in RNF207 may influence the duration of CC QT interval, a mesure of cardiac repolarization that depends on CC multiple environmental and genetic contributors. Prolonged or shortened CC QT intervals predisposes to ventricular arrhythmias and are a risk CC factor for sudden cardiac death. CC -!- SEQUENCE CAUTION: CC Sequence=AAI28238.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AK056658; BAB71243.1; -; mRNA. DR EMBL; AK127700; BAC87091.1; -; mRNA. DR EMBL; AK128246; BAC87352.1; -; mRNA. DR EMBL; AK294223; BAG57527.1; -; mRNA. DR EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC119780; AAI19781.1; -; mRNA. DR EMBL; BC128237; AAI28238.1; ALT_INIT; mRNA. DR CCDS; CCDS59.2; -. [Q6ZRF8-1] DR RefSeq; NP_997279.2; NM_207396.2. [Q6ZRF8-1] DR AlphaFoldDB; Q6ZRF8; -. DR SMR; Q6ZRF8; -. DR BioGRID; 132764; 384. DR STRING; 9606.ENSP00000367173; -. DR iPTMnet; Q6ZRF8; -. DR PhosphoSitePlus; Q6ZRF8; -. DR BioMuta; RNF207; -. DR DMDM; 158563957; -. DR jPOST; Q6ZRF8; -. DR MassIVE; Q6ZRF8; -. DR PaxDb; 9606-ENSP00000367173; -. DR PeptideAtlas; Q6ZRF8; -. DR ProteomicsDB; 68123; -. [Q6ZRF8-1] DR ProteomicsDB; 68126; -. [Q6ZRF8-4] DR Antibodypedia; 27241; 134 antibodies from 18 providers. DR DNASU; 388591; -. DR Ensembl; ENST00000377939.5; ENSP00000367173.4; ENSG00000158286.13. [Q6ZRF8-1] DR GeneID; 388591; -. DR KEGG; hsa:388591; -. DR MANE-Select; ENST00000377939.5; ENSP00000367173.4; NM_207396.3; NP_997279.2. DR UCSC; uc001amg.4; human. [Q6ZRF8-1] DR AGR; HGNC:32947; -. DR CTD; 388591; -. DR DisGeNET; 388591; -. DR GeneCards; RNF207; -. DR HGNC; HGNC:32947; RNF207. DR HPA; ENSG00000158286; Tissue enhanced (heart). DR MIM; 616923; gene. DR neXtProt; NX_Q6ZRF8; -. DR OpenTargets; ENSG00000158286; -. DR PharmGKB; PA145148144; -. DR VEuPathDB; HostDB:ENSG00000158286; -. DR eggNOG; KOG4367; Eukaryota. DR GeneTree; ENSGT00510000048612; -. DR HOGENOM; CLU_034912_0_0_1; -. DR InParanoid; Q6ZRF8; -. DR OMA; YEDSYRH; -. DR OrthoDB; 2878026at2759; -. DR PhylomeDB; Q6ZRF8; -. DR TreeFam; TF318184; -. DR PathwayCommons; Q6ZRF8; -. DR SIGNOR; Q6ZRF8; -. DR BioGRID-ORCS; 388591; 16 hits in 1191 CRISPR screens. DR ChiTaRS; RNF207; human. DR GenomeRNAi; 388591; -. DR Pharos; Q6ZRF8; Tbio. DR PRO; PR:Q6ZRF8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q6ZRF8; Protein. DR Bgee; ENSG00000158286; Expressed in apex of heart and 131 other cell types or tissues. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:BHF-UCL. DR GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0086019; P:cell-cell signaling involved in cardiac conduction; ISS:BHF-UCL. DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IGI:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:1903954; P:positive regulation of voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISS:BHF-UCL. DR GO; GO:1903762; P:positive regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:BHF-UCL. DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISS:BHF-UCL. DR GO; GO:1901207; P:regulation of heart looping; ISS:BHF-UCL. DR CDD; cd19814; Bbox1_RNF207-like; 1. DR CDD; cd16558; RING-HC_RNF207; 1. DR Gene3D; 1.20.58.1540; Actin interacting protein 3, C-terminal domain; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR039320; RNF207. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR22635:SF0; RING FINGER PROTEIN 207; 1. DR PANTHER; PTHR22635; UNCHARACTERIZED; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q6ZRF8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; KW Reference proteome; Zinc; Zinc-finger. FT CHAIN 1..634 FT /note="RING finger protein 207" FT /id="PRO_0000300809" FT ZN_FING 25..64 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 93..145 FT /note="B box-type; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT REGION 552..634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 422..457 FT /evidence="ECO:0000255" FT COILED 494..518 FT /evidence="ECO:0000255" FT COMPBIAS 557..580 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 609..634 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT VAR_SEQ 1..227 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_028439" FT VAR_SEQ 109..244 FT /note="DVETTYFCNTCGQPLCARCRDETHRARMFARHDIVALGQRSRDVPQKCTLHA FT EPYLLFSTDKKLLLCIRCFRDMQKESRAHCVDLESAYVQGCERLEQAVLAVKALQTATR FT EAIALLQAMVEEVRHSAAEEEDAIH -> AGAAGRVGEEQRVPGCTVPNACTCTQHVFR FT GRPGSGFSSTSLGHLGPKCEPHYTGGETEVQNKGLEPVSRQWQRLRPFDLGRAHWSPIQ FT GGVVDLHRRGSPVCRPGPTLKGLCYPSGIEAATAQGRWGQHAVPSGL (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_027863" FT VAR_SEQ 245..634 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_027864" FT VAR_SEQ 315..371 FT /note="ELMERLQGIVTRPHHLRPIQSSKIASDHRAEFARCLEPLLLLGPRRVAAAAS FT GANTL -> AGRGLRPQGADGAPLPLPSRKDVGVTRPKAHAAPVHQHQGAAGGGREHAL FT RRALPPL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_028440" FT VAR_SEQ 372..634 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_028441" FT VAR_SEQ 512..519 FT /note="AQLHDLLQ -> GSRQLAAE (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_028442" FT VAR_SEQ 520..634 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_028443" FT VARIANT 421 FT /note="A -> T (in dbSNP:rs12073329)" FT /id="VAR_052112" FT VARIANT 539 FT /note="R -> C (in dbSNP:rs55823245)" FT /id="VAR_061818" FT VARIANT 573 FT /note="N -> S (in dbSNP:rs709209)" FT /evidence="ECO:0000269|PubMed:19305409" FT /id="VAR_052113" FT VARIANT 603 FT /note="G -> A (associated with prolonged QT interval in FT heart's electrical cycle; behaves like wild-type in terms FT of protein expression, subcellular location and shortening FT of heart's action potential duration, when expressed in FT neonatal rabbit cardiomyocytes; dbSNP:rs846111)" FT /evidence="ECO:0000269|PubMed:19305409, FT ECO:0000269|PubMed:25281747" FT /id="VAR_052114" FT MUTAGEN 25 FT /note="C->R: Loss of KCNH2 up-regulation." FT /evidence="ECO:0000269|PubMed:25281747" FT CONFLICT 309 FT /note="F -> L (in Ref. 1; BAB71243)" FT /evidence="ECO:0000305" SQ SEQUENCE 634 AA; 70861 MW; A434507E22D45AFF CRC64; MSGAIFGPLE GPSSLDAPSI HPLVCPLCHV QYERPCLLDC FHDFCAGCLR GRATDGRLTC PLCQHQTVLK GPSGLPPVDR LLQFLVDSSG DGVEAVRCAN CDLECSEQDV ETTYFCNTCG QPLCARCRDE THRARMFARH DIVALGQRSR DVPQKCTLHA EPYLLFSTDK KLLLCIRCFR DMQKESRAHC VDLESAYVQG CERLEQAVLA VKALQTATRE AIALLQAMVE EVRHSAAEEE DAIHALFGSM QDRLAERKAL LLQAVQSQYE EKDKAFKEQL SHLATLLPTL QVHLVICSSF LSLANKAEFL DLGYELMERL QGIVTRPHHL RPIQSSKIAS DHRAEFARCL EPLLLLGPRR VAAAASGANT LAGGLGPKAL TGPHCPSPVG KMSGSPVQKP TLHRSISTKV LLAEGENTPF AEHCRHYEDS YRHLQAEMQS LKDQVQELHR DLTKHHSLIK AEIMGDVLHK SLQLDVQIAS EHASLEGMRV VFQEIWEEAY QRVANEQEIY EAQLHDLLQL RQENAYLTTI TKQITPYVRS IAKVKERLEP RFQAPVDEQS ESLQNTHDDS RNNAASARNN PGSVPEKREK TSEPKGNSWA PNGLSEEPLL KNMDHHRSKQ KNGGDVPTWR EHPT //