KCNH5_HUMAN
ID KCNH5_HUMAN Reviewed; 988 AA.
AC Q8NCM2; C9JP98;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 5;
DE AltName: Full=Ether-a-go-go potassium channel 2;
DE Short=hEAG2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv10.2;
GN Name=KCNH5; Synonyms=EAG2;
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 [MRNA] (ISOFORM 1), AND VARIANT THR-745.
RC TISSUE=Brain;
RX PubMed=11943152; DOI=10.1016/s0014-5793(02)02365-7;
RA Schoenherr R., Gessner G., Loeber K., Heinemann S.H.;
RT "Functional distinction of human EAG1 and EAG2 potassium channels.";
RL FEBS Lett. 514:204-208(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT THR-745.
RC TISSUE=Fetal brain;
RX PubMed=12135768; DOI=10.1016/s0014-5793(02)03055-7;
RA Ju M., Wray D.;
RT "Molecular identification and characterisation of the human eag2 potassium
RT channel.";
RL FEBS Lett. 524:204-210(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-745.
RC TISSUE=PNS;
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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-785, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18655026; DOI=10.1002/pmic.200700887;
RA Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J.,
RA Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
RT "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell
RT line Chang liver cells.";
RL Proteomics 8:2885-2896(2008).
RN [8]
RP VARIANT HIS-327.
RX PubMed=23647072; DOI=10.1111/epi.12201;
RA Veeramah K.R., Johnstone L., Karafet T.M., Wolf D., Sprissler R.,
RA Salogiannis J., Barth-Maron A., Greenberg M.E., Stuhlmann T., Weinert S.,
RA Jentsch T.J., Pazzi M., Restifo L.L., Talwar D., Erickson R.P.,
RA Hammer M.F.;
RT "Exome sequencing reveals new causal mutations in children with epileptic
RT encephalopathies.";
RL Epilepsia 54:1270-1281(2013).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Elicits a non-inactivating outward rectifying current. Channel
CC properties may be modulated by cAMP and subunit assembly.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits. Heteromultimer with KCNH1/EAG
CC (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q8NCM2-1; Sequence=Displayed;
CC Name=2; Synonyms=2b;
CC IsoId=Q8NCM2-2; Sequence=VSP_000973, VSP_000974;
CC Name=3;
CC IsoId=Q8NCM2-3; Sequence=VSP_000972, VSP_000975, VSP_000976;
CC -!- TISSUE SPECIFICITY: Detected in brain, skeletal muscle, heart,
CC placenta, lung and liver, and at low levels in kidney.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC
CC 1.A.1.20) subfamily. Kv10.2/KCNH5 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11016.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF418206; AAM28435.1; -; mRNA.
DR EMBL; AF472412; AAM49565.1; -; mRNA.
DR EMBL; AF493798; AAM49574.1; -; mRNA.
DR EMBL; AK074484; BAC11016.1; ALT_SEQ; mRNA.
DR EMBL; AL109985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80819.1; -; Genomic_DNA.
DR EMBL; BC073979; AAH73979.1; -; mRNA.
DR CCDS; CCDS45122.1; -. [Q8NCM2-2]
DR CCDS; CCDS9756.1; -. [Q8NCM2-1]
DR RefSeq; NP_647479.2; NM_139318.4. [Q8NCM2-1]
DR RefSeq; NP_758963.1; NM_172375.2. [Q8NCM2-2]
DR AlphaFoldDB; Q8NCM2; -.
DR SMR; Q8NCM2; -.
DR BioGRID; 118024; 7.
DR IntAct; Q8NCM2; 2.
DR STRING; 9606.ENSP00000321427; -.
DR ChEMBL; CHEMBL2362996; -.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q8NCM2; -.
DR GuidetoPHARMACOLOGY; 571; -.
DR TCDB; 1.A.1.20.9; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q8NCM2; 1 site.
DR iPTMnet; Q8NCM2; -.
DR PhosphoSitePlus; Q8NCM2; -.
DR BioMuta; KCNH5; -.
DR DMDM; 334302891; -.
DR MassIVE; Q8NCM2; -.
DR PaxDb; Q8NCM2; -.
DR PeptideAtlas; Q8NCM2; -.
DR PRIDE; Q8NCM2; -.
DR Antibodypedia; 11594; 60 antibodies from 18 providers.
DR DNASU; 27133; -.
DR Ensembl; ENST00000322893.12; ENSP00000321427.7; ENSG00000140015.20. [Q8NCM2-1]
DR Ensembl; ENST00000394968.2; ENSP00000378419.1; ENSG00000140015.20. [Q8NCM2-3]
DR Ensembl; ENST00000420622.6; ENSP00000395439.2; ENSG00000140015.20. [Q8NCM2-2]
DR GeneID; 27133; -.
DR KEGG; hsa:27133; -.
DR MANE-Select; ENST00000322893.12; ENSP00000321427.7; NM_139318.5; NP_647479.2.
DR UCSC; uc001xfx.5; human. [Q8NCM2-1]
DR CTD; 27133; -.
DR DisGeNET; 27133; -.
DR GeneCards; KCNH5; -.
DR HGNC; HGNC:6254; KCNH5.
DR HPA; ENSG00000140015; Group enriched (brain, retina).
DR MalaCards; KCNH5; -.
DR MIM; 605716; gene.
DR neXtProt; NX_Q8NCM2; -.
DR OpenTargets; ENSG00000140015; -.
DR PharmGKB; PA30040; -.
DR VEuPathDB; HostDB:ENSG00000140015; -.
DR eggNOG; KOG0501; Eukaryota.
DR GeneTree; ENSGT00940000156540; -.
DR HOGENOM; CLU_005746_3_1_1; -.
DR InParanoid; Q8NCM2; -.
DR OMA; EKKEEWN; -.
DR OrthoDB; 464006at2759; -.
DR PhylomeDB; Q8NCM2; -.
DR TreeFam; TF313130; -.
DR PathwayCommons; Q8NCM2; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; Q8NCM2; -.
DR BioGRID-ORCS; 27133; 21 hits in 1071 CRISPR screens.
DR ChiTaRS; KCNH5; human.
DR GeneWiki; KCNH5; -.
DR GenomeRNAi; 27133; -.
DR Pharos; Q8NCM2; Tclin.
DR PRO; PR:Q8NCM2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8NCM2; protein.
DR Bgee; ENSG00000140015; Expressed in buccal mucosa cell and 60 other tissues.
DR Genevisible; Q8NCM2; HS.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR030171; EAG2.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR10217:SF533; PTHR10217:SF533; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01464; EAGCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50113; PAC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Glycoprotein; Ion channel;
KW Ion transport; Isopeptide bond; Membrane; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..988
FT /note="Potassium voltage-gated channel subfamily H member
FT 5"
FT /id="PRO_0000054010"
FT TOPO_DOM 1..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 420..440
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 12..90
FT /note="PAS"
FT DOMAIN 91..143
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT REGION 704..715
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 717..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..948
FT /note="CAD (involved in subunit assembly)"
FT /evidence="ECO:0000250"
FT REGION 969..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 432..437
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 842..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 550..667
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920E3"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18655026"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_000972"
FT VAR_SEQ 608..611
FT /note="GKGD -> DHLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12135768"
FT /id="VSP_000973"
FT VAR_SEQ 612..988
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12135768"
FT /id="VSP_000974"
FT VAR_SEQ 674..682
FT /note="IIFRKISDV -> GWFSMANAL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_000975"
FT VAR_SEQ 683..988
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_000976"
FT VARIANT 327
FT /note="R -> H (found in a child with sporadic epilepsy;
FT unknown pathological significance; dbSNP:rs587777164)"
FT /evidence="ECO:0000269|PubMed:23647072"
FT /id="VAR_077834"
FT VARIANT 745
FT /note="A -> T (in dbSNP:rs4902176)"
FT /evidence="ECO:0000269|PubMed:11943152,
FT ECO:0000269|PubMed:12135768, ECO:0000269|PubMed:15489334"
FT /id="VAR_065162"
SQ SEQUENCE 988 AA; 111877 MW; A58E4CE0A32C83BC CRC64;
MPGGKRGLVA PQNTFLENIV RRSSESSFLL GNAQIVDWPV VYSNDGFCKL SGYHRADVMQ
KSSTCSFMYG ELTDKKTIEK VRQTFDNYES NCFEVLLYKK NRTPVWFYMQ IAPIRNEHEK
VVLFLCTFKD ITLFKQPIED DSTKGWTKFA RLTRALTNSR SVLQQLTPMN KTEVVHKHSR
LAEVLQLGSD ILPQYKQEAP KTPPHIILHY CAFKTTWDWV ILILTFYTAI MVPYNVSFKT
KQNNIAWLVL DSVVDVIFLV DIVLNFHTTF VGPGGEVISD PKLIRMNYLK TWFVIDLLSC
LPYDIINAFE NVDEGISSLF SSLKVVRLLR LGRVARKLDH YLEYGAAVLV LLVCVFGLVA
HWLACIWYSI GDYEVIDEVT NTIQIDSWLY QLALSIGTPY RYNTSAGIWE GGPSKDSLYV
SSLYFTMTSL TTIGFGNIAP TTDVEKMFSV AMMMVGSLLY ATIFGNVTTI FQQMYANTNR
YHEMLNNVRD FLKLYQVPKG LSERVMDYIV STWSMSKGID TEKVLSICPK DMRADICVHL
NRKVFNEHPA FRLASDGCLR ALAVEFQTIH CAPGDLIYHA GESVDALCFV VSGSLEVIQD
DEVVAILGKG DVFGDIFWKE TTLAHACANV RALTYCDLHI IKREALLKVL DFYTAFANSF
SRNLTLTCNL RKRIIFRKIS DVKKEEEERL RQKNEVTLSI PVDHPVRKLF QKFKQQKELR
NQGSTQGDPE RNQLQVESRS LQNGASITGT SVVTVSQITP IQTSLAYVKT SESLKQNNRD
AMELKPNGGA DQKCLKVNSP IRMKNGNGKG WLRLKNNMGA HEEKKEDWNN VTKAESMGLL
SEDPKSSDSE NSVTKNPLRK TDSCDSGITK SDLRLDKAGE ARSPLEHSPI QADAKHPFYP
IPEQALQTTL QEVKHELKED IQLLSCRMTA LEKQVAEILK ILSEKSVPQA SSPKSQMPLQ
VPPQIPCQDI FSVSRPESPE SDKDEIHF
