ID   KCNH2_MOUSE             Reviewed;        1162 AA.
AC   O35219; O35220; O35221; O35989;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   08-NOV-2023, entry version 190.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 2;
DE   AltName: Full=Ether-a-go-go-related gene potassium channel 1;
DE            Short=ERG-1;
DE            Short=Eag-related protein 1;
DE            Short=Ether-a-go-go-related protein 1;
DE            Short=MERG;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv11.1;
GN   Name=Kcnh2; Synonyms=Erg, Merg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND
RP   VARIANTS ARG-186; THR-455; TYR-752 AND ASN-1006.
RC   STRAIN=129/Sv, and BALB/cJ; TISSUE=Heart;
RX   PubMed=9351462; DOI=10.1161/01.res.81.5.870;
RA   London B., Trudeau M.C., Newton K.P., Beyer A.K., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Satler C.A., Robertson G.A.;
RT   "Two isoforms of the mouse ether-a-go-go-related gene coassemble to form
RT   channels with properties similar to the rapidly activating component of the
RT   cardiac delayed rectifier K+ current.";
RL   Circ. Res. 81:870-878(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Atrial tumor;
RX   PubMed=9351446; DOI=10.1161/01.res.81.5.719;
RA   Lees-Miller J.P., Kondo C., Wang L., Duff H.J.;
RT   "Electrophysiological characterization of an alternatively processed ERG K+
RT   channel in mouse and human hearts.";
RL   Circ. Res. 81:719-726(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-245; SER-285;
RP   SER-286; SER-322; SER-873; SER-876 AND SER-1140, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1017, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly
CC       rectifying potassium channel. Channel properties are modulated by cAMP
CC       and subunit assembly. Mediates the rapidly activating component of the
CC       delayed rectifying potassium current in heart (IKr) (By similarity).
CC       {ECO:0000250|UniProtKB:Q12809}.
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. Interacts with DNAJB12 and
CC       DNAJB14; chaperones DNAJB12 and DNAJB14 promote tetramerization (By
CC       similarity). Heteromultimer with KCNH6/ERG2 and KCNH7/ERG3 (By
CC       similarity). Interacts with ALG10B (By similarity). Heteromultimer with
CC       KCNE1 and KCNE2. Interacts with CANX. The core-glycosylated, but not
CC       the fully glycosylated form interacts with RNF207. Interacts with
CC       NDFIP1 and NDFIP2 (By similarity). {ECO:0000250|UniProtKB:O08962,
CC       ECO:0000250|UniProtKB:Q12809}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1; Synonyms=1A, A;
CC         IsoId=O35219-1; Sequence=Displayed;
CC       Name=2; Synonyms=1A';
CC         IsoId=O35219-2; Sequence=VSP_000969;
CC       Name=3; Synonyms=1B, B;
CC         IsoId=O35219-3; Sequence=VSP_000970;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in heart, brain and testis
CC       and at low levels in lung. Isoform 3 is expressed predominantly in
CC       heart. The expression of isoform 2 is low in all tissues tested.
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   -!- PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF012868; AAC53418.1; -; mRNA.
DR   EMBL; AF012869; AAC53419.1; -; mRNA.
DR   EMBL; AF012871; AAC53420.1; -; Genomic_DNA.
DR   EMBL; AF012870; AAC53420.1; JOINED; Genomic_DNA.
DR   EMBL; AF012871; AAC53421.1; -; Genomic_DNA.
DR   EMBL; AF012871; AAC53422.1; -; Genomic_DNA.
DR   EMBL; AF012870; AAC53422.1; JOINED; Genomic_DNA.
DR   EMBL; AF034762; AAB87571.1; -; mRNA.
DR   CCDS; CCDS19116.1; -. [O35219-1]
DR   CCDS; CCDS80224.1; -. [O35219-3]
DR   RefSeq; NP_001281091.1; NM_001294162.1.
DR   AlphaFoldDB; O35219; -.
DR   BMRB; O35219; -.
DR   SMR; O35219; -.
DR   ComplexPortal; CPX-3197; Voltage-gated potassium channel complex variant 2.
DR   ComplexPortal; CPX-3198; Voltage-gated potassium channel complex variant 1.
DR   IntAct; O35219; 31.
DR   STRING; 10090.ENSMUSP00000047705; -.
DR   GlyCosmos; O35219; 1 site, No reported glycans.
DR   GlyGen; O35219; 1 site.
DR   iPTMnet; O35219; -.
DR   PhosphoSitePlus; O35219; -.
DR   jPOST; O35219; -.
DR   MaxQB; O35219; -.
DR   PaxDb; 10090-ENSMUSP00000047705; -.
DR   PeptideAtlas; O35219; -.
DR   ProteomicsDB; 269265; -. [O35219-1]
DR   ProteomicsDB; 269266; -. [O35219-2]
DR   ProteomicsDB; 269267; -. [O35219-3]
DR   DNASU; 16511; -.
DR   GeneID; 16511; -.
DR   KEGG; mmu:16511; -.
DR   UCSC; uc008wrb.1; mouse. [O35219-3]
DR   AGR; MGI:1341722; -.
DR   CTD; 3757; -.
DR   MGI; MGI:1341722; Kcnh2.
DR   eggNOG; KOG0498; Eukaryota.
DR   InParanoid; O35219; -.
DR   OrthoDB; 66005at2759; -.
DR   PhylomeDB; O35219; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   Reactome; R-MMU-5576890; Phase 3 - rapid repolarisation.
DR   BioGRID-ORCS; 16511; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Erg; mouse.
DR   PRO; PR:O35219; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O35219; Protein.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:1902937; C:inward rectifier potassium channel complex; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR   GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:MGI.
DR   GO; GO:0005216; F:monoatomic ion channel activity; ISO:MGI.
DR   GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR   GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; ISO:MGI.
DR   GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR   GO; GO:0086011; P:membrane repolarization during action potential; ISO:MGI.
DR   GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:1903765; P:negative regulation of potassium ion export across plasma membrane; ISO:MGI.
DR   GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
DR   GO; GO:0055075; P:potassium ion homeostasis; ISO:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IDA:MGI.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IDA:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IDA:MGI.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.1200.260; -; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR003967; K_chnl_volt-dep_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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10217:SF506; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 2; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 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; PR01470; ERGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Methylation; Phosphoprotein; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..1162
FT                   /note="Potassium voltage-gated channel subfamily H member
FT                   2"
FT                   /id="PRO_0000054000"
FT   TOPO_DOM        1..405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..452
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        453..473
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        474..497
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        498..518
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        519..522
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        544..549
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        550..570
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        571..613
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        614..634
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        635..640
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        641..661
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        662..1162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..88
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          92..144
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   REGION          233..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1125..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           626..631
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        256..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         744..861
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12809"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08962"
FT   MOD_RES         873
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1017
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..378
FT                   /note="MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELC
FT                   GYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVD
FT                   VVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPAL
FT                   LALTARESSVRTGSMHSAGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAE
FT                   ERRALVGPGSASPVASIRGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSAD
FT                   DIEAMRAGALPPPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKG
FT                   DPFLASPTSDREIIAPKIKERTHNVTEKVTQ -> MAIPTGKESRTGALQPRAQKGRVR
FT                   RAVRISSLVAQE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9351446,
FT                   ECO:0000303|PubMed:9351462"
FT                   /id="VSP_000970"
FT   VAR_SEQ         1..59
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9351462"
FT                   /id="VSP_000969"
FT   VARIANT         186
FT                   /note="H -> R (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:9351462"
FT   VARIANT         455
FT                   /note="A -> T (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:9351462"
FT   VARIANT         752
FT                   /note="C -> Y (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:9351462"
FT   VARIANT         1006
FT                   /note="D -> N (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:9351462"
SQ   SEQUENCE   1162 AA;  126886 MW;  A9455F7F10B61E46 CRC64;
     MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM
     QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG
     AVIMFILNFE VVMEKDMVGS PAHDTNHRGP STSWLASGRA KTFRLKLPAL LALTARESSV
     RTGSMHSAGA PGAVVVDVDL TPAAPSSESL ALDEVSAMDN HVAGLGPAEE RRALVGPGSA
     SPVASIRGPH PSPRAQSLNP DASGSSCSLA RTRSRESCAS VRRASSADDI EAMRAGALPP
     PPRHASTGAM HPLRSGLLNS TSDSDLVRYR TISKIPQITL NFVDLKGDPF LASPTSDREI
     IAPKIKERTH NVTEKVTQVL SLGADVLPEY KLQAPRIHRW TILHYSPFKA VWDWLILLLV
     IYTAVFTPYS AAFLLKETED GSQAPDCGYA CQPLAVVDLI VDIMFIVDIL INFRTTYVNA
     NEEVVSHPGR IAVHYFKGWF LIDMVAAIPF DLLIFGSGSE ELIGLLKTAR LLRLVRVARK
     LDRYSEYGAA VLFLLMCTFA LIAHWLACIW YAIGNMEQPH MDSHIGWLHN LGDQIGKPYN
     SSGLGGPSIK DKYVTALYFT FSSLTSVGFG NVSPNTNSEK IFSICVMLIG SLMYASIFGN
     VSAIIQRLYS GTARYHTQML RVREFIRFHQ IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK
     GFPECLQADI CLHLNRSLLQ HCKPFRGATK GCLRALAMKF KTTHAPPGDT LVHAGDLLTA
     LYFISRGSIE ILRGDVVVAI LGKNDIFGEP LNLYARPGKS NGDVRALTYC DLHKIHRDDL
     LEVLDMYPEF SDHFWSSLEI TFNLRDTNMI PGSPGSAELE SGFNRQRKRK LSFRRRTDKD
     TEQPGEVSAL GQGPARVGPG PSCRGQPGGP WGESPSSGPS SPESSEDEGP GRSSSPLRLV
     PFSSPRPPGD PPGGEPLTED GEKSDTCNPL SGAFSGVSNI FSFWGDSRGR QYQELPRCPA
     PAPSLLNIPL SSPGRRSRGD VESRLDALQR QLNRLETRLS ADMATVLQLL QRQMTLVPPA
     YSAVTTPGPG PTSASPLLPV GPVPTLTLDS LSQVSQFVAF EELPAGAPEL PQDGPTRRLS
     LPGQLGALTS QPLHRHGSDP GS
//