LOCUS       NP_038597               1162 aa            linear   ROD 19-NOV-2024
DEFINITION  voltage-gated inwardly rectifying potassium channel KCNH2 isoform 1
            [Mus musculus].
ACCESSION   NP_038597 XP_911235 XP_924762 XP_924773
VERSION     NP_038597.2
DBSOURCE    REFSEQ: accession NM_013569.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1162)
  AUTHORS   Schwarz,J.R., Freitag,S., Pechmann,Y., Hermans-Borgmeyer,I.,
            Wagner,W., Hornig,S. and Kneussel,M.
  TITLE     Purkinje cell hyperexcitability and depressive-like behavior in
            mice lacking erg3 (ether-a-go-go-related gene) K+ channel subunits
  JOURNAL   Sci Adv 10 (40), eadn6836 (2024)
   PUBMED   39365861
REFERENCE   2  (residues 1 to 1162)
  AUTHORS   Sinha,T., Lammerts van Bueren,K., Dickel,D.E., Zlatanova,I.,
            Thomas,R., Lizama,C.O., Xu,S.M., Zovein,A.C., Ikegami,K.,
            Moskowitz,I.P., Pollard,K.S., Pennacchio,L.A. and Black,B.L.
  TITLE     Differential Etv2 threshold requirement for endothelial and
            erythropoietic development
  JOURNAL   Cell Rep 39 (9), 110881 (2022)
   PUBMED   35649376
REFERENCE   3  (residues 1 to 1162)
  AUTHORS   Anderson,L.B., Ravara,B., Hameed,S., Latour,C.D., Latour,S.M.,
            Graham,V.M., Hashmi,M.N., Cobb,B., Dethrow,N., Urazaev,A.K.,
            Davie,J.K., Albertin,G., Carraro,U., Zampieri,S. and Pond,A.L.
  TITLE     MERG1A Protein Abundance Increases in the Atrophied Skeletal Muscle
            of Denervated Mice, But Does Not Affect NFkappaB Activity
  JOURNAL   J Neuropathol Exp Neurol 80 (8), 776-788 (2021)
   PUBMED   34363662
  REMARK    GeneRIF: MERG1A Protein Abundance Increases in the Atrophied
            Skeletal Muscle of Denervated Mice, But Does Not Affect NFkappaB
            Activity.
REFERENCE   4  (residues 1 to 1162)
  AUTHORS   Dierich,M., Altoe,A., Koppelmann,J., Evers,S., Renigunta,V.,
            Schafer,M.K., Naumann,R., Verhulst,S., Oliver,D. and Leitner,M.G.
  TITLE     Optimized Tuning of Auditory Inner Hair Cells to Encode Complex
            Sound through Synergistic Activity of Six Independent K+ Current
            Entities
  JOURNAL   Cell Rep 32 (1), 107869 (2020)
   PUBMED   32640234
REFERENCE   5  (residues 1 to 1162)
  AUTHORS   van den Boogaard,M., van Weerd,J.H., Bawazeer,A.C., Hooijkaas,I.B.,
            van de Werken,H.J.G., Tessadori,F., de Laat,W., Barnett,P.,
            Bakkers,J. and Christoffels,V.M.
  TITLE     Identification and Characterization of a Transcribed Distal
            Enhancer Involved in Cardiac Kcnh2 Regulation
  JOURNAL   Cell Rep 28 (10), 2704-2714 (2019)
   PUBMED   31484079
  REMARK    GeneRIF: Identification and Characterization of a Transcribed
            Distal Enhancer Involved in Cardiac Kcnh2 Regulation.
REFERENCE   6  (residues 1 to 1162)
  AUTHORS   Trudeau,M.C., Titus,S.A., Branchaw,J.L., Ganetzky,B. and
            Robertson,G.A.
  TITLE     Functional analysis of a mouse brain Elk-type K+ channel
  JOURNAL   J Neurosci 19 (8), 2906-2918 (1999)
   PUBMED   10191308
REFERENCE   7  (residues 1 to 1162)
  AUTHORS   London,B., Trudeau,M.C., Newton,K.P., Beyer,A.K., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A., Satler,C.A. and Robertson,G.A.
  TITLE     Two isoforms of the mouse ether-a-go-go-related gene coassemble to
            form channels with properties similar to the rapidly activating
            component of the cardiac delayed rectifier K+ current
  JOURNAL   Circ Res 81 (5), 870-878 (1997)
   PUBMED   9351462
REFERENCE   8  (residues 1 to 1162)
  AUTHORS   Lees-Miller,J.P., Kondo,C., Wang,L. and Duff,H.J.
  TITLE     Electrophysiological characterization of an alternatively processed
            ERG K+ channel in mouse and human hearts
  JOURNAL   Circ Res 81 (5), 719-726 (1997)
   PUBMED   9351446
REFERENCE   9  (residues 1 to 1162)
  AUTHORS   Curran,M.E., Splawski,I., Timothy,K.W., Vincent,G.M., Green,E.D.
            and Keating,M.T.
  TITLE     A molecular basis for cardiac arrhythmia: HERG mutations cause long
            QT syndrome
  JOURNAL   Cell 80 (5), 795-803 (1995)
   PUBMED   7889573
REFERENCE   10 (residues 1 to 1162)
  AUTHORS   Warmke,J.W. and Ganetzky,B.
  TITLE     A family of potassium channel genes related to eag in Drosophila
            and mammals
  JOURNAL   Proc Natl Acad Sci U S A 91 (8), 3438-3442 (1994)
   PUBMED   8159766
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113055.9.
            
            On Sep 7, 2007 this sequence version replaced NP_038597.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1, also known as
            Merg1a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF012868.1, BC051016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 10.94 cM"
     Protein         1..1162
                     /product="voltage-gated inwardly rectifying potassium
                     channel KCNH2 isoform 1"
                     /note="potassium voltage-gated channel subfamily H member
                     2; eag-related protein 1; ether-a-go-go-related protein 1;
                     ether-a-go-go-related gene potassium channel 1;
                     voltage-gated potassium channel subunit Kv11.1;
                     voltage-gated inwardly rectifying potassium channel KCNH2"
                     /calculated_mol_wt=126774
     Region          30..328
                     /region_name="PRK13559"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:237427"
     Region          38..130
                     /region_name="PAS_9"
                     /note="PAS domain; pfam13426"
                     /db_xref="CDD:463873"
     Region          233..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12809; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08962; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            406..426
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Region          411..670
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            453..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            498..518
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            523..543
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            550..570
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Region          626..631
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:Q63472"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            641..661
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Region          744..855
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Region          744..844
                     /region_name="cNMP-binding domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00060"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            order(808..809,820..822)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(842..844,848..850)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          873..991
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            873
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Site            1017
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     Region          1125..1162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35219.2)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35219.2)"
     CDS             1..1162
                     /gene="Kcnh2"
                     /gene_synonym="ERG1; LQT; Lqt2; M-erg; Merg1; merg1a;
                     merg1b"
                     /coded_by="NM_013569.2:322..3810"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS19116.1"
                     /db_xref="GeneID:16511"
                     /db_xref="MGI:MGI:1341722"
ORIGIN      
        1 mpvrrghvap qntfldtiir kfegqsrkfi ianarvenca viycndgfce lcgysraevm
       61 qrpctcdflh gprtqrraaa qiaqallgae erkveiafyr kdgscflclv dvvpvknedg
      121 avimfilnfe vvmekdmvgs pahdtnhrgp stswlasgra ktfrlklpal laltaressv
      181 rtgsmrsaga pgavvvdvdl tpaapssesl aldevsamdn hvaglgpaee rralvgpgsa
      241 spvasirgph pspraqslnp dasgsscsla rtrsrescas vrrassaddi eamragalpp
      301 pprhastgam hplrsgllns tsdsdlvryr tiskipqitl nfvdlkgdpf lasptsdrei
      361 iapkikerth nvtekvtqvl slgadvlpey klqaprihrw tilhyspfka vwdwlilllv
      421 iytavftpys aafllketed gsqapdcgya cqplavvdli vdimfivdil infrttyvna
      481 neevvshpgr iavhyfkgwf lidmvaaipf dllifgsgse eligllktar llrlvrvark
      541 ldryseygaa vlfllmctfa liahwlaciw yaignmeqph mdshigwlhn lgdqigkpyn
      601 ssglggpsik dkyvtalyft fssltsvgfg nvspntnsek ifsicvmlig slmyasifgn
      661 vsaiiqrlys gtaryhtqml rvrefirfhq ipnplrqrle eyfqhawsyt ngidmnavlk
      721 gfpeclqadi clhlnrsllq hckpfrgatk gclralamkf ktthappgdt lvhagdllta
      781 lyfisrgsie ilrgdvvvai lgkndifgep lnlyarpgks ngdvraltyc dlhkihrddl
      841 levldmypef sdhfwsslei tfnlrdtnmi pgspgsaele sgfnrqrkrk lsfrrrtdkd
      901 teqpgevsal gqgparvgpg pscrgqpggp wgespssgps spessedegp grsssplrlv
      961 pfssprppgd ppggeplted geksdtcnpl sgafsgvsni fsfwgdsrgr qyqelprcpa
     1021 papsllnipl sspgrrsrgd vesrldalqr qlnrletrls admatvlqll qrqmtlvppa
     1081 ysavttpgpg ptsaspllpv gpvptltlds lsqvsqfvaf eelpagapel pqdgptrrls
     1141 lpgqlgalts qplhrhgsdp gs
//
