ID Q53HN5_HUMAN Unreviewed; 313 AA.
AC Q53HN5;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Potassium channel, subfamily K, member 6 variant {ECO:0000313|EMBL:BAD96265.1};
DE Flags: Fragment;
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 {ECO:0000313|EMBL:BAD96265.1};
RN [1] {ECO:0000313|EMBL:BAD96265.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Coronary artery {ECO:0000313|EMBL:BAD96265.1};
RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8;
RA Maruyama K., Sugano S.;
RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic
RT mRNAs with oligoribonucleotides.";
RL Gene 138:171-174(1994).
RN [2] {ECO:0000313|EMBL:BAD96265.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Coronary artery {ECO:0000313|EMBL:BAD96265.1};
RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3;
RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.;
RT "Construction and characterization of a full length-enriched and a 5'-end-
RT enriched cDNA library.";
RL Gene 200:149-156(1997).
RN [3] {ECO:0000313|EMBL:BAD96265.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Coronary artery {ECO:0000313|EMBL:BAD96265.1};
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
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DR EMBL; AK222545; BAD96265.1; -; mRNA.
DR AlphaFoldDB; Q53HN5; -.
DR PeptideAtlas; Q53HN5; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.70; -; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR005408; 2pore_dom_K_chnl_TWIK.
DR InterPro; IPR005409; 2pore_dom_K_chnl_TWIK2.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003:SF28; POTASSIUM CHANNEL SUBFAMILY K MEMBER 6; 1.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01587; TWIK2CHANNEL.
DR PRINTS; PR01586; TWIKCHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU003857, ECO:0000313|EMBL:BAD96265.1};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..145
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 181..257
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 288..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038061-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD96265.1"
SQ SEQUENCE 313 AA; 33757 MW; 137B55BDFB0575DE CRC64;
MRRGALLAGA LAAYAAYLVL GALLVARLEG PHEARLRAEL ETLRAQLLQR SPCVAAPALD
AFVERVLAAG RLGRVVLANA SGSANASDPA WDFASALFFA STLITTVGYG YTTPLTDAGK
AFSIAFALLG VPTTMLLLTA SAQRLSLLLT HVPLSWLSMR WGWDPRRAAC WHLVALLGVV
VTVCFLVPAV IFAHLEEAWS FLDAFYFCFI SLSTIGLGDY VPGEAPGQPY RALYKVLVTV
YLFLGLVAMV LVLQTFRHVS DLHGLTELIL LPPPCPASFN ADEDDRVDIL GPQPEPHQQL
SASSHTDYAS IPR
//
