ORK1_DROME
ID ORK1_DROME Reviewed; 1001 AA.
AC Q94526; B5RIM4; Q0KHU1; Q32KC8; Q95TX7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Open rectifier potassium channel protein 1;
DE AltName: Full=Two pore domain potassium channel Ork1;
GN Name=Ork1; ORFNames=CG1615;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, Larva, and Muscle;
RX PubMed=8917578; DOI=10.1073/pnas.93.23.13256;
RA Goldstein S.A.N., Price L.A., Rosenthal D.N., Pausch M.H.;
RT "ORK1, a potassium-selective leak channel with two pore domains cloned from
RT Drosophila melanogaster by expression in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13256-13261(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-1001.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-373; SER-562;
RP SER-565; SER-685; SER-691 AND SER-715, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Background potassium channel. Rectification is dependent on
CC external potassium concentration. Acts as an outwardly rectifying
CC channel but as external potassium levels increase, this is reversed.
CC {ECO:0000269|PubMed:8917578}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widespread expression in adult, strongest
CC expression in muscle, brain and ovary. Also present at low levels in
CC larva and embryo. {ECO:0000269|PubMed:8917578}.
CC -!- MISCELLANEOUS: Inhibited by barium.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U55321; AAC69250.1; -; mRNA.
DR EMBL; AE014298; AAN09276.1; -; Genomic_DNA.
DR EMBL; BT023951; ABB36455.1; -; mRNA.
DR EMBL; BT044148; ACH92213.1; -; mRNA.
DR EMBL; AY058455; AAL13684.1; ALT_INIT; mRNA.
DR PIR; T13807; T13807.
DR RefSeq; NP_001285096.1; NM_001298167.1.
DR RefSeq; NP_511112.1; NM_078557.5.
DR RefSeq; NP_727466.1; NM_167259.3.
DR AlphaFoldDB; Q94526; -.
DR BioGRID; 58437; 3.
DR DIP; DIP-22401N; -.
DR IntAct; Q94526; 3.
DR STRING; 7227.FBpp0073261; -.
DR GlyGen; Q94526; 1 site.
DR iPTMnet; Q94526; -.
DR PaxDb; Q94526; -.
DR DNASU; 32020; -.
DR EnsemblMetazoa; FBtr0073404; FBpp0073260; FBgn0017561.
DR EnsemblMetazoa; FBtr0073405; FBpp0073261; FBgn0017561.
DR EnsemblMetazoa; FBtr0346304; FBpp0312045; FBgn0017561.
DR GeneID; 32020; -.
DR KEGG; dme:Dmel_CG1615; -.
DR CTD; 32020; -.
DR FlyBase; FBgn0017561; Ork1.
DR VEuPathDB; VectorBase:FBgn0017561; -.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_331565_0_0_1; -.
DR InParanoid; Q94526; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q94526; -.
DR Reactome; R-DME-1299344; TWIK-related spinal cord K+ channel (TRESK).
DR Reactome; R-DME-1299361; TWIK-related alkaline pH activated K+ channel (TALK).
DR Reactome; R-DME-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-DME-5576886; Phase 4 - resting membrane potential.
DR SignaLink; Q94526; -.
DR BioGRID-ORCS; 32020; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32020; -.
DR PRO; PR:Q94526; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0017561; Expressed in oocyte and 15 other tissues.
DR ExpressionAtlas; Q94526; baseline and differential.
DR Genevisible; Q94526; DM.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0034705; C:potassium channel complex; IDA:FlyBase.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022841; F:potassium ion leak channel activity; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:FlyBase.
DR GO; GO:0002027; P:regulation of heart rate; IMP:FlyBase.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1001
FT /note="Open rectifier potassium channel protein 1"
FT /id="PRO_0000101769"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 95..111
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 208..224
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..1001
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 591..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 454
FT /note="A -> V (in Ref. 4; ABB36455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1001 AA; 109290 MW; 09AE1A3669072E07 CRC64;
MSPNRWILLL IFYISYLMFG AAIYYHIEHG EEKISRAEQR KAQIAINEYL LEELGDKNTT
TQDEILQRIS DYCDKPVTLP PTYDDTPYTW TFYHAFFFAF TVCSTVGYGN ISPTTFAGRM
IMIAYSVIGI PVNGILFAGL GEYFGRTFEA IYRRYKKYKM STDMHYVPPQ LGLITTVVIA
LIPGIALFLL LPSWVFTYFE NWPYSISLYY SYVTTTTIGF GDYVPTFGAN QPKEFGGWFV
VYQIFVIVWF IFSLGYLVMI MTFITRGLQS KKLAYLEQQL SSNLKATQNR IWSGVTKDVG
YLRRMLNELY ILKVKPVYTD VDIAYTLPRS NSCPDLSMYR VEPAPIPSRK RAFSVCADMV
AAQREAGMVH ANSDTELSKL DREKTFETAE AYRQTTDLLA KVVNALATVK PPPAEQEDAA
LYGGYHGFSD SQILASEWSF STVNEFTSPR RPRARACSDF NLEAPRWQSE RPLRSSHNEW
TWSGDNQQIQ EAFNQRYKGQ QRANGAANST MVHLEPDALE EQLKKQSPGA GRVKKFSMPD
GLRRLFPFQK KRPSQDLERK LSVVSVPEGV ISQQARSPLD YYSNTVTAAS SQSYLRNGRG
PPPPFESNGS LASGGGGLTN MGFQMEDGAT PPSALGGGAY QRKAAAGKRR RESIYTQNQA
PSARRGSMYP PTAHALAQMQ MRRGSLATSG SGSAAMAAVA ARRGSLFPAT ASASSLTSAP
RRSSIFSVTS EKDMNVLEQT TIADLIRALE VVHTHAVLDE QQQAAAAGGA AGGGGISRGS
RKQRKMGNAG LEPPQLPPIL SLFAGDQTRT LQAAAANRLY ARRSTIVGIS PTGGAATAPA
ARSLLEPPPS YTERAANQSQ ITAGPSNAPT VQSKFRRRFS VRPTALQIPP GQAPPPGASL
MEQSSQTALQ RRLSLRPSPL ARELSPTSPP GGSGSALPAG AIDESGGTSA QRLLPLPAGT
RPSTSSTHSP LSRIVQISQA QRKSSMPSAA ATGSSGAPAE K
