GenomeNet

Database: UniProt
Entry: F1LPA2_RAT
LinkDB: F1LPA2_RAT
Original site: F1LPA2_RAT 
ID   F1LPA2_RAT              Unreviewed;       912 AA.
AC   F1LPA2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Potassium voltage-gated channel subfamily Q member 3 {ECO:0000313|Ensembl:ENSRNOP00000006930.6};
GN   Name=Kcnq3 {ECO:0000313|Ensembl:ENSRNOP00000006930.6,
GN   ECO:0000313|RGD:69222};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000006930.6, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000006930.6, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000006930.6,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000006930.6}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000006930.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   RefSeq; NP_113785.3; NM_031597.4.
DR   AlphaFoldDB; F1LPA2; -.
DR   Ensembl; ENSRNOT00000006930.8; ENSRNOP00000006930.6; ENSRNOG00000005206.8.
DR   GeneID; 29682; -.
DR   KEGG; rno:29682; -.
DR   CTD; 3786; -.
DR   RGD; 69222; Kcnq3.
DR   VEuPathDB; HostDB:ENSRNOG00000005206; -.
DR   GeneTree; ENSGT00940000159760; -.
DR   HOGENOM; CLU_011722_8_2_1; -.
DR   OMA; QDRDDYM; -.
DR   TreeFam; TF315186; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000005206; Expressed in frontal cortex and 5 other cell types or tissues.
DR   ExpressionAtlas; F1LPA2; baseline and differential.
DR   GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:Ensembl.
DR   GO; GO:0099610; P:action potential initiation; IEA:Ensembl.
DR   GO; GO:0097314; P:apoptosome assembly; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR   GO; GO:0098976; P:excitatory chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0098977; P:inhibitory chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR   GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0021675; P:nerve development; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0016322; P:neuron remodeling; IEA:Ensembl.
DR   GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR   GO; GO:0036343; P:psychomotor behavior; IEA:Ensembl.
DR   GO; GO:0099611; P:regulation of action potential firing threshold; IEA:Ensembl.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:1903701; P:substantia propria of cornea development; IEA:Ensembl.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 6.10.140.1910; -; 2.
DR   InterPro; IPR020969; Ankyrin-G_BS.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR003948; K_chnl_volt-dep_KCNQ3.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   PANTHER; PTHR47735:SF11; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 3; 1.
DR   PANTHER; PTHR47735; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 1.
DR   Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01462; KCNQ3CHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          165..397
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          487..689
FT                   /note="Potassium channel voltage dependent KCNQ C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03520"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..912
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  100947 MW;  3E64A5D7A7241828 CRC64;
     MALEFPGLQP PPPPRPVPQA LLLPGAAAEK AKRPVGARQM GLKARRAAGA AGGGGGEGGG
     GGGGAANPAG GDSAVAGDEE RKVGLAPGDV EQVTLALGTG ADKDGTLLLE GGGREEGQRR
     TPQGIGLLAK TPLSRPVKRN NAKYRRIQTL IYDALERPRG WALLYHALVF LIVLGCLILA
     VLTTFKEYET VSGDWLLLLE TFAIFIFGAE FALRIWAAGC CCRYKGWRGR LKFARKPLCM
     LDIFVLIASV PVVAVGNQGN VLATSLRSLR FLQILRMLRM DRRGGTWKLL GSAICAHSKE
     LITAWYIGFL TLILSSFLVY LVEKDVPEMD AQGEEMKEEF ETYADALWWG LITLATIGYG
     DKTPKTWEGR LIAATFSLIG VSFFALPAGI LGSGLALKVQ EQHRQKHFEK RRKPAAELIQ
     AAWRYYATNP NRLDLVATWR FYESVVSFPF FRKEQLEAAA SQKLGLLDRV RLSNPRGSNT
     KGKLFTPLNV DAIEESPSKE PKPVGLNNKE RFRTAFRMKA YAFWQSSEDA GTGDPMTEDR
     GYGNDFLIED MIPTLKAAIR AVRILQFRLY KKKFKETLRP YDVKDVIEQY SAGHLDMLSR
     IKYLQTRIDM IFTPGPPSTP KHKKSQKGSA FTYPSQQSPR NEPYVARAAT SETEDQSMMG
     KFVKVERQVH DMGKKLDFLV DMHMQHMERL QVHVTEYYPT KGASSPAEGE KKEDNRYSDL
     KTIICNYSES GPPDPPYSFH QVPIDRVGPY GFFAHDPVKL TRGGPSSTKA QANLPSSGST
     YAERPTVLPI LTLLDSCVSY HSQTELQGPY SDHISPRQRR SITRDSDTPL SLMSVNHEEL
     ERSPSGFSIS QDRDDYVFGP SGGSSWMREK RYLAEGETDT DTDPFTPSGS MPMSSTGDGI
     SDSIWTPSNK PT
//
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