KCNB2_RAT
ID KCNB2_RAT Reviewed; 907 AA.
AC Q63099;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Potassium voltage-gated channel subfamily B member 2 {ECO:0000312|RGD:621349};
DE AltName: Full=CDRK {ECO:0000303|PubMed:1550672};
DE AltName: Full=Voltage-gated potassium channel subunit Kv2.2;
GN Name=Kcnb2 {ECO:0000312|RGD:621349};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1550672; DOI=10.1016/0896-6273(92)90275-i;
RA Hwang P.M., Glatt C.E., Bredt D.S., Yellen G., Snyder S.H.;
RT "A novel K+ channel with unique localizations in mammalian brain: molecular
RT cloning and characterization.";
RL Neuron 8:473-481(1992).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9305895; DOI=10.1074/jbc.272.39.24371;
RA Salinas M., Duprat F., Heurteaux C., Hugnot J.-P., Lazdunski M.;
RT "New modulatory alpha subunits for mammalian Shab K+ channels.";
RL J. Biol. Chem. 272:24371-24379(1997).
RN [3]
RP REVIEW.
RX PubMed=10414301; DOI=10.1111/j.1749-6632.1999.tb11293.x;
RA Coetzee W.A., Amarillo Y., Chiu J., Chow A., Lau D., McCormack T.,
RA Moreno H., Nadal M.S., Ozaita A., Pountney D., Saganich M.,
RA Vega-Saenz de Miera E., Rudy B.;
RT "Molecular diversity of K+ channels.";
RL Ann. N. Y. Acad. Sci. 868:233-285(1999).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10719893; DOI=10.1016/s0896-6273(00)80902-2;
RA Lim S.T., Antonucci D.E., Scannevin R.H., Trimmer J.S.;
RT "A novel targeting signal for proximal clustering of the Kv2.1 K+ channel
RT in hippocampal neurons.";
RL Neuron 25:385-397(2000).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20202934; DOI=10.1074/jbc.m109.074260;
RA Kihira Y., Hermanstyne T.O., Misonou H.;
RT "Formation of heteromeric Kv2 channels in mammalian brain neurons.";
RL J. Biol. Chem. 285:15048-15055(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes, primarily in the brain and
CC smooth muscle cells (PubMed:1550672). Channels open or close in
CC response to the voltage difference across the membrane, letting
CC potassium ions pass in accordance with their electrochemical gradient.
CC Homotetrameric channels mediate a delayed-rectifier voltage-dependent
CC outward potassium current that display rapid activation and slow
CC inactivation in response to membrane depolarization (PubMed:1550672).
CC Can form functional homotetrameric and heterotetrameric channels that
CC contain variable proportions of KCNB1; channel properties depend on the
CC type of alpha subunits that are part of the channel (PubMed:20202934).
CC Can also form functional heterotetrameric channels with other alpha
CC subunits that are non-conducting when expressed alone, such as KCNS1
CC and KCNS2, creating a functionally diverse range of channel complexes
CC (PubMed:9305895). In vivo, membranes probably contain a mixture of
CC heteromeric potassium channel complexes, making it difficult to assign
CC currents observed in intact tissues to any particular potassium channel
CC family member. Contributes to the delayed-rectifier voltage-gated
CC potassium current in cortical pyramidal neurons and smooth muscle cells
CC (PubMed:1550672, PubMed:20202934). {ECO:0000250|UniProtKB:A6H8H5,
CC ECO:0000269|PubMed:1550672, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:9305895}.
CC -!- ACTIVITY REGULATION: Inhibited by quinine at micromolar levels (By
CC similarity). Modestly sensitive to millimolar levels of
CC tetraethylammonium (TEA) (PubMed:1550672). Modestly sensitive to
CC millimolar levels of 4-aminopyridine (4-AP).
CC {ECO:0000250|UniProtKB:Q95167, ECO:0000269|PubMed:1550672,
CC ECO:0000305|PubMed:10414301}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Homotetrameric channels expressed in xenopus oocytes or in
CC mammalian non-neuronal cells display delayed-rectifier voltage-
CC dependent potassium currents which are activated during membrane
CC depolarization, i.e within a risetime of about 20 msec
CC (PubMed:1550672). After that, inactivate very slowly
CC (PubMed:1550672). Their activation requires low threshold potentials
CC of about -20 to -30 mV, with a midpoint activation at about 10 mV.
CC For inactivation, the voltage at half-maximal amplitude is about -30
CC mV. Channels have an unitary conductance of about 14 pS. The voltage-
CC dependence of activation and inactivation and other channel
CC characteristics vary depending on the experimental conditions, the
CC expression system and post-translational modifications.
CC {ECO:0000269|PubMed:1550672, ECO:0000305|PubMed:10414301};
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCNB1 (PubMed:20202934).
CC Heterotetramer with KCNS1 and KCNS2 (PubMed:9305895).
CC {ECO:0000250|UniProtKB:A6H8H5, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:9305895}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10719893,
CC ECO:0000269|PubMed:1550672, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}.
CC Perikaryon {ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:20202934}.
CC Cell projection, dendrite {ECO:0000269|PubMed:10719893,
CC ECO:0000269|PubMed:20202934}. Note=Localized uniformly throughout cell
CC bodies and dendrites (PubMed:10719893). Colocalizes with KCNB1 to high-
CC density somatodendritic clusters on cortical pyramidal neurons
CC (PubMed:20202934). {ECO:0000269|PubMed:10719893,
CC ECO:0000269|PubMed:20202934}.
CC -!- TISSUE SPECIFICITY: Expressed in pyramidal neurons of the cerebral
CC cortex (at protein level) (PubMed:20202934). In the brain, the greatest
CC density occurs in the olfactory bulb, followed by the cerebral cortex,
CC hippocampus, and cerebellum. In peripheral tissues it is most prominent
CC in whole tongue epithelium and circumvallate papillae (PubMed:1550672).
CC {ECO:0000269|PubMed:1550672, ECO:0000269|PubMed:20202934}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- PTM: Phosphorylated (PubMed:20202934). {ECO:0000269|PubMed:20202934}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
CC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40905.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M77482; AAA40905.1; ALT_FRAME; mRNA.
DR PIR; JH0595; JH0595.
DR PDB; 6EBK; EM; 3.30 A; B/D/F/H=278-311.
DR PDB; 6EBL; EM; 3.00 A; B/D/F/H=278-311.
DR PDB; 6EBM; EM; 4.00 A; B/D/F/H=278-311.
DR PDBsum; 6EBK; -.
DR PDBsum; 6EBL; -.
DR PDBsum; 6EBM; -.
DR AlphaFoldDB; Q63099; -.
DR SMR; Q63099; -.
DR STRING; 10116.ENSRNOP00000050431; -.
DR GuidetoPHARMACOLOGY; 547; -.
DR GlyGen; Q63099; 1 site.
DR iPTMnet; Q63099; -.
DR PhosphoSitePlus; Q63099; -.
DR PaxDb; Q63099; -.
DR PRIDE; Q63099; -.
DR ABCD; Q63099; 3 sequenced antibodies.
DR UCSC; RGD:621349; rat.
DR RGD; 621349; Kcnb2.
DR eggNOG; KOG3713; Eukaryota.
DR InParanoid; Q63099; -.
DR PhylomeDB; Q63099; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q63099; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003973; K_chnl_volt-dep_Kv2.
DR InterPro; IPR005826; K_chnl_volt-dep_Kv2.2.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03521; Kv2channel; 1.
DR PRINTS; PR01515; KV22CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01495; SHABCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..907
FT /note="Potassium voltage-gated channel subfamily B member
FT 2"
FT /id="PRO_0000054050"
FT TOPO_DOM 1..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 191..212
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 213..232
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 233..254
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 255..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 266..284
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 285..296
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 297..317
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 318..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 333..355
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 356..368
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 369..380
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 381..388
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 389..395
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 396..424
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 425..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 381..386
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT COMPBIAS 519..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:6EBK"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6EBK"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:6EBK"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:6EBK"
SQ SEQUENCE 907 AA; 102096 MW; B242D9A6753A1295 CRC64;
MAEKAPPGLN RKTSRSTLSL PPEPVDIIRS KTCSRRVKIN VGGLNHEVLW RTLDRLPRTR
LGKLRDCNTH ESLLEVCDDY NLNENEYFFD RHPGAFTSIL NFYRTGKLHM MEEMCALSFG
QELDYWGIDE IYLESCCQAR YHQKKEQMNE ELRREAETMR DGEGEEFDNT CCPEKRKKLW
DLLEKPNSSV AAKILAIVSI LFIVLSTIAL SLNTLPELQE NDEFGQPSDN RKLAHVEAVC
IAWFTMEYLL RFLSSPNKWK FFKGPLNVID LLAILPYYVT IFLTESNKSV LQFQNVRRVV
QIFRIMRILR ILKLARHSTG LQSLGFTLRR SYNELGLLIL FLAMGIMIFS SLVFFAEKDE
DATKFTSIPA SFWWATITMT TVGYGDIYPK TLLGKIVGGL CCIAGVLVIA LPIPIIVNNF
SEFYKEQKRQ EKAIKRREAL ERAKRNGSIV SMNLKDAFAR SMELIDVAVE KAGESANIKD
SVDDNHLSPS RWKWARKALS ETSSNKSYEN KYQEVSQKDS HEQLNNTSSS SPQHLSAQKL
EMLYNEITKT QTHSHPNPDC QEQPERPSAY EEEIEMEEVV CPQEQLAVAQ TEVIVDMKST
SSIDSFTSCA TDFTETERSP LPPPSASHLQ MKFPTDLPGM DEHQRVRAPP FLTLSRDKGP
AAREAALDYA PIDITVNLDA GASHGPLQPD SASDSPKSSL KGSNPLKSRS LKVNFQENRG
SAPQTPPSTA RPLPVTTADF PLTTPQHMST ILLEESPPPG TETLPGADVS AHCQGPSKGL
SPRVPKQKLF PFSSRERRSF TEIDTGEDED FLDLQRPRPD KQADPSPNCL ADKPGEARDP
LREEGCVGSS SPQNTDHNCR QDIYQAVGEV KKDSSQEGYK MENHLFAPEI HSNPGDTGYC
PTRETSM
