KCNB2_CANLF
ID KCNB2_CANLF Reviewed; 809 AA.
AC Q95167;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Potassium voltage-gated channel subfamily B member 2 {ECO:0000250|UniProtKB:Q92953};
DE AltName: Full=Voltage-gated potassium channel subunit Kv2.2;
DE Flags: Fragment;
GN Name=KCNB2 {ECO:0000250|UniProtKB:Q92953};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9612272; DOI=10.1152/ajpgi.1998.274.5.g901;
RA Schmalz F., Kinsella J., Koh S.D., Vogalis F., Schneider A., Flynn E.R.,
RA Kenyon J.L., Horowitz B.;
RT "Molecular identification of a component of delayed rectifier current in
RT gastrointestinal smooth muscles.";
RL Am. J. Physiol. 274:G901-G911(1998).
RN [2]
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).
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:9612272). 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:9612272).
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. Can also form
CC functional heterotetrameric channels with other alpha subunits that are
CC non-conducting when expressed alone, such as KCNS1 and KCNS2, creating
CC a functionally diverse range of channel complexes. In vivo, membranes
CC probably contain a mixture of heteromeric potassium channel complexes,
CC making it difficult to assign currents observed in intact tissues to
CC any particular potassium channel family member. Contributes to the
CC delayed-rectifier voltage-gated potassium current in cortical pyramidal
CC neurons and smooth muscle cells (By similarity).
CC {ECO:0000250|UniProtKB:A6H8H5, ECO:0000250|UniProtKB:Q63099,
CC ECO:0000269|PubMed:9612272}.
CC -!- ACTIVITY REGULATION: Inhibited by quinine at micromolar levels
CC (PubMed:9612272). Modestly sensitive to millimolar levels of
CC tetraethylammonium (TEA) and 4-aminopyridine (4-AP) (PubMed:9612272).
CC {ECO:0000250|UniProtKB:Q63099, ECO:0000269|PubMed:9612272,
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. After that,
CC inactivate very slowly (PubMed:9612272). Their activation requires
CC low threshold potentials of about -20 to -30 mV, with a midpoint
CC activation at about 10 mV. For inactivation, the voltage at half-
CC maximal amplitude is about -30 mV. Channels have an unitary
CC conductance of about 14 pS (PubMed:9612272). The voltage-dependence
CC of activation and inactivation and other channel characteristics vary
CC depending on the experimental conditions, the expression system and
CC post-translational modifications. {ECO:0000269|PubMed:9612272,
CC ECO:0000305|PubMed:10414301};
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCNB1. Heterotetramer with
CC KCNS1 and KCNS2. {ECO:0000250|UniProtKB:Q63099}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9612272};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q63099}. Perikaryon
CC {ECO:0000250|UniProtKB:Q63099}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63099}. Note=Localized uniformly throughout
CC cell bodies and dendrites. Colocalizes with KCNB1 to high-density
CC somatodendritic clusters on cortical pyramidal neurons.
CC {ECO:0000250|UniProtKB:Q63099}.
CC -!- TISSUE SPECIFICITY: Expressed in smooth muscle cells (PubMed:9612272).
CC {ECO:0000269|PubMed:9612272}.
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. {ECO:0000250|UniProtKB:Q63099}.
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=AAB08432.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U69963; AAB08432.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001003247.1; NM_001003247.1.
DR AlphaFoldDB; Q95167; -.
DR SMR; Q95167; -.
DR STRING; 9615.ENSCAFP00000053736; -.
DR PaxDb; Q95167; -.
DR PRIDE; Q95167; -.
DR GeneID; 403925; -.
DR CTD; 9312; -.
DR eggNOG; KOG3713; Eukaryota.
DR InParanoid; Q95167; -.
DR OrthoDB; 203440at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS: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 Cell membrane; Cell projection; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..>809
FT /note="Potassium voltage-gated channel subfamily B member
FT 2"
FT /id="PRO_0000054047"
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..354
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 355..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..809
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 549..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..809
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..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63099"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 809
SQ SEQUENCE 809 AA; 90602 MW; E1FF56334F3DA9C8 CRC64;
MAEKAPPGLN RKTSRSTLSL PPEPVDIIRS KTCSRRVKIN VGGLNHEVLW RTPDRLPRTR
LGKLRDCNTH ESLLEVCDDY NLGHNEYFFD RHPGAFTSIL NFYRTGKLHM MEEMCALSVG
QELDYWGIDE IYLESCCQAR YHQKKEQMNE ELRREAETMR DGEGEEFDNT CCPEKRKKSR
DLLEKPNSSV AAKILAIVSN LFIVLSTIAL SLNTLPELQE MDEFGQPNDN PQLAHVEAVC
NAWFTMEYLL RFLSSPNKWK FFKGPLNVID LLAILPYYVT IFLTESNKSV LQFQNVRRVV
QIFRIMRILR ILKLARHSTG LQSLGFTLRR SYNELGLLIL FLAMGIMIFS SLVFFAEKDA
DATKFTSIPA SFWWATITMT TVGYGDIYPK TLLGKSVGGL CCIAGVLVIA LPIPIIVPPF
SEFYKEQKRQ EKAIKRREAL ERAKRNGSIV SMNLKDAFAR SMELIDVAVE KAGESSSTKD
SADDNHLSPS RWKWARKALS ETSSNKSYEN KYQEVSQKDS HEQLNNTSSS SPQHLSAQKL
EMLYNEITKT QPHPAPNPDG QEQPDRPSAY EEEIEMEEVV CPQEQLAVAQ GEVIVDMKST
SSIDSFTSCA TDFTETERSP LPPLSASHLQ MRFPPDLAGT DEHQRARGPP FLMLARGKGP
AGRDAILEYA PVDITVSLDA SGSKVGSHGP LQPDSASESP KSSLKGSNPL KSRSLRVNFK
ENRGSAPQTP PSTARPLPVT TADFSLTAPQ LISTILLEET PSQGDRPLLG AEGSAHCQGP
SKGLSPRFPK QKLFPFSSRE RRSFTEIDT
