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Database: UniProt
Entry: KCNB2_RABIT
LinkDB: KCNB2_RABIT
Original site: KCNB2_RABIT 
ID   KCNB2_RABIT             Reviewed;         911 AA.
AC   Q95L11;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-SEP-2017, entry version 93.
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;
GN   Name=KCNB2 {ECO:0000250|UniProtKB:Q92953};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12399537;
RA   Malysz J., Farrugia G., Ou Y., Szurszewski J.H., Nehra A.,
RA   Gibbons S.J.;
RT   "The Kv2.2 alpha subunit contributes to delayed rectifier K(+)
RT   currents in myocytes from rabbit corpus cavernosum.";
RL   J. Androl. 23:899-910(2002).
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
CC       transmembrane potassium transport in excitable membranes,
CC       primarily in the brain and smooth muscle cells. Channels open or
CC       close in response to the voltage difference across the membrane,
CC       letting potassium ions pass in accordance with their
CC       electrochemical gradient. Homotetrameric channels mediate a
CC       delayed-rectifier voltage-dependent outward potassium current that
CC       display rapid activation and slow inactivation in response to
CC       membrane depolarization. Can form functional homotetrameric and
CC       heterotetrameric channels that contain variable proportions of
CC       KCNB1; channel properties depend on the type of alpha subunits
CC       that are part of the channel. Can also form functional
CC       heterotetrameric channels with other alpha subunits that are non-
CC       conducting when expressed alone, such as KCNS1 and KCNS2, creating
CC       a functionally diverse range of channel complexes. In vivo,
CC       membranes probably contain a mixture of heteromeric potassium
CC       channel complexes, making it difficult to assign currents observed
CC       in intact tissues to any particular potassium channel family
CC       member. Contributes to the delayed-rectifier voltage-gated
CC       potassium current in cortical pyramidal neurons and smooth muscle
CC       cells. {ECO:0000250|UniProtKB:A6H8H5,
CC       ECO:0000250|UniProtKB:Q63099}.
CC   -!- ENZYME REGULATION: Inhibited by quinine at micromolar levels.
CC       Modestly sensitive to millimolar levels of tetraethylammonium
CC       (TEA) and 4-aminopyridine (4-AP). {ECO:0000250|UniProtKB:Q63099,
CC       ECO:0000250|UniProtKB:Q95167, 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
CC         that, inactivate very slowly. Their activation requires low
CC         threshold potentials of about -20 to -30 mV, with a midpoint
CC         activation at about 10 mV. For inactivation, the voltage at
CC         half-maximal amplitude is about -30 mV. Channels have an unitary
CC         conductance of about 14 pS. The voltage-dependence of activation
CC         and inactivation and other channel characteristics vary
CC         depending on the experimental conditions, the expression system
CC         and post-translational modifications.
CC         {ECO:0000250|UniProtKB:Q63099, ECO:0000305|PubMed:10414301};
CC   -!- SUBUNIT: Homotetramer or heterotetramer with KCNB1. Heterotetramer
CC       with KCNS1 and KCNS2. {ECO:0000250|UniProtKB:Q63099}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q63099}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q63099}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q63099}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q63099}. Note=Localized uniformly
CC       throughout cell bodies and dendrites. Colocalizes with KCNB1 to
CC       high-density somatodendritic clusters on cortical pyramidal
CC       neurons. {ECO:0000250|UniProtKB:Q63099}.
CC   -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
CC       and is characterized by a series of positively charged amino acids
CC       at every third position. Channel opening and closing is effected
CC       by a conformation change that affects the position and orientation
CC       of the voltage-sensor paddle formed by S3 and S4 within the
CC       membrane. A transmembrane electric field that is positive inside
CC       would push the positively charged S4 segment outwards, thereby
CC       opening the pore, while a field that is negative inside would pull
CC       the S4 segment inwards and close the pore. Changes in the position
CC       and orientation of S4 are then transmitted to the activation gate
CC       formed by the inner helix bundle via the S4-S5 linker region.
CC       {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}.
DR   EMBL; AY037947; AAK84954.1; -; mRNA.
DR   RefSeq; NP_001075606.1; NM_001082137.1.
DR   UniGene; Ocu.2697; -.
DR   ProteinModelPortal; Q95L11; -.
DR   SMR; Q95L11; -.
DR   STRING; 9986.ENSOCUP00000002420; -.
DR   GeneID; 100008877; -.
DR   KEGG; ocu:100008877; -.
DR   CTD; 9312; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   HOGENOM; HOG000113206; -.
DR   HOVERGEN; HBG052225; -.
DR   InParanoid; Q95L11; -.
DR   KO; K04886; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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: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:0072661; P:protein targeting to plasma membrane; ISS:UniProtKB.
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.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03521; Kv2channel; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01515; KV22CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01495; SHABCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Complete proteome; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    911       Potassium voltage-gated channel subfamily
FT                                B member 2.
FT                                /FTId=PRO_0000054049.
FT   TOPO_DOM      1    190       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    191    212       Helical; Name=Segment S1.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    213    232       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    233    254       Helical; Name=Segment S2.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    255    265       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    266    284       Helical; Name=Segment S3.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    285    296       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    297    317       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    318    332       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    333    354       Helical; Name=Segment S5.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    355    368       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    369    380       Helical; Name=Pore helix.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    381    388       {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    389    395       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    396    424       Helical; Name=Segment S6.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    425    911       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOTIF       381    386       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOD_RES     448    448       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q63099}.
FT   CARBOHYD    287    287       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   911 AA;  102279 MW;  69353D0664C5D689 CRC64;
     MAEKAPPGLN RKTSRSTLSL PPEPVDIIKS KTCSRRVKIN VGGLNHEVLW RTLDRLPRTR
     LGKLRDCNTH ESLLEVCDDY NLGDNEYFFD RHPGAFTSIL NFYRTGKLHM MEEMCALSFG
     QELDYWGIDE IYLESCCQAR YHQKKEQMNE ELRREAETMR EREGEEFDNT CCPEKRKKLW
     DLLEKPNSSV AAKILAIVSI LFIVLSTIAL SLNTLPELQE TDEFGQPSDN PKLAHVEAVC
     IAWFTMEYLL RFLSSPNKWK FFKGPLNVID LLAILPYYVT IFLTESNKSV LQFQNVRRVV
     QIFRIMRILR ILKLARHSTG LQSLGFTLRR SYNELGLLIL FLAMGIMIFS SLVFFAEKDE
     DATKFTSIPA SFWWATITMT TVGYGDIYPK TLLGKIVGGL CCIAGVLVIA LPIPIIVNNF
     SEFYKEQKRQ EKAIKRREAL ERAKRNGSIV SMNLKDAFAR SMELIDVAVE KAGETANTKD
     SADDNHLSPS RWKWARKALS ESSSNKSYEN KYQEVSQKDS HEQLNNTSSS SPQHLSAQKL
     EMLYNEITKT QPHSHQAPDC QEQPERPSAY EEEIEMEEVV CPQEQLAVAQ TEVIVDMKST
     SSIDSFTSCA TDFTETERSP LPPPSASHLH MKFPTDFPGT EEHQRARGPP FLTLTREKGP
     AAREGALEYS PIDITVNLDA GSSQCGLHGP LQSDSATDSP KSSLKGSNPL KSRSLKVNFK
     ENRGSAPQTP PSTARPLPVT TADFSLSTPQ HISTILLEES PAQGDRLLLD AELPAQCQGL
     AKGLSPRFPK QKLFAFSSRE RRSFTEIDTG EDEDFLELQG ARADKQADSS PNCFAEKPSD
     ARHPLSEEGC GGSSSPPNTG HNCRQDSFHA VGEVQKDSSQ EGYKMENHLF APEIHSNPGD
     TGYCPTRETS M
//
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