ID U3K1I0_FICAL Unreviewed; 913 AA.
AC U3K1I0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Potassium voltage-gated channel subfamily B member 2 {ECO:0000256|ARBA:ARBA00015830};
GN Name=KCNB2 {ECO:0000313|Ensembl:ENSFALP00000008884.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000008884.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000008884.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000008884.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
CC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily.
CC {ECO:0000256|ARBA:ARBA00009411}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005042237.1; XM_005042180.1.
DR AlphaFoldDB; U3K1I0; -.
DR STRING; 59894.ENSFALP00000008884; -.
DR Ensembl; ENSFALT00000008922.2; ENSFALP00000008884.1; ENSFALG00000008520.2.
DR GeneID; 101818041; -.
DR KEGG; fab:101818041; -.
DR CTD; 9312; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000161902; -.
DR HOGENOM; CLU_011722_2_0_1; -.
DR OMA; YNPINRA; -.
DR OrthoDB; 1478695at2759; -.
DR Proteomes; UP000016665; Chromosome 2.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR CDD; cd18412; BTB_POZ_KCNB2; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF134; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY B MEMBER 2; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 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; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 190..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..144
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..169
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 102890 MW; E81F45E94BB836B2 CRC64;
MAEKAPPGIT KKSSRSTLSL PPEPVEIIRS KACSRRVKIN VGGLNHEVLW RTLDRLPRTR
LGKLRDCNTH ESLLEVCDDY NLNENEYFFD RHPGAFTSIL NFYRTGKLHM MEEMCALSFG
QELDYWGIDE IYLESCCQAR YHQKKEQMNE ELRREAETLR EREGEEFDNT CCPEKRKKLW
DLLEKPNSSV AAKILAIVSI LFIVLSTIAL SLNTLPELQE IDEFGQPNDN PQLAHVEAVC
IAWFTMEYLL RFLSSPNKWK FFKGPLNVID LLAILPYYVT IFLTESNKSV LQFQNVRRVV
QIFRIMRILR ILKLARHSTG LQSLGFTLRR SYNELGLLIL FLAMGIMIFS SLVFFAEKDE
DATKFTSIPA SFWWATITMT TVGYGDIYPK TLLGKIVGGL CCIAGVLVIA LPIPIIVNNF
SEFYKEQKRQ EKAIKRREAL ERAKRNGSIV SMNLKDAFAR SMEMIDVAVD SGKLGEPLSP
KEIPDDSHLS PSRWKWARRT VSETSSNKSY ENKYQEVSQR DSHEQLNNAA ASSSPQHLSA
QKLEMLYNEI TKTQSQPNLN AGYQDQSAKP PRYEEEIEME EVIGHRDPLP AGPADIVMDM
RSTSSIDSFA SCATDFTETE RSPLSLFPGS HLQMRFPTDA VNLEDNQRAR SSQFIPFAKD
RGFSPTDVTF DYNPINRAVI SDGSGSQTVS HGHFHFDTAM ESPKSSLKGS NPLKSRSLKV
NFKDNRGGAP QTPPSTARPL PVTAGADFTQ ATPQHISTIL LEENSPQGER PVLGADASAL
GQGPAKKSSP LFPKQKLFTF PSKERRSFTE IDTGEEEEFM ELHGVKHEKK QDIKTNCCGD
KHSDGNNLTG EPQITSSPKS MSHNCTQDIY HAVGEVKPDS NQEGHKMENH LFAPEIHSSP
GETAYCPTRE TSM
//
