Swiss-Prot entry

ID   Q811T2_RAT  PRELIMINARY;      PRT;   758 AA.
AC   Q811T2;
DT   01-JUN-2003 (TrEMBLrel. 24, Created)
DT   01-JUN-2003 (TrEMBLrel. 24, Last sequence update)
DT   01-MAR-2004 (TrEMBLrel. 26, Last annotation update)
DE   Kv3.3d voltage gated potassium channel subunit splice variant.
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. 
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague-Dawley;
RA   Vega-Saenz de Miera E., Rudy B.;
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient (By similarity).
CC   -!- FUNCTION: This protein mediates the voltage-dependent potassium
CC       ion permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient (By similarity).
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein (By similarity).
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments (By similarity).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments (By similarity).
DR   EMBL; AY179604; AAO23561.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; O76457; 3KVT. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   GO; GO:0016021; C:integral to membrane; IEA.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA.
DR   GO; GO:0005515; F:protein binding; IEA.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA.
DR   GO; GO:0006812; P:cation transport; IEA.
DR   GO; GO:0006813; P:potassium ion transport; IEA.
DR   InterPro; IPR000210; BTB_POZ.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR001622; K+channel_pore.
DR   InterPro; IPR005404; KV3.3_channel.
DR   InterPro; IPR003968; Kv_channel.
DR   InterPro; IPR003091; K_channel.
DR   InterPro; IPR003131; K_tetra.
DR   InterPro; IPR005820; M+channel_nlg.
DR   InterPro; IPR003974; Shaw_channel.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01582; KV33CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   ProtoMap; Q811T2.
DR   PRESAGE; Q811T2.
DR   ModBase; Q811T2.
DR   SMR; Q811T2.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Ion transport; Ionic channel; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transport; Voltage-gated channel.
SQ   SEQUENCE   758 AA;  80783 MW;  BC6186BAFBC3A227 CRC64;
     MLSSVCVWSF SGRQGTRKQH SQPAPTPQPP ESSPPPLLPP PQQQCAQPGT AASPAGAPLS
     CGPGGRRAEP CSGLPAVAMG RHGGGGGDSG KIVINVGGVR HETYRSTLRT LPGTRLAGLT
     EPEAAARFDY DPGTDEFFFD RHPGVFAYVL NYYRTGKLHC PADVCGPLFE EELGFWGIDE
     TDVEACCWMT YRQHRDAEEA LDSFEAPDSS GNANANAGGA HDAGLDDEAG AGGGGLDGAG
     GELKRLCFQD AGGGAGGPAG GPGGAGGTWW RRWQPRVWAL FEDPYSSRAA RYVAFASLFF
     ILISITTFCL ETHEGFIHIS NKTVTQASPI PGAPPENITN VEVETEPFLT YVEGVCVVWF
     TFEFLMRVTF CPDKVEFLKS SLNIIDCVAI LPFYLEVGLS GLSSKAAKDV LGFLRVVRFV
     RILRIFKLTR HFVGLRVLGH TLRASTNEFL LLIIFLALGV LIFATMIYYA ERIGADPDDI
     LGSNHTYFKN IPIGFWWAVV TMTTLGYGDM YPKTWSGMLV GALCALAGVL TIAMPVPVIV
     NNFGMYYSLA MAKQKLPKKK NKHIPRPPQP GSPNYCKPDP PPPPPPHPHH GSGGISPPPP
     ITPPSMGVTV AGAYPPGPHT HPGLLRGGAG GLGIMGLPPL PAPGEPCPLA QEEVIETNRA
     DPRPNGDPAA AALAHEDCPA IDQPAMSPED KSPITPGSRG RYSRDRACFL VTDYAPSPDG
     SIRKATGAPP LPPPCWRKPG PPSFLPDLNA NAAAWISP
//