Swiss-Prot entry

ID   KCAB2_RAT      STANDARD;      PRT;   367 AA.
AC   P62483; P97381; Q60942; Q64284;
DT   16-OCT-2001 (Rel. 40, Created)
DT   16-OCT-2001 (Rel. 40, Last sequence update)
DT   13-SEP-2005 (Rel. 48, Last annotation update)
DE   Voltage-gated potassium channel beta-2 subunit (K(+) channel beta-2
DE   subunit) (Kv-beta-2).
GN   Name=Kcnab2; Synonyms=Ckbeta2, Kcnb3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Rattus. 
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain cortex;
RX   MEDLINE=94239521; PubMed=8183366 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/369289a0;
RA   Rettig J., Heinemann S.H., Wunder F., Lorra C., Parcej D.N.,
RA   Dolly J.O., Pongs O.;
RT   "Inactivation properties of voltage-gated K+ channels altered by
RT   presence of beta-subunit.";
RL   Nature 369:289-294(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-367, INTERACTION WITH
RP   KCNA1, AND TETRAMERIZATION.
RX   PubMed=10884227 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1126/science.289.5476.123;
RA   Gulbis J.M., Zhou M., Mann S., MacKinnon R.;
RT   "Structure of the cytoplasmic beta subunit-T1 assembly of voltage-
RT   dependent K+ channels.";
RL   Science 289:123-127(2000).
CC   -!- FUNCTION: Accessory potassium channel protein which modulates the
CC       activity of the pore-forming alpha subunit.
CC   -!- SUBUNIT: Forms heteromultimeric complex with alpha subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic (Potential).
CC   -!- DOMAIN: Alteration of functional properties of alpha subunit is
CC       mediated through N-terminal domain of beta subunit (Probable).
CC   -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC       family.
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CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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CC   --------------------------------------------------------------------------
DR   EMBL; X76724; CAA54142.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; S45312; S45312.
DR   PDB; 1EXB; X-ray; A=36-367. [ExPASy / RCSB]
DR   PDB; 1QRQ; X-ray; A/B/C/D=36-360. [ExPASy / RCSB]
DR   SMR; P62483; 36-361.
DR   Ensembl; ENSRNOG00000011550; Rattus_norvegicus
DR   RGD; 61828; Kcnab2.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR005401; KCNAB2_channel.
DR   InterPro; IPR005402; KCNAB3_channel.
DR   InterPro; IPR005399; KCNAB_channel.
DR   InterPro; IPR005983; KCNAB_euk.
DR   InterPro; Graphical view of domain structure.
DR   PANTHER; PTHR11732:SF69; KCNAB_channel; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   PRINTS; PR01579; KCNAB2CHANEL.
DR   PRINTS; PR01580; KCNAB3CHANEL.
DR   PRINTS; PR01577; KCNABCHANNEL.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   TIGRFAMs; TIGR01293; Kv_beta; 1.
DR   CMR; P62483.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P62483.
DR   ProtoNet; P62483.
DR   ProtoMap; P62483.
DR   PRESAGE; P62483.
DR   DIP; P62483.
DR   ModBase; P62483.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   3D-structure; Ion transport; Ionic channel; Phosphorylation;
KW   Potassium; Potassium transport; Transport; Voltage-gated channel.
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   STRAND       39     41       
FT   TURN         43     44       
FT   STRAND       48     50       
FT   STRAND       52     55       
FT   HELIX        59     63       
FT   HELIX        66     78       
FT   TURN         79     80       
FT   STRAND       83     87       
FT   TURN         88     89       
FT   HELIX        90     93       
FT   HELIX        94    106       
FT   TURN        107    107       
FT   HELIX       110    112       
FT   STRAND      114    119       
FT   STRAND      121    121       
FT   HELIX       126    128       
FT   STRAND      129    129       
FT   HELIX       133    147       
FT   TURN        148    148       
FT   STRAND      152    157       
FT   TURN        162    163       
FT   HELIX       166    178       
FT   TURN        179    180       
FT   STRAND      182    188       
FT   HELIX       192    205       
FT   TURN        206    206       
FT   STRAND      212    216       
FT   STRAND      218    218       
FT   TURN        219    220       
FT   STRAND      221    221       
FT   HELIX       223    227       
FT   TURN        228    228       
FT   HELIX       229    236       
FT   STRAND      239    243       
FT   TURN        245    246       
FT   HELIX       247    252       
FT   TURN        253    255       
FT   TURN        261    262       
FT   HELIX       264    266       
FT   TURN        268    269       
FT   HELIX       271    278       
FT   HELIX       280    299       
FT   TURN        300    300       
FT   HELIX       303    312       
FT   TURN        315    316       
FT   STRAND      317    322       
FT   HELIX       327    334       
FT   TURN        335    335       
FT   HELIX       336    339       
FT   HELIX       340    342       
FT   HELIX       345    355       
SQ   SEQUENCE   367 AA;  41021 MW;  5303FD1411B324FC CRC64;
     MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF
     GGQITDEMAE HLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF
     WGGKAETERG LSRKHIIEGL KASLERLQLE YVDVVFANRP DPNTPMEETV RAMTHVINQG
     MAMYWGTSRW SSMEIMEAYS VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA
     MTWSPLACGI VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
     CTLPQLAIAW CLRNEGVSSV LLGASNAEQL MENIGAIQVL PKLSSSIVHE IDSILGNKPY
     SKKDYRS
//