ID D3X752_CHICK Unreviewed; 1137 AA.
AC D3X752;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE AltName: Full=Slowpoke homolog {ECO:0000256|ARBA:ARBA00033447};
GN Name=kcnma1 {ECO:0000313|EMBL:ADD16638.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:ADD16638.1};
RN [1] {ECO:0000313|EMBL:ADD16638.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cochlea {ECO:0000313|EMBL:ADD16638.1};
RX PubMed=20479127; DOI=10.1128/MCB.00073-10;
RA Miranda-Rottmann S., Kozlov A.S., Hudspeth A.J.;
RT "Highly specific alternative splicing of transcripts encoding BK channels
RT in the chicken's cochlea is a minor determinant of the tonotopic
RT gradient.";
RL Mol. Cell. Biol. 30:3646-3660(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily.
CC {ECO:0000256|ARBA:ARBA00008648}.
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DR EMBL; GU223622; ADD16638.1; -; mRNA.
DR AlphaFoldDB; D3X752; -.
DR VEuPathDB; HostDB:geneid_374065; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR047871; K_chnl_Slo-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR048735; Slowpoke-like_C.
DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR PANTHER; PTHR10027:SF33; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT ALPHA-1; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF21014; Slowpoke_C; 1.
DR PRINTS; PR01449; BKCHANNELA.
DR PRINTS; PR00169; KCHANNEL.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000313|EMBL:ADD16638.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
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}.
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..355
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 505..592
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 957..1077
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
FT REGION 660..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1137 AA; 127633 MW; 0AE8B7DBC92566E2 CRC64;
MSNNINANNL NTDSSSSPVN VPKMDALIIP VTMEVPCDSR GQRMWWAFLA SSMVTFFGGL
FIILLWRTLK YLWTVCCHCG VKNKEAQKIN GGGDTQADGA CKPTDEKEEN VAAEVGWMTS
VKDWAGVMIS AQTLTGRVLV VLVFALSIGA LVIYFIDSSN PIESCQNFYK DFTLQIDMAF
NVFFLLYFGL RFIAANDKLW FWLEVNSVVD FFTVPPVFVS VYLNRSWLGL RFLRALRLIQ
FSEILQFLNI LKTSNSIKLV NLCSIFISTW LTAAGFIHLV ENSGDPWENF QNNQQLTYWE
CVYLLMVTMS TVGYGDVYAK TTLGRLFMVF FILGGLAMFA SYVPEIIELI GNRKKYGGSY
SAVSGRKHIV VCGHMTLESV SNFLKDFLHK DRDDVNVEIV FLHNISPNLE LEALFKRHFT
QVEFYQGSVL NPHDLARVKI ESADACLILA NKYCADPDAE DASNIMRVIS IKNYHPKIRI
ITQMLQYHNK AHLLNIPSWN WKEGDDAICL AELKLGFIAQ SCLAPGPSTM LANLFSMRSF
IKIEEDTWQK YYLEGVANEM YTEYLSSAFV GLSFPAVCEL VFAKLKLLMI AIEYKSEKRE
SSILINPGNH VKIQEGTLGF FIASDAKEVK RAFFYCKACH DDITDPKRIK KCGCKRLEDE
QPSTLSPKKK QRNGGMRNSP NSSPKLMRHD PLLIPGNEQI DNMDANVKKY DSTGMFHWCP
AKDIEKVILT RSEAAMTVLS GHVVVCIFGD VKSALIGLRN LVMPLRASNF HYHELKHIVF
VGSLEYLRRE WETLHNFPKV SILPGTPLSR ADLRAVNINL CDMCVILSAN QNNIDDASLQ
DKECILASLN IKSMQFDDSI GVLQANSQGF TPPGMDRSSP DNSPVHGLLR QPSITTGANI
PIITELVNDS NVQFLDQDDD DDPDTELYLT QPFACGTAFA VSVLDSLMSA TYFNDNILTL
IRTLVTGGAT PELEALIAEE NALRGGYSTP QTPANRDRCR VAQLALYDGP FADLGDGGCY
GDLFCKALKT YNMLCFGIYR LRDAHLSTPS QCTKRYVITN PPYEFELVPT DLIFCLMQFD
HNAGQSRASL SHSSHSSYSS SKKSSSVHSI PSTANRPNRT KTRDSREKQK YVQEDRL
//
