NCKX1_BISBI
ID NCKX1_BISBI Reviewed; 300 AA.
AC O46383;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Sodium/potassium/calcium exchanger 1;
DE AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 1;
DE AltName: Full=Retinal rod Na-Ca+K exchanger;
DE AltName: Full=Solute carrier family 24 member 1;
DE Flags: Fragment;
GN Name=SLC24A1; Synonyms=NCKX1;
OS Bison bison (American bison) (Bos bison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bison.
OX NCBI_TaxID=9901;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9478004;
RA Tucker J.E., Winkfein R.J., Cooper C.B., Schnetkamp P.P.M.;
RT "cDNA cloning of the human retinal rod Na-Ca + K exchanger: comparison with
RT a revised bovine sequence.";
RL Invest. Ophthalmol. Vis. Sci. 39:435-440(1998).
CC -!- FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+)
CC and 1 K(+) in exchange for 4 Na(+). Critical component of the visual
CC transduction cascade, controlling the calcium concentration of outer
CC segments during light and darkness. Light causes a rapid lowering of
CC cytosolic free calcium in the outer segment of both retinal rod and
CC cone photoreceptors and the light-induced lowering of calcium is caused
CC by extrusion via this protein which plays a key role in the process of
CC light adaptation. {ECO:0000250|UniProtKB:O60721}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in)
CC + 4 Na(+)(out); Xref=Rhea:RHEA:69967, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q28139};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28139};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: The uncleaved signal sequence is required for efficient membrane
CC targeting and proper membrane integration and topology.
CC {ECO:0000250|UniProtKB:Q28139}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC24A subfamily. {ECO:0000305}.
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DR EMBL; AF025480; AAC13320.1; -; mRNA.
DR AlphaFoldDB; O46383; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR004481; K/Na/Ca-exchanger.
DR PANTHER; PTHR10846; PTHR10846; 1.
PE 2: Evidence at transcript level;
KW Antiport; Calcium; Calcium transport; Cell membrane; Ion transport;
KW Membrane; Potassium; Potassium transport; Sensory transduction; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN <1..>300
FT /note="Sodium/potassium/calcium exchanger 1"
FT /id="PRO_0000209495"
FT TRANSMEM 259..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 300
SQ SEQUENCE 300 AA; 31671 MW; 2BE592DA5AB9781E CRC64;
DPGSQGVGAE AENTGERTGG EAEAPAEGEN GERSGGDAAL GGESEGKAEN ESEGDIPAER
RGDDEDEGEI QAEGGEVKGD EDEGEIQAGE GGEVEGDEDE GEIQAGEGGE VEGDEDEGEI
QAGEGGEVEG DEDEGEIQAG EGGEVKDDEG EIQAGEAGEV EGEDGEVEGG EDEGEIQAGE
GGEGETGEQE LNAEIQGEAK DDEEGVDGEG GGDGGDSEDE EEEDEEEDEE EEEEEEEEEE
EENEQPLSLE WPETRRKQAI YLFLLPIVFP LWLTVPDVRR LEAKKFFVIT FLGSILWIAM
