NCKX1_BOVIN
ID NCKX1_BOVIN Reviewed; 1216 AA.
AC Q28139; O46384;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
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;
GN Name=SLC24A1; Synonyms=NCKX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 66-88; 232-249;
RP 647-660 AND 1119-1136, FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=1582405; DOI=10.1002/j.1460-2075.1992.tb05219.x;
RA Reilaender H., Achilles A., Friedel U., Maul G., Lottspeich F., Cook N.J.;
RT "Primary structure and functional expression of the Na/Ca,K-exchanger from
RT bovine rod photoreceptors.";
RL EMBO J. 11:1689-1695(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 725-1216 (ISOFORM 1).
RC TISSUE=Retina;
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).
RN [3]
RP FUNCTION OF THE N-TERMINUS IN TARGETING, MUTAGENESIS OF ARG-65, AND
RP GLYCOSYLATION.
RX PubMed=10608890; DOI=10.1074/jbc.274.53.38177;
RA McKiernan C.J., Friedlander M.;
RT "The retinal rod Na(+)/Ca(2+),K(+) exchanger contains a noncleaved signal
RT sequence required for translocation of the N-terminus.";
RL J. Biol. Chem. 274:38177-38182(1999).
CC -!- FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+)
CC and 1 K(+) in exchange for 4 Na(+) (PubMed:1582405, PubMed:10608890).
CC Critical component of the visual transduction cascade, controlling the
CC calcium concentration of outer segments during light and darkness.
CC Light causes a rapid lowering of cytosolic free calcium in the outer
CC segment of both retinal rod and cone photoreceptors and the light-
CC induced lowering of calcium is caused by extrusion via this protein
CC which plays a key role in the process of light adaptation (By
CC similarity). {ECO:0000250|UniProtKB:O60721,
CC ECO:0000269|PubMed:10608890, ECO:0000269|PubMed:1582405}.
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:0000305|PubMed:1582405};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:1582405};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q28139-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28139-2; Sequence=VSP_006159;
CC -!- TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:1582405}.
CC -!- PTM: The uncleaved signal sequence is required for efficient membrane
CC targeting and proper membrane integration and topology.
CC {ECO:0000269|PubMed:10608890}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10608890}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC24A subfamily. {ECO:0000305}.
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 EMBL; X66481; CAA47108.1; -; mRNA.
DR EMBL; AF025664; AAB88884.1; -; mRNA.
DR PIR; S20969; S20969.
DR RefSeq; NP_777080.1; NM_174655.2. [Q28139-2]
DR AlphaFoldDB; Q28139; -.
DR STRING; 9913.ENSBTAP00000036386; -.
DR TCDB; 2.A.19.4.1; the ca(2+):cation antiporter (caca) family.
DR PaxDb; Q28139; -.
DR PRIDE; Q28139; -.
DR GeneID; 282474; -.
DR KEGG; bta:282474; -.
DR CTD; 9187; -.
DR eggNOG; KOG1307; Eukaryota.
DR HOGENOM; CLU_007948_6_0_1; -.
DR InParanoid; Q28139; -.
DR OrthoDB; 1168500at2759; -.
DR TreeFam; TF318759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004481; K/Na/Ca-exchanger.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR InterPro; IPR004817; SLC24A1.
DR PANTHER; PTHR10846; PTHR10846; 2.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR TIGRFAMs; TIGR00927; 2A1904; 2.
DR TIGRFAMs; TIGR00367; TIGR00367; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Calcium; Calcium transport; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome; Repeat;
KW Sensory transduction; Signal; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport; Vision.
FT CHAIN 1..1216
FT /note="Sodium/potassium/calcium exchanger 1"
FT /id="PRO_0000223302"
FT SIGNAL 1..?
FT /note="Not cleaved"
FT /evidence="ECO:0000269|PubMed:10608890"
FT TOPO_DOM 1..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..1024
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1025..1045
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1046..1052
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1074..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1110..1127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1149..1157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1158..1178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1179..1185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1186..1206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1207..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 488..528
FT /note="Alpha-1"
FT REPEAT 796..811
FT /note="1; approximate"
FT REPEAT 812..828
FT /note="2"
FT REPEAT 829..845
FT /note="3"
FT REPEAT 846..862
FT /note="4"
FT REPEAT 863..879
FT /note="5"
FT REPEAT 880..896
FT /note="6"
FT REPEAT 897..913
FT /note="7"
FT REPEAT 914..928
FT /note="8; approximate"
FT REPEAT 1096..1127
FT /note="Alpha-2"
FT REGION 94..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..928
FT /note="8 X 17 AA tandem repeats of D-E-D-E-G-E-I-Q-A-G-E-
FT [GA]-G-E-V-[EK]-G"
FT COMPBIAS 107..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..904
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..945
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1014
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 717
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60721"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 868..884
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1582405"
FT /id="VSP_006159"
FT MUTAGEN 65
FT /note="R->A: Does not affect the targeting."
FT /evidence="ECO:0000269|PubMed:10608890"
FT CONFLICT 84
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..245
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="A -> G (in Ref. 2; AAB88884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 131614 MW; 39F149A74D1D0523 CRC64;
MGKLIRMGAQ ERRSLWPKRL HWSRPLFLLG MLIIGSTYQY LTSPQGLPTL WAAVSSQHPV
KVASRDLSNK EMMMVSSETS KSSSEMEVEA WAPEATAGRD GTPPGIARKN TPSTPRGTAS
ITPAIPNNYS PTPTGTGKVK EDTSATPSGV LNHYTQSRPM VNSYTRLTAR GEVKSSRPTQ
SRGKEEKYSP SPLGRMVNSY APSTLMTMPR SHGITPRTTV KDREIMATKK MLATNPSKRL
VEKTTPTPLK GITDNTPTFL LSDLETDTLT SPRNVVEKKT LTTPRRVDSN SSTNHQGLVG
KNNLTTPQGM VLEHTAAVSE GQVTISTMTR SSPTETKAST DAWKVRNPLP RTSAPIIRIS
SATFRGLLKN PSKAPSTPAA PRVRANPTIQ VRHCLVVEPA PVAPTAPSPS WTTAVIPGIP
SPSGQPDLYP KAEYPRDLFS VEERRQGWVV LHIFGMMYVF VALAIVCDEY FVPALGVITD
KLQISEDVAG ATFMAAGGSA PELFTSLIGV FISHSNVGIG TIVGSAVFNI LFVIGTCALF
SREILNLTWW PLFRDITFYI FDLMMLILFF LDSLIAWWES VLLLLAYAFY VFTMKWNQQL
ELWVKEQLNK RPVAKVMALG DLSKPGDGTV VVDEQQDNKK LKLSSMLTRG SSSASLHNST
IRSTIYQLML HSLDPLGEAR PSKDKEEETL IPEAKATPQA KAESKPEEEP AKLPEVTVTP
APAPDVKGDQ EEDPGSQGVG AEAENTGERT GGEAEAPAEG ENGERSGGDA ALGGESEGKA
ENESEGDIPA ERRGDDEDEG EIQAEGGEVK GDEDEGEIQA GEGGEVEGDE DEGEIQAGEG
GEVEGDEDEG EIQAGEAGEV EGDEDEGEIQ AGEGGEVEGD EDEGEIQAGE AGEVEGDEDE
GEIQAGEGGE VKGDEGEIQA GEAGEVEGED GEVEGGEDEG EIQAGEGGEG ETGEQELNAE
IQGEAKDDEE GVDGEGGGDG GDSEDEEEED EEEEDEEEEE EEEEEEEEEN EQPLSLEWPE
TRRKQAIYLF LLPIVFPLWL TVPDVRRLEA KKFFVITFLG SILWIAMFSY LMVWWAHQVG
ETIGISEEIM GLTILAAGTS IPDLITSVIV ARKGLGDMAV SSSVGSNIFD ITVGLPLPWM
LFSLINGLQP VAVSSNGLFC AIVLLFLMLL FVISSIALCK WRMNKILGFT MFLLYFVFLI
ISVMLEDRII SCPVSV
