NCKX1_CHICK
ID NCKX1_CHICK Reviewed; 663 AA.
AC Q9IAL8;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
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: Precursor;
GN Name=SLC24A1; Synonyms=NCKX1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RC TISSUE=Retina;
RX PubMed=10662833; DOI=10.1523/jneurosci.20-04-01424.2000;
RA Prinsen C.F.M., Szerencsei R.T., Schnetkamp P.P.M.;
RT "Molecular cloning and functional expression of the potassium-dependent
RT sodium-calcium exchanger from human and chicken retinal cone
RT photoreceptors.";
RL J. Neurosci. 20:1424-1434(2000).
CC -!- FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+)
CC and 1 K(+) in exchange for 4 Na(+) (PubMed:10662833). Critical
CC component of the visual transduction cascade, controlling the calcium
CC concentration of outer segments during light and darkness. Light causes
CC a rapid lowering of cytosolic free calcium in the outer segment of both
CC retinal rod and cone photoreceptors and the light-induced lowering of
CC calcium is caused by extrusion via this protein which plays a key role
CC in the process of light adaptation (By similarity).
CC {ECO:0000250|UniProtKB:O60721, ECO:0000269|PubMed:10662833}.
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:10662833};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28139};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Retinal rods. Localizes to the inner segment of rod
CC photoreceptors. {ECO:0000269|PubMed:10662833}.
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; AF177984; AAF25808.1; -; mRNA.
DR RefSeq; NP_001001773.1; NM_001001773.1.
DR AlphaFoldDB; Q9IAL8; -.
DR SMR; Q9IAL8; -.
DR STRING; 9031.ENSGALP00000012102; -.
DR PaxDb; Q9IAL8; -.
DR GeneID; 414892; -.
DR KEGG; gga:414892; -.
DR CTD; 9187; -.
DR VEuPathDB; HostDB:geneid_414892; -.
DR eggNOG; KOG1307; Eukaryota.
DR InParanoid; Q9IAL8; -.
DR OrthoDB; 1168500at2759; -.
DR PhylomeDB; Q9IAL8; -.
DR PRO; PR:Q9IAL8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IGI:ARUK-UCL.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:ARUK-UCL.
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 PANTHER; PTHR10846; PTHR10846; 2.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR TIGRFAMs; TIGR00367; TIGR00367; 1.
PE 2: Evidence at transcript level;
KW Antiport; Calcium; Calcium transport; Cell membrane; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Repeat; Sensory transduction; Signal; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN 1..663
FT /note="Sodium/potassium/calcium exchanger 1"
FT /id="PRO_0000019366"
FT SIGNAL 1..?
FT /note="Not cleaved"
FT /evidence="ECO:0000250|UniProtKB:Q28139"
FT TOPO_DOM 32..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..574
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 170..210
FT /note="Alpha-1"
FT REPEAT 543..574
FT /note="Alpha-2"
FT REGION 308..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 663 AA; 73772 MW; DD624E3080C43082 CRC64;
MHLPRRRRLQ RNRIFFFLAV VSLLSVYQLQ FSPSAIPALL TAHQHEDPVK VTSREPFRNK
TSKTGNVTAA PKIRHCVYID PEPTVPITAS EDTTQRENVN ESYPDEKPVY ESKGEYPQDL
FSVEERRQGW VVLHIFGMMY VFVALAIVCD EYFVPALGVI TEKLQISEDV AGATFMAAGG
SAPELFTSLI GVFISHSNVG IGTIVGSAVF NILFVIGTCA LFSREILHLT WWPLFRDISF
YIVDLLMLIL FFLDSVIDWW ESLLLLTAYA TYVFTMKHNV SLEQWVKEEL SKKLNAVQAA
SAEHMRKKSS VAVAEDGTKP ADGKKLQPTT ALQRGTSSAS LHNSQMRSTI FQLMIHTLDP
LAGAKFKDRV DILSNIAKVK ADSLTGQGTK PEAEEEKQAS QNTVQVTPAS DSEPSKDKQK
EDTPQDGQPP SDSDNSEDSS SDSEDDSDDD STDDEENDEP LSLEWPETRK KQAIYLFLFP
IVFPLWSTIP DVRNPDSKKF FVITFFGSII WIAAFSYLMV WWAHQVGETI GISEEIMGLT
ILAAGTSIPD LITSVIVARK GLGDMAVSSS VGSNIFDITV GLPVPWFLYS VFNGFSPVAV
SSNGLFCAIV LLFLMLLFVI ISIALCKWKM NKILGVTMFA LYFVFLIISV MLEDRIISCP
VSV
