NCKX1_MOUSE
ID NCKX1_MOUSE Reviewed; 1130 AA.
AC Q91WD8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 {ECO:0000312|MGI:MGI:2384871}; Synonyms=Nckx1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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; BC016094; AAH16094.1; -; mRNA.
DR RefSeq; NP_659062.1; NM_144813.1.
DR RefSeq; XP_017168760.1; XM_017313271.1.
DR AlphaFoldDB; Q91WD8; -.
DR STRING; 10090.ENSMUSP00000035616; -.
DR PhosphoSitePlus; Q91WD8; -.
DR PaxDb; Q91WD8; -.
DR PRIDE; Q91WD8; -.
DR ProteomicsDB; 340913; -.
DR Antibodypedia; 26029; 133 antibodies from 23 providers.
DR DNASU; 214111; -.
DR Ensembl; ENSMUST00000037798; ENSMUSP00000035616; ENSMUSG00000034452.
DR GeneID; 214111; -.
DR KEGG; mmu:214111; -.
DR UCSC; uc009qcl.1; mouse.
DR CTD; 9187; -.
DR MGI; MGI:2384871; Slc24a1.
DR VEuPathDB; HostDB:ENSMUSG00000034452; -.
DR eggNOG; KOG1307; Eukaryota.
DR GeneTree; ENSGT01030000234532; -.
DR HOGENOM; CLU_007948_6_0_1; -.
DR InParanoid; Q91WD8; -.
DR OMA; WPESRQK; -.
DR OrthoDB; 1168500at2759; -.
DR PhylomeDB; Q91WD8; -.
DR TreeFam; TF318759; -.
DR Reactome; R-MMU-425561; Sodium/Calcium exchangers.
DR BioGRID-ORCS; 214111; 6 hits in 74 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91WD8; protein.
DR Bgee; ENSMUSG00000034452; Expressed in retinal neural layer and 19 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; ISO:MGI.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
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:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
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 2: Evidence at transcript level;
KW Antiport; Calcium; Calcium transport; Cell membrane; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sensory transduction; Signal; Symport; Transmembrane; Transmembrane helix;
KW Transport; Vision.
FT CHAIN 1..1130
FT /note="Sodium/potassium/calcium exchanger 1"
FT /id="PRO_0000455293"
FT SIGNAL 1..?
FT /note="Not cleaved"
FT /evidence="ECO:0000250|UniProtKB:Q28139"
FT TOPO_DOM 1..419
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..489
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 960..966
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 988..1002
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1024..1041
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1063..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1092..1099
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1100..1120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1121..1130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 461..501
FT /note="Alpha-1"
FT /evidence="ECO:0000305"
FT REPEAT 1010..1041
FT /note="Alpha-2"
FT /evidence="ECO:0000305"
FT REGION 104..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..778
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..828
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..928
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60721"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1130 AA; 124667 MW; 65C144872D9B532F CRC64;
MGKLIRMGTQ ERRLLRPKRL HWSRLLFLLG MLIIGSTYQH LRRPQNPPSM WTKVSSQQPI
KLAVRDLPNN EMAVAGSDPP EASSEVEDGM LAAQDTVIMD EAAPSIAMED TPNPPRTTKI
PPASLKNSYS PTTAGTRRQK ENIPPTPSGA PSHFISTPGR QRVKSYIPKP RGERKNSSPT
HAREKGRTHT PSPAGAHTIS PTATVRDRET MATYRLLETR FERTAGETTA ASLKRMVLNT
PTFLTHEVET NLMTSSSLVG KNTAVSLRKG ERNISTTPQG AVPQHTPATS EEQMTVSTRM
GSIPATIEGS TAARRINNPL SRTSAPAIRI ASATNREKRP STAPSTLVTP KATMSTQVHR
CVVVEPAPAV PMTPSPGVTS ILFPETPSSG PSALPPGWPN LHPKAEYPPD LFSVEDRRQG
WVVLHIFGMM YVFVALAIVC DEYFVPALGV ITHKLQISED VAGATFMAAG GSAPELFTSL
IGVFISHSNV GIGTIVGSAV FNILFVIGTC ALFSREILNL TWWPLFRDVS FYILDLSMLI
VFFLDSFIAW WESLLLLLAY ALYVFTMKWN KQIELWVKEQ LSRRPVAKVM ALGDLSKPSE
DAVEENEQQD SKKLKLPSVL TRGSSSASLH NSIIRNTIYH LMLHSLDPLG EARPSKDKQE
SLNQEARVLS QTKAESSPDE DEPAELPAVT VTPAPAPDAK GDQEDDPGCQ EDVDEAERRG
EMTGEEGEKE TETEGKKDEQ EGETEAERKE DEQEEETEAE GKEQEGETEA EGKEDEQEGE
TEAEGKKDEQ EGETEAEGKE EQEGETEAEG KEDEQEGETE AEGKEEQEGE TEAESKEVEQ
ERETEAEGKD KHEGQGETQP DDTEVKDGEG ETEANAEDQC EATQGEKGAD GGGESDGGDS
EEEEDEEDEE EEEEEDEEEE EEENEEPLSL EWPDSRQKQA IYLFLLPIVF PLWLTIPDVR
RQESRKFFVI TFLGSIIWIA MFSYLMVWWA HQVGETIGIS EEIMGLTILA AGTSIPDLIT
SVIVARKGLG DMAVSSSVGS NIFDITVGLP VPWLLFSLIN ALQPVPVSSN GLFCAIVLLF
LMLLFVIFSI ASCKWRMNKI LGFTMFLLYF VFLVISVMLE DRIISCPVSV