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NCKX5_MOUSE
ID   NCKX5_MOUSE             Reviewed;         501 AA.
AC   Q8C261; Q6XE39; Q8CJF1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Sodium/potassium/calcium exchanger 5;
DE   AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 5;
DE   AltName: Full=Solute carrier family 24 member 5;
DE   Flags: Precursor;
GN   Name=Slc24a5; Synonyms=Nckx5;
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 [MRNA].
RC   STRAIN=BALB/cJ;
RA   Satoh J., Smith C., Romero M.F.;
RT   "Cloning and characterization of a novel, mouse renal divalent cation
RT   transporter (JSX).";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ishibashi K.;
RT   "Cloning of a new member of Na-Ca exchanger.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16357253; DOI=10.1126/science.1116238;
RA   Lamason R.L., Mohideen M.-A.P.K., Mest J.R., Wong A.C., Norton H.L.,
RA   Aros M.C., Jurynec M.J., Mao X., Humphreville V.R., Humbert J.E., Sinha S.,
RA   Moore J.L., Jagadeeswaran P., Zhao W., Ning G., Makalowska I.,
RA   McKeigue P.M., O'Donnell D., Kittles R., Parra E.J., Mangini N.J.,
RA   Grunwald D.J., Shriver M.D., Canfield V.A., Cheng K.C.;
RT   "SLC24A5, a putative cation exchanger, affects pigmentation in zebrafish
RT   and humans.";
RL   Science 310:1782-1786(2005).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=22677781; DOI=10.1159/000337493;
RA   Hu P., Lacruz R.S., Smith C.E., Smith S.M., Kurtz I., Paine M.L.;
RT   "Expression of the sodium/calcium/potassium exchanger, NCKX4, in
RT   ameloblasts.";
RL   Cells Tissues Organs 196:501-509(2012).
CC   -!- FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+)
CC       and 1 K(+) to the melanosome in exchange for 4 cytoplasmic Na(+).
CC       Involved in pigmentation, possibly by participating in ion transport in
CC       melanosomes. Predominant sodium-calcium exchanger in melanocytes.
CC       {ECO:0000250|UniProtKB:Q71RS6}.
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:Q71RS6};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:Q71RS6}; Multi-pass membrane protein
CC       {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q71RS6}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in melanin-producing cells such as
CC       skin and eye compared to other tissues. Strongly overexpressed in
CC       melanoma cell lines. Expressed in dental tissues.
CC       {ECO:0000269|PubMed:16357253, ECO:0000269|PubMed:22677781}.
CC   -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC       family. SLC24A subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC24122.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Skin-deep - Issue 74 of
CC       September 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/074";
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DR   EMBL; AY236527; AAP57526.1; -; mRNA.
DR   EMBL; AB085629; BAC24122.1; ALT_FRAME; mRNA.
DR   EMBL; AK089225; BAC40800.1; -; mRNA.
DR   EMBL; BC094232; AAH94232.1; -; mRNA.
DR   CCDS; CCDS38226.1; -.
DR   RefSeq; NP_778199.2; NM_175034.3.
DR   AlphaFoldDB; Q8C261; -.
DR   STRING; 10090.ENSMUSP00000063887; -.
DR   iPTMnet; Q8C261; -.
DR   PhosphoSitePlus; Q8C261; -.
DR   MaxQB; Q8C261; -.
DR   PaxDb; Q8C261; -.
DR   PRIDE; Q8C261; -.
DR   ProteomicsDB; 252929; -.
DR   Antibodypedia; 24489; 98 antibodies from 28 providers.
DR   DNASU; 317750; -.
DR   Ensembl; ENSMUST00000070353; ENSMUSP00000063887; ENSMUSG00000035183.
DR   GeneID; 317750; -.
DR   KEGG; mmu:317750; -.
DR   UCSC; uc008mbv.1; mouse.
DR   CTD; 283652; -.
DR   MGI; MGI:2677271; Slc24a5.
DR   VEuPathDB; HostDB:ENSMUSG00000035183; -.
DR   eggNOG; KOG1307; Eukaryota.
DR   GeneTree; ENSGT01030000234532; -.
DR   HOGENOM; CLU_007948_5_0_1; -.
DR   InParanoid; Q8C261; -.
DR   OMA; RLWAWIT; -.
DR   OrthoDB; 1168500at2759; -.
DR   PhylomeDB; Q8C261; -.
DR   TreeFam; TF318759; -.
DR   Reactome; R-MMU-425561; Sodium/Calcium exchangers.
DR   BioGRID-ORCS; 317750; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Slc24a5; mouse.
DR   PRO; PR:Q8C261; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8C261; protein.
DR   Bgee; ENSMUSG00000035183; Expressed in blastocyst and 73 other tissues.
DR   ExpressionAtlas; Q8C261; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; IDA:ARUK-UCL.
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:0070509; P:calcium ion import; 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:0034220; P:ion transmembrane transport; ISO:MGI.
DR   GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
DR   GO; GO:0030318; P:melanocyte differentiation; IBA:GO_Central.
DR   GO; GO:0048022; P:negative regulation of melanin biosynthetic process; IMP:MGI.
DR   GO; GO:0050896; P:response to stimulus; 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; IPR030245; SLC24A5.
DR   PANTHER; PTHR10846; PTHR10846; 1.
DR   PANTHER; PTHR10846:SF61; PTHR10846:SF61; 1.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   TIGRFAMs; TIGR00367; TIGR00367; 1.
PE   2: Evidence at transcript level;
KW   Antiport; Calcium; Calcium transport; Golgi apparatus; Ion transport;
KW   Membrane; Potassium; Potassium transport; Reference proteome;
KW   Sensory transduction; Signal; Sodium; Sodium transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..501
FT                   /note="Sodium/potassium/calcium exchanger 5"
FT                   /id="PRO_0000045754"
FT   TOPO_DOM        30..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..136
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..305
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..334
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..438
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..470
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        492..501
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        40
FT                   /note="T -> K (in Ref. 2; BAC24122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="I -> V (in Ref. 1; AAP57526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="A -> G (in Ref. 2; BAC24122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="S -> C (in Ref. 2; BAC24122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474
FT                   /note="V -> L (in Ref. 2; BAC24122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        488
FT                   /note="I -> V (in Ref. 2; BAC24122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  54984 MW;  B0AFD2BE7FC7AB34 CRC64;
     MRTKWGPTWT RRVLLLGIFW VSAYLPVRGV SLPPRLPRAT GNSTQCAVSP ASEFPEGFFT
     KQESTDGGIV IYFLIILYMC MAISIVCDKY FLPSLEIISD SLGLSQDVAG ATFMAAGSSA
     PELVTAFLGV FITKGDIGIS TILGSAIYNL LGICAACGLL SNMVSTLSCW PLFRDCAVYA
     VSVGAVFGII FDNRIYWYEG AGLLLIYGLY VLLLCFDTTI SRHVMKTCSP CCPCLARAME
     ERIEQQTLLG WEDESQLFIR RQSRTDSGIF QEDSGYSQLS LSLHGLSQVS EDPPSVFSMP
     EADLRRIFWV LSLPIITLLA LTTPDCRRKF WKNYFVITFF MSALWISAFT YILVWMVTVT
     GETLGIPDTV MGLTLLAAGT SIPDTVTSVL VARKGKGDMA ISNIVGSNVF DMLCLGLPWF
     IKTAFTNASA PIEVNSKGLT YITISLNISI LFLFLAVHFN GWKLDRKLGV VCLVLYLGLA
     TLSVLYEIGI IGNNRIRGCG V
 
 
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