NCKX5_DANRE
ID NCKX5_DANRE Reviewed; 513 AA.
AC Q49SH1; Q49P06; Q592E6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Sodium/potassium/calcium exchanger 5;
DE AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 5;
DE AltName: Full=Protein golden;
DE AltName: Full=Solute carrier family 24 member 5;
DE Flags: Precursor;
GN Name=slc24a5; Synonyms=nckx5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=19414594; DOI=10.1128/mcb.00177-09;
RA Wittkopp N., Huntzinger E., Weiler C., Sauliere J., Schmidt S.,
RA Sonawane M., Izaurralde E.;
RT "Nonsense-mediated mRNA decay effectors are essential for zebrafish
RT embryonic development and survival.";
RL Mol. Cell. Biol. 29:3517-3528(2009).
CC -!- FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+)
CC and 1 K(+) to the melanosome in exchange for 4 cytoplasmic Na(+) (By
CC similarity). Involved in pigmentation, possibly by participating in ion
CC transport in melanosomes (PubMed:16357253). Predominant sodium-calcium
CC exchanger in melanocytes (PubMed:16357253).
CC {ECO:0000250|UniProtKB:Q71RS6, ECO:0000269|PubMed:16357253}.
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:0000305|PubMed:16357253}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000305|PubMed:16357253}. Note=Enriched
CC in late-stage melanosomes. {ECO:0000250|UniProtKB:Q71RS6}.
CC -!- TISSUE SPECIFICITY: Highly expressed in melanin-producing cells.
CC Colocalizes with melanin biosynthesis marker dct.
CC {ECO:0000269|PubMed:16357253}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the retinal pigment epithelium and in
CC the melanopore precursors at 1 day post-fertilization.
CC {ECO:0000269|PubMed:19414594}.
CC -!- DISRUPTION PHENOTYPE: Fishes show a delayed and reduced development of
CC pigmentation. They display a diminished number, size and density of
CC melanosomes. {ECO:0000269|PubMed:16357253}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC24A subfamily. {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; AY538713; AAY89721.1; -; mRNA.
DR EMBL; AY581204; AAS76476.1; -; Genomic_DNA.
DR EMBL; AY682553; AAY89722.1; -; mRNA.
DR RefSeq; NP_001025451.1; NM_001030280.1.
DR AlphaFoldDB; Q49SH1; -.
DR STRING; 7955.ENSDARP00000030499; -.
DR PaxDb; Q49SH1; -.
DR GeneID; 570312; -.
DR KEGG; dre:570312; -.
DR CTD; 283652; -.
DR eggNOG; KOG1307; Eukaryota.
DR InParanoid; Q49SH1; -.
DR OrthoDB; 1168500at2759; -.
DR PhylomeDB; Q49SH1; -.
DR PRO; PR:Q49SH1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; IEA:InterPro.
DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:InterPro.
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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..513
FT /note="Sodium/potassium/calcium exchanger 5"
FT /id="PRO_0000045755"
FT TOPO_DOM 36..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 192
FT /note="A -> S (in Ref. 1; AAS76476)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="R -> K (in Ref. 1; AAS76476)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="E -> D (in Ref. 1; AAS76476)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="D -> N (in Ref. 1; AAY89722)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="S -> R (in Ref. 1; AAY89722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56782 MW; 42023F56CFB37045 CRC64;
MRTDVFLQRR KRRDVLLSII ALLLLIFAIV HLVFCAGLSF QGSSSARVRR DLENASECVQ
PQSSEFPEGF FTVQERKDGG ILIYFMIIFY MLLSVSIVCD EYFLPSLEVI SERLGLSQDV
AGATFMAAGS SAPELVTAFL GVFVTKGDIG VSTIMGSAVY NLLCICAACG LLSSAVGRLS
CWPLFRDCVA YAISVAAVIA IISDNRVYWY DGACLLLVYG VYVAVLCFDL RISEYVMQRF
SPCCWCLKPR DRDSGEQQPL VGWSDDSSLR VQRRSRNDSG IFQDDSGYSH LSLSLHGLNE
ISDEHKSVFS MPDHDLKRIL WVLSLPVSTL LFVSVPDCRR PFWKNFYMLT FLMSAVWISA
FTYVLVWMVT IVGETLGIPD TVMGMTLLAA GTSIPDTVAS VMVAREGKSD MAMSNIVGSN
VFDMLCLGLP WFIQTVFVDV GSPVEVNSSG LVFMSCTLLL SIIFLFLAVH INGWKLDWKL
GLVCLACYIL FATLSILYEL GIIGNNPIRS CSD
