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Database: UniProt
Entry: A0A0G2JZK7_RAT
LinkDB: A0A0G2JZK7_RAT
Original site: A0A0G2JZK7_RAT 
ID   A0A0G2JZK7_RAT          Unreviewed;       921 AA.
AC   A0A0G2JZK7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Solute carrier family 8 member A2 {ECO:0000313|Ensembl:ENSRNOP00000071086.2};
GN   Name=Slc8a2 {ECO:0000313|Ensembl:ENSRNOP00000071086.2,
GN   ECO:0000313|RGD:620194};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000071086.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000071086.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071086.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000071086.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071086.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in);
CC         Xref=Rhea:RHEA:69955, ChEBI:CHEBI:29101, ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00033667};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC       family. SLC8 subfamily. {ECO:0000256|ARBA:ARBA00007489}.
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DR   AlphaFoldDB; A0A0G2JZK7; -.
DR   Ensembl; ENSRNOT00000086396.2; ENSRNOP00000071086.2; ENSRNOG00000001492.8.
DR   RGD; 620194; Slc8a2.
DR   VEuPathDB; HostDB:ENSRNOG00000001492; -.
DR   GeneTree; ENSGT00940000158344; -.
DR   OMA; PEDKHQK; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000001492; Expressed in frontal cortex and 10 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JZK7; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0005432; F:calcium:sodium antiporter activity; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990034; P:calcium ion export across plasma membrane; IEA:Ensembl.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0007612; P:learning; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0099608; P:regulation of action potential firing pattern; IEA:Ensembl.
DR   GO; GO:0106056; P:regulation of calcineurin-mediated signaling; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR   Gene3D; 2.60.40.2030; -; 2.
DR   Gene3D; 1.20.1420.30; NCX, central ion-binding region; 2.
DR   InterPro; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR004836; Na_Ca_Ex.
DR   InterPro; IPR032452; Na_Ca_Ex_C-exten.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR   NCBIfam; TIGR00845; caca; 1.
DR   PANTHER; PTHR11878; SODIUM/CALCIUM EXCHANGER; 1.
DR   PANTHER; PTHR11878:SF8; SODIUM_CALCIUM EXCHANGER 2; 1.
DR   Pfam; PF03160; Calx-beta; 2.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   Pfam; PF16494; Na_Ca_ex_C; 1.
DR   PRINTS; PR01259; NACAEXCHNGR.
DR   SMART; SM00237; Calx_beta; 2.
DR   SUPFAM; SSF141072; CalX-like; 2.
PE   3: Inferred from homology;
KW   Antiport {ECO:0000256|ARBA:ARBA00022449};
KW   Calcium {ECO:0000256|ARBA:ARBA00022568};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ   SEQUENCE   921 AA;  100495 MW;  8062A6015A9F90B0 CRC64;
     MAPLALVGVA LLLGAPHCLG EATPTPSLPP PPANDSDASP GGCQGSYRCQ PGVLLPVWEP
     DDPSLGDKAA RAVVYFVAMV YMFLGVSIIA DRFMASIEVI TSKEKEITIT KANGETSVGT
     VRIWNETVSN LTLMALGSSA PEILLSVIEV CGHNFQAGEL GPGTIVGSAA FNMFVVIAVC
     VYVIPAGESR KIKHLRVFFV TASWSIFAYV WLYLILAVFS PGVVQVWEAL LTLVFFPVCV
     VFAWMADKRL LFYKYVYKRY RTDPRSGIII GAEGDPPKSI ELDGTFVGTE VPGELGALGT
     GPAEARELDA SRREVIQILK DLKQKHPDKD LEQLVGIAKY YALLHQQKSR AFYRIQATRL
     MTGAGNVLRR HAADAARRPG ANDGAPDDED DGASRIFFEP SLYHCLENCG SVLLSVACQG
     GEGNSTFYVD YRTEDGSAKA GSDYEYSEGT LVFKPGETQK ELRIGIIDDD IFEEDEHFFV
     RLLNLRVGDA QGMFEPDGGG RPKGRLVAPL LATVTILDDD HAGIFSFQDR LLHVSECMGT
     VDVRVVRSSG ARGTVRLPYR TVDGTARGGG VHYEDACGEL EFGDDETMKT LQVKIVDDEE
     YEKKDNFFIE LGQPQWLKRG ISALLLNQGD GDRKLTAEEE EAQRIAEMGK PVLGENCRLE
     VIIEESYDFK NTVDKLIKKT NLALVIGTHS WREQFLEAVT VSAGDEEEDE DGSREERLPS
     CFDYVMHFLT VFWKVLFACV PPTEYCHGWA CFGVCILVIG LLTALIGDLA SHFGCTVGLK
     DSVNAVVFVA LGTSIPDTFA SKVAALQDQC ADASIGNVTG SNAVNVFLGL GVAWSVAAVY
     WAVQGRPFEV RTGTLAFSVT LFTVFAFVGI AVLLYRRRPH IGGELGGPRG PKLATTALFL
     GLWFLYILFA SLEAYCHIRG F
//
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