NCLX_CHICK
ID NCLX_CHICK Reviewed; 593 AA.
AC F1NXU8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 4.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Mitochondrial sodium/calcium exchanger protein {ECO:0000305};
DE AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 6 {ECO:0000250|UniProtKB:Q925Q3};
DE AltName: Full=Sodium/calcium exchanger protein, mitochondrial {ECO:0000250|UniProtKB:Q925Q3};
DE AltName: Full=Sodium/potassium/calcium exchanger 6 {ECO:0000250|UniProtKB:Q925Q3};
DE AltName: Full=Solute carrier family 8 member B1 {ECO:0000250|UniProtKB:Q6J4K2};
DE Flags: Precursor;
GN Name=SLC8B1 {ECO:0000250|UniProtKB:Q6J4K2};
GN Synonyms=NCKX6 {ECO:0000250|UniProtKB:Q925Q3},
GN NCLX {ECO:0000250|UniProtKB:Q925Q3};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION.
RX PubMed=27328625; DOI=10.1038/srep28378;
RA Kim B., Takeuchi A., Hikida M., Matsuoka S.;
RT "Roles of the mitochondrial Na(+)-Ca(2+) exchanger, NCLX, in B lymphocyte
RT chemotaxis.";
RL Sci. Rep. 6:28378-28378(2016).
CC -!- FUNCTION: Mitochondrial sodium/calcium antiporter that mediates sodium-
CC dependent calcium efflux from mitochondrion, by mediating the exchange
CC of 3 sodium ions per 1 calcium ion (By similarity). Plays a central
CC role in mitochondrial calcium homeostasis by mediating mitochondrial
CC calcium extrusion: calcium efflux is essential for mitochondrial
CC function and cell survival, notably in cardiomyocytes (By similarity).
CC Involved in B-lymphocyte chemotaxis (PubMed:27328625).
CC {ECO:0000250|UniProtKB:Q6J4K2, ECO:0000250|UniProtKB:Q925Q3,
CC ECO:0000269|PubMed:27328625}.
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:0000250|UniProtKB:Q6J4K2};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q6J4K2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6J4K2}.
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; AADN04000321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1NXU8; -.
DR STRING; 9031.ENSGALP00000013555; -.
DR PaxDb; F1NXU8; -.
DR VEuPathDB; HostDB:geneid_417032; -.
DR eggNOG; KOG2399; Eukaryota.
DR HOGENOM; CLU_004979_3_2_1; -.
DR InParanoid; F1NXU8; -.
DR OrthoDB; 478735at2759; -.
DR TreeFam; TF323444; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; ISS:UniProtKB.
DR GO; GO:0086038; F:calcium:sodium antiporter activity involved in regulation of cardiac muscle cell membrane potential; ISS:UniProtKB.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0099093; P:calcium export from the mitochondrion; ISS:UniProtKB.
DR GO; GO:0006812; P:cation transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:1901623; P:regulation of lymphocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR Pfam; PF01699; Na_Ca_ex; 2.
PE 3: Inferred from homology;
KW Antiport; Calcium; Calcium transport; Glycoprotein; Ion transport; Lithium;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Sensory transduction; Sodium; Sodium transport; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..593
FT /note="Mitochondrial sodium/calcium exchanger protein"
FT /id="PRO_0000440954"
FT TOPO_DOM 21..93
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..178
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..239
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..369
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..428
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..496
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..564
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 268..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 593 AA; 64331 MW; 0CA63B8306228EFC CRC64;
MGPLWALRVA GALSVAGVLA GHDGSQRAGQ PAALDAGTRG DGVGHDRGVD CREVRKRNSS
ERCRFVRGTP DCRLDGGFLD YLGGAFCTFP SSLLPLSVSL YALWLLYLFV ILGVTAEKFF
CPNLSAISTN LKLSHNGLGV VGHSLTPALH GVTFLAFGNG APDIFSAVVA FSDPRTAGLA
VGAIFGAGIF VTTVVAGGIA LVKPFAAASR PFLRDVIFYM VAVFLTFLVL YFGYITLGEA
LGYLGLYVFY VFTVVLCTWI HRWQRGDGPP PPGPWEPAIP TDAEEQESSG TNCGDYGEEY
RPLLPYHETS LHILSTALSP LDKHKWRRKP WYWRLFKVLK VPVELVLLLT VPVVDPDKDD
LNWKRPLNCL HIVTGPLLCI FTLKSGAYGL YQIQGVFPVW ALVALAGSVL AIIVFVTTHN
EEPPKYHCVF AFLGFLSSAM WINAAATELV NILRTLGIIF ELSNTVLGLT LLAWGNSIGD
TFSDLTMARQ GYPRMAFSAC FGGIIFNILV GVGLGCLLQM TNSQMVVKLE PDSLLVWILA
GALGLSLVFS FVAVPAQCFQ LGKAYGTCLI LYYLVFLCVA LLTEFRVIHL AAT
