NAH_SCHPO
ID NAH_SCHPO Reviewed; 468 AA.
AC P36606;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Na(+)/H(+) antiporter;
GN Name=sod2; ORFNames=SPAC977.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1314171; DOI=10.1002/j.1460-2075.1992.tb05209.x;
RA Jia Z.-P., McCullough N., Martel R., Hemmingsen S., Young P.G.;
RT "Gene amplification at a locus encoding a putative Na+/H+ antiporter
RT confers sodium and lithium tolerance in fission yeast.";
RL EMBO J. 11:1631-1640(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9094438; DOI=10.1016/s0014-5793(97)00169-5;
RA Dibrov P., Smith J.J., Young P.G., Fliegel L.;
RT "Identification and localization of the sod2 gene product in fission
RT yeast.";
RL FEBS Lett. 405:119-124(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449 AND SER-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Sodium export from cell, takes up external protons in
CC exchange for internal sodium ions. Involved in regulation of pH.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the fungal Na(+)/H(+) exchanger family.
CC {ECO:0000305}.
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DR EMBL; Z11736; CAA77796.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB69632.1; -; Genomic_DNA.
DR PIR; S20951; S20951.
DR RefSeq; NP_592782.1; NM_001018182.2.
DR PDB; 2M7X; NMR; -; A=125-154.
DR PDBsum; 2M7X; -.
DR AlphaFoldDB; P36606; -.
DR SMR; P36606; -.
DR BioGRID; 279667; 6.
DR STRING; 4896.SPAC977.10.1; -.
DR TCDB; 2.A.36.4.3; the monovalent cation:proton antiporter-1 (cpa1) family.
DR iPTMnet; P36606; -.
DR MaxQB; P36606; -.
DR PaxDb; P36606; -.
DR PRIDE; P36606; -.
DR EnsemblFungi; SPAC977.10.1; SPAC977.10.1:pep; SPAC977.10.
DR GeneID; 2543239; -.
DR KEGG; spo:SPAC977.10; -.
DR PomBase; SPAC977.10; sod2.
DR VEuPathDB; FungiDB:SPAC977.10; -.
DR eggNOG; KOG4505; Eukaryota.
DR HOGENOM; CLU_008635_5_0_1; -.
DR InParanoid; P36606; -.
DR OMA; FARDGWF; -.
DR PhylomeDB; P36606; -.
DR PRO; PR:P36606; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:PomBase.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:PomBase.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:PomBase.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:PomBase.
DR GO; GO:0051452; P:intracellular pH reduction; IMP:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:PomBase.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IMP:PomBase.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004712; Na+/H+_antiporter_fungi.
DR PANTHER; PTHR31382:SF4; PTHR31382:SF4; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..468
FT /note="Na(+)/H(+) antiporter"
FT /id="PRO_0000052405"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:2M7X"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:2M7X"
SQ SEQUENCE 468 AA; 52177 MW; 04908860E57B9069 CRC64;
MGWRQLDIDK VHLALIVAGG FITFFCYFSE VFRKKLLVGE AVLGSITGLI FGPHAAKLVD
PFSWGDHGDY LTVEICRIVL DVRVFASAIE LPGAYFQHNF RSIIVMLLPV MAYGWLVTAG
FAYALFPQIN FLGSLLIAGC ITSTDPVLSA LIVGEGPLAK KTPERIRSLL IAESGCNDGM
AVPFFYFAIK LLTVKPSRNA GRDWVLLVVL YECAFGIFFG CVIGYLLSFI LKHAQKYRLI
DAISYYSLPL AIPLLCSGIG TIIGVDDLLM SFFAGILFNW NDLFSKNISA CSVPAFIDQT
FSLLFFTYYG TIIPWNNFNW SVEGLPVWRL IVFSILTLVC RRLPVVFSVK PLVPDIKTWK
EALFVGHFGP IGVCAVYMAF LAKLLLSPDE IEKSIYESTT VFSTLNEIIW PIISFVILSS
IIVHGFSIHV LVIWGKLKSL YLNRKVTKSD SDLELQVIGV DKSQEDYV
