PBO4_CAEEL
ID PBO4_CAEEL Reviewed; 783 AA.
AC G5EBK1;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Na(+)/H(+) exchanger protein 7 {ECO:0000303|PubMed:18291648};
DE AltName: Full=Na(+)/H(+) antiporter nhx-7 {ECO:0000303|PubMed:12021279};
DE AltName: Full=PBoc defective protein pbo-4 {ECO:0000303|PubMed:18291648};
GN Name=pbo-4 {ECO:0000312|EMBL:CAA91995.2, ECO:0000312|WormBase:K09C8.1};
GN Synonyms=nhx-7 {ECO:0000312|EMBL:AAM18109.1}; ORFNames=K09C8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM18109.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12021279; DOI=10.1074/jbc.m203200200;
RA Nehrke K., Melvin J.E.;
RT "The NHX family of Na+-H+ exchangers in Caenorhabditis elegans.";
RL J. Biol. Chem. 277:29036-29044(2002).
RN [2] {ECO:0000312|EMBL:CAA91995.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA91995.2};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-318.
RX PubMed=18191228; DOI=10.1016/j.cell.2007.10.058;
RA Beg A.A., Ernstrom G.G., Nix P., Davis M.W., Jorgensen E.M.;
RT "Protons act as a transmitter for muscle contraction in C. elegans.";
RL Cell 132:149-160(2008).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18291648; DOI=10.1016/j.cub.2008.01.054;
RA Pfeiffer J., Johnson D., Nehrke K.;
RT "Oscillatory transepithelial H(+) flux regulates a rhythmic behavior in C.
RT elegans.";
RL Curr. Biol. 18:297-302(2008).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CMD-1, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-271; 541-MET--LEU-545; 569-LYS-LYS-570
RP AND THR-618.
RX PubMed=23319594; DOI=10.1074/jbc.m112.434852;
RA Allman E., Waters K., Ackroyd S., Nehrke K.;
RT "Analysis of Ca2+ signaling motifs that regulate proton signaling through
RT the Na+/H+ exchanger NHX-7 during a rhythmic behavior in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 288:5886-5895(2013).
RN [6]
RP FUNCTION.
RX PubMed=25849533; DOI=10.1371/journal.pone.0124515;
RA Sheng M., Hosseinzadeh A., Muralidharan S.V., Gaur R., Selstam E., Tuck S.;
RT "Aberrant fat metabolism in Caenorhabditis elegans mutants with defects in
RT the defecation motor program.";
RL PLoS ONE 10:E0124515-E0124515(2015).
CC -!- FUNCTION: Na+/H+ exchanger which mediates the transient acidification
CC of the coelomic space and plays a role in contraction of posterior body
CC muscles during defecation (PubMed:18191228, PubMed:18291648,
CC PubMed:23319594). Probably by regulating the defecation motor program,
CC required for fatty acid uptake by intestinal cells (PubMed:25849533).
CC {ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:18291648,
CC ECO:0000269|PubMed:23319594, ECO:0000269|PubMed:25849533}.
CC -!- SUBUNIT: Interacts (via C-terminus) with cmd-1.
CC {ECO:0000269|PubMed:23319594}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:12021279, ECO:0000269|PubMed:18191228,
CC ECO:0000269|PubMed:23319594}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12021279, ECO:0000269|PubMed:18191228,
CC ECO:0000269|PubMed:23319594}.
CC -!- TISSUE SPECIFICITY: Detected in the posterior cells of the intestine.
CC {ECO:0000269|PubMed:12021279, ECO:0000269|PubMed:18191228}.
CC -!- DISRUPTION PHENOTYPE: Loss of posterior body wall muscle contractions
CC (pBoc), weak movement of tail, weak enteric muscle contractions, severe
CC reduction in acidification of the pseudocoelom and slight constipation.
CC Normal oscillatory Ca(2+) signaling in the intestine with unaffected
CC defecation period and timing and normal locomotion.
CC {ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:18291648,
CC ECO:0000269|PubMed:23319594}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF497831; AAM18109.1; -; mRNA.
DR EMBL; Z68006; CAA91995.2; -; Genomic_DNA.
DR PIR; T23539; T23539.
DR RefSeq; NP_509830.2; NM_077429.5.
DR AlphaFoldDB; G5EBK1; -.
DR SMR; G5EBK1; -.
DR STRING; 6239.K09C8.1; -.
DR EPD; G5EBK1; -.
DR PaxDb; G5EBK1; -.
DR PeptideAtlas; G5EBK1; -.
DR EnsemblMetazoa; K09C8.1.1; K09C8.1.1; WBGene00003943.
DR GeneID; 181285; -.
DR KEGG; cel:CELE_K09C8.1; -.
DR CTD; 181285; -.
DR WormBase; K09C8.1; CE31034; WBGene00003943; pbo-4.
DR eggNOG; KOG1966; Eukaryota.
DR HOGENOM; CLU_005912_4_3_1; -.
DR InParanoid; G5EBK1; -.
DR OMA; LVNEREW; -.
DR OrthoDB; 412663at2759; -.
DR PhylomeDB; G5EBK1; -.
DR Reactome; R-CEL-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-CEL-425986; Sodium/Proton exchangers.
DR PRO; PR:G5EBK1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003943; Expressed in larva and 2 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; IMP:UniProtKB.
DR GO; GO:1904731; P:positive regulation of intestinal lipid absorption; IMP:UniProtKB.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IMP:WormBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0030641; P:regulation of cellular pH; IMP:WormBase.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR004709; NaH_exchanger.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Antiport; Calmodulin-binding; Cell membrane; Coiled coil; Glycoprotein;
KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..783
FT /note="Na(+)/H(+) exchanger protein 7"
FT /id="PRO_0000424354"
FT TRANSMEM 1..18
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 19..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 745..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 649..702
FT /evidence="ECO:0000255"
FT COMPBIAS 757..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 271
FT /note="E->Q: Limited Na(+)/H(+) exchange activity, low
FT amplitude pH oscillations and reduced strength in pBoc."
FT /evidence="ECO:0000269|PubMed:23319594"
FT MUTAGEN 318
FT /note="G->R: In sa300; complete loss of posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228,
FT ECO:0000269|PubMed:18291648"
FT MUTAGEN 541..545
FT /note="MVQHL->RRQHR: Reduced pBoc strength, low amplitude
FT pH oscillations, and suppressed ability to rescue pBoc
FT defect in the null mutant. Accumulates in intracellular
FT space."
FT /evidence="ECO:0000269|PubMed:23319594"
FT MUTAGEN 569..570
FT /note="KK->AA: Reduced Na(+)/H(+) exchange activity but
FT complete rescue of pBoc defect in the null mutant."
FT /evidence="ECO:0000269|PubMed:23319594"
FT MUTAGEN 618
FT /note="T->A: Increased Na(+)/H(+) exchange activity and
FT strong extended pBoc. Complete rescue of pBoc defect in the
FT null mutant."
FT /evidence="ECO:0000269|PubMed:23319594"
SQ SEQUENCE 783 AA; 88410 MW; 06A1C6BFAC64281A CRC64;
MWIKLLFFFT TLLVSTSGLG DDGITALLDP NSTEFSTVLP SNNSEKFSYM LASVKNMNMT
ASEFEEFIKV LKHRQSKDHS GEHVGNEHDE SHGISVVSWH WDYVKNELVL TLFFIVIGLF
KLVYHHTFVT RKILPESCCL IFIGIAIGFF FVGDATHASI KFLEFKSKVF FFYLLPPIIL
ESAYSLKDRA FIENIGTILL YAVVGTILNI VLLAAALLIL IWVGIMGKYN LSVMDILTFA
SLVAAVDPVA VLAVFQEVGV NKMLYFMVFG ESLFNDAVTI VCYNLAIEFQ TLPDFTWYHG
FLGLLSFLCV SIGGLIIGLI CGAISSFVTK FTTDVRVVEP VVLFGMAYLA YLGSEMFHFS
GIIALIACGL FQTHYACCNI SYKSFTSVMY ITKVCSTLCE SLIFIILGVM LVNEREWFWT
DWHPVFSAVS VVLCVVVRFG VTFFLTYFVN QFTGGVRHIS FQEQFIMSYG GLRGAVSFSL
VFMISANPDV KNTMLGATYA VILFTNIIQG STIKLFVKWL NIRLAKKEDH FRLFIEFNNG
MVQHLSQGIE DLCGDKSLSL INRMSELSKK YVRPLLEKNY TANKAKKEGK LVELNRAVAM
REALNNSPSQ SSFQRQHTID EMAESGALPH DLLDEEHQGH HHHGQVHPDN EDADQRANEL
IKDVSSIRQL MHNPFEDCYL DRNLTHEEEK EQARLKMKKT RAFKFSSVRK TIGFFGKKKS
VRRHATQQGI LHSAIATIGV QSVDRPSTST RVSVEDEEQG LTMKEMEEEH PLMTITESEE
TSF
