NHE1_DICDI
ID NHE1_DICDI Reviewed; 674 AA.
AC Q552S0; Q86IB9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Sodium/hydrogen exchanger 1;
DE Short=DdNHE1;
DE Short=NHE1;
DE Short=Na-H exchanger 1;
DE Flags: Precursor;
GN Name=nhe1; ORFNames=DDB_G0275711;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, ACTIVITY
RP REGULATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15851518; DOI=10.1083/jcb.200412145;
RA Patel H., Barber D.L.;
RT "A developmentally regulated Na-H exchanger in Dictyostelium discoideum is
RT necessary for cell polarity during chemotaxis.";
RL J. Cell Biol. 169:321-329(2005).
RN [4]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
CC -!- FUNCTION: Regulation of intracellular pH homeostasis in response to
CC cAMP, which is essential for chemotaxis. Necessary for F-actin
CC localization and the kinetics of actin polymerization during chemotaxis
CC and cell polarity but not for directional sensing.
CC {ECO:0000269|PubMed:15851518}.
CC -!- ACTIVITY REGULATION: LY294002, an inhibitor of the catalytic subunit of
CC PI3-kinase, blocks NHE1-dependent (but not NHE1-independent) increase
CC in intracellular pH in response to cAMP. {ECO:0000269|PubMed:15851518}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Predominantly localizes to the leading-edge
CC of the chemotaxing polarized cells. {ECO:0000269|PubMed:15851518}.
CC -!- DEVELOPMENTAL STAGE: Expressed in chemotactically competent cells but
CC in not vegetative cells. {ECO:0000269|PubMed:15851518}.
CC -!- INDUCTION: Expression is induced 6 hours after starvation. Down-
CC regulated by Pseudomonas aeruginosa infection (strains PAO1 and PA14).
CC {ECO:0000269|PubMed:15851518, ECO:0000269|PubMed:18590548}.
CC -!- DISRUPTION PHENOTYPE: Impaired polarity. Starved mutant cells
CC differentiate, and in response to the chemoattractant cAMP retain
CC directional sensing; however, they cannot attain a polarized
CC morphology, but instead extend mislocalized pseudopodia around the cell
CC and exhibit decreased velocity. In response to chemoattractant, mutant
CC cells lack a leading edge localization of F-actin and have
CC significantly attenuated de novo F-actin polymerization but increased
CC abundance of membrane-associated phosphatidylinositol 3,4,5-
CC trisphosphate. However, they retain directional sensing.
CC {ECO:0000269|PubMed:15851518}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69606.1; -; Genomic_DNA.
DR RefSeq; XP_643611.1; XM_638519.1.
DR AlphaFoldDB; Q552S0; -.
DR SMR; Q552S0; -.
DR STRING; 44689.DDB0231789; -.
DR TCDB; 2.A.36.1.11; the monovalent cation:proton antiporter-1 (cpa1) family.
DR PaxDb; Q552S0; -.
DR EnsemblProtists; EAL69606; EAL69606; DDB_G0275711.
DR GeneID; 8620198; -.
DR KEGG; ddi:DDB_G0275711; -.
DR dictyBase; DDB_G0275711; nhe1.
DR eggNOG; KOG1965; Eukaryota.
DR HOGENOM; CLU_005912_11_0_1; -.
DR InParanoid; Q552S0; -.
DR OMA; RPHSLRM; -.
DR PhylomeDB; Q552S0; -.
DR Reactome; R-DDI-425986; Sodium/Proton exchangers.
DR PRO; PR:Q552S0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031256; C:leading edge membrane; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; ISS:dictyBase.
DR GO; GO:0070650; P:actin filament bundle distribution; IMP:dictyBase.
DR GO; GO:0030041; P:actin filament polymerization; IMP:dictyBase.
DR GO; GO:0097230; P:cell motility in response to potassium ion; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:dictyBase.
DR GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IMP:dictyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:dictyBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0036051; P:protein localization to trailing edge; IMP:dictyBase.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:dictyBase.
DR GO; GO:0061118; P:regulation of positive chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0051592; P:response to calcium ion; IMP:dictyBase.
DR GO; GO:0035864; P:response to potassium ion; IMP:dictyBase.
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 2: Evidence at transcript level;
KW Antiport; Ion transport; Membrane; Reference proteome; Signal; Sodium;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..674
FT /note="Sodium/hydrogen exchanger 1"
FT /id="PRO_0000386638"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 31..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 75521 MW; 86AC7C3E8C1F2452 CRC64;
MKLNKSYILI VVLLLSLFYS SVSSTKTTLI KSNNHYNSDN SNNDNKNINI NNNNDGDGDD
DDDNNKILIT PENQNHLIHD IGIDSSSTEI LFGSSSNSGS CGEKNNTKQN ALANQREANT
IIFIIMLILT GSVLIVYFII SLDIPFVPES VAVVTYGIIL GIVFRFFYSD IVNHVVSFEP
ENFFLFILPT IIFETGYSLH KTDFFNNIGP ILMFAVFGTI ITFLVVGFGI YIVGYFGVSI
ALSLKDSFAF GSIISSTDPV CTLAIFQALN VDPMLYILVL GESILNDATS MMLYSVVEDT
STRDIIISCA MFTVVAIGSV ILGVVMALLL SLILKWINIG KFPALETIFM VMFSYMSYVL
AGALDISGVL AVFFFGITLN QYGAYSLSPY TKLTSGQLFR TAAFISETFL FLYFGLSLTA
HEFKFDLGLF SWSILFTCLA RAISVFPMCF LLNKFLKTKI PWVIQVAIWF AGLRGAFAFS
LSLDYISEDE HMNAYIRTNT LLVVVFTIFV FGMGTYPLLR VLGIKTSQTD QSLDNISKPM
SKQTKQKDRT KLYESFDDKY FKPWFRKRVP PLANEAIEIF EKMVIQSSHD HELDSNPLRF
DDDEEDDDDE DLDFDSDLDL NININTDSIH QSDNNNNDNG NNNNNNNNII INNNSQHHSN
DGSNNKNNDT LPLI
