SL9A3_TRISC
ID SL9A3_TRISC Reviewed; 832 AA.
AC M5A7P9; M5A8K9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Sodium/hydrogen exchanger 3 {ECO:0000303|PubMed:23485868};
DE AltName: Full=Na(+)/H(+) exchanger 3 {ECO:0000303|PubMed:23485868};
DE Short=NHE-3 {ECO:0000303|PubMed:23485868};
DE AltName: Full=Solute carrier family 9 member 3 {ECO:0000250|UniProtKB:P48764};
GN Name=slc9a3 {ECO:0000312|EMBL:BAN04722.1};
GN Synonyms=nhe3 {ECO:0000303|PubMed:23485868};
OS Triakis scyllium (Banded houndshark) (Hemigaleus pingi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC Triakis.
OX NCBI_TaxID=30494;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAN04722.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Gill {ECO:0000312|EMBL:BAN04722.1}, and
RC Kidney {ECO:0000312|EMBL:BAN04721.1};
RX PubMed=23485868; DOI=10.1152/ajpregu.00417.2012;
RA Li S., Kato A., Takabe S., Chen A.-P., Romero M.F., Umezawa T., Nakada T.,
RA Hyodo S., Hirose S.;
RT "Expression of a novel isoform of Na+/H+ exchanger 3 (NHE3) in the kidney
RT and intestine of banded houndshark Triakis scyllium.";
RL Am. J. Physiol. 304:R865-R876(2013).
CC -!- FUNCTION: Involved in pH regulation to eliminate acids generated by
CC active metabolism or to counter adverse environmental conditions. Major
CC proton extruding system driven by the inward sodium ion chemical
CC gradient. Plays an important role in signal transduction.
CC {ECO:0000250|UniProtKB:P48764}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:23485868}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23485868}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:23485868}; Synonyms=g
CC {ECO:0000303|PubMed:23485868};
CC IsoId=M5A7P9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:23485868}; Synonyms=k/i
CC {ECO:0000303|PubMed:23485868};
CC IsoId=M5A7P9-2; Sequence=VSP_047941;
CC -!- TISSUE SPECIFICITY: Detected in early distal renal tubules in the
CC kidney bundle zone, in proximal and late distal tubules in the kidney
CC sinus zone, in absorptive epithelial cells of the intestine and in
CC rectal epithelium (at protein level). Isoform 1 is expressed strongly
CC in the gills, at intermediate levels in the kidney, spleen, rectum,
CC spiral intestine and skin, and weakly in the brain, blood and rectal
CC gland. Isoform 2 is expressed strongly in the kidney, rectum and spiral
CC intestine, and weakly in muscles and the rectal gland.
CC {ECO:0000269|PubMed:23485868}.
CC -!- INDUCTION: High salinity induces expression of isoform 2 in the kidney;
CC conversely, low salinity induces expression in the intestine.
CC {ECO:0000269|PubMed:23485868}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000255}.
CC -!- CAUTION: The number, localization and denomination of hydrophobic
CC domains in the Na(+)/H(+) exchangers vary among authors. {ECO:0000305}.
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DR EMBL; AB632345; BAN04721.1; -; mRNA.
DR EMBL; AB632346; BAN04722.1; -; mRNA.
DR AlphaFoldDB; M5A7P9; -.
DR SMR; M5A7P9; -.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015385; F:sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISS:UniProtKB.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR018410; Na/H_exchanger_3/5.
DR InterPro; IPR004709; NaH_exchanger.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR PRINTS; PR01087; NAHEXCHNGR3.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Antiport; Cell membrane; Ion transport;
KW Membrane; Phosphoprotein; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..832
FT /note="Sodium/hydrogen exchanger 3"
FT /id="PRO_0000423519"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 7..27
FT /note="Name=A/M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 69..89
FT /note="Name=B/M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=C/M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=D/M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=E/M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=F/M5A"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=G/M5B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=H/M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=I/M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=J/M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical; Name=K/M9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 421..441
FT /note="Name=L"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..450
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical; Name=M/M10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..832
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..83
FT /note="MGRNRSGCVARCVSLTALVLLLCCPVVRSSEAETDPDSHTEHGDSHGGSREG
FT NDTGFQIVTFRWEHVQTPYVIALWILVASLG -> MGKERSQCAGSRCLWSLALLAAGC
FT SAAGTFSRSEPSAESQSSPQNSSNPGYQIVYFDWEYVEKPYVVAGWILVAGLA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:23485868"
FT /id="VSP_047941"
SQ SEQUENCE 832 AA; 92913 MW; 6ACB728455A4759C CRC64;
MGRNRSGCVA RCVSLTALVL LLCCPVVRSS EAETDPDSHT EHGDSHGGSR EGNDTGFQIV
TFRWEHVQTP YVIALWILVA SLGKIVFHLS EKVTSVVPES ALLIVLGLIL GGIVWAADHS
ASFTLTPTVF FFYLLPPIVL DAGYFMPNRH FFGNLGTILT YAVIGTVWNA ATTGLSLYGV
FLLGLMGDLK AGLLEFLLFG SLIAAVDPVA VLAVFEEVHV NEVLFIIVFG ESLLNDAVTV
VLYNVFNSFV EVGAGNVQGL DYFKGIVSFF VVSLGGTAVG IIFAFILSLV TRFTKHVRVI
EPGFVFVISY LSYLTADMLS LSAILAITFC GICCQKYVKA NLCEQSITTV RYAMKMLASG
AETIIFMFLG ISAVNPTIWT WNTAFILLTL VFISVYRVIG VVIQTWILNH YRVVQLEIID
QVVMSYGGLR GAVAFALVVL LDSNYVGERR LFVSTTIIVV YFTVIFQGLT IKPLVKWLKV
KRSQHKEPLL NEKLHGRAFD HILSAIEDIS GQIGHNYLRD KWTNFDRKYL SKIMMRKSAQ
ISRDKILSVF RELNLKDAIS YVSEGERKGS LAFIRSSSDV NVDFTGPRHS VVDSSVSAVL
RESTSEVCLD MHAVENRAKS PKDREEIVTH HMLQQHLYKP RKRYRLNYSR HKLARSEGEK
QDKEIFQRTM KKRLENFKPT KLGTNYTTKF RNMKKERAAK KKHSDAVPNG RLATHSVSFH
VNKDSEVEDP ADGGISFLIT PASNDADETG TGIDNPSFSN EEDQSIYQMI PPWISNEETV
IPSQRARLQI PRSPTNFRRL TPLQLSNRSI DAFLLADISD EHPLSFLPES SM
