SL9A3_MOUSE
ID SL9A3_MOUSE Reviewed; 829 AA.
AC G3X939; Q8BZU0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Sodium/hydrogen exchanger 3 {ECO:0000305};
GN Name=Slc9a3 {ECO:0000312|MGI:MGI:105064};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-805 AND SER-808, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBUNIT: Binds SLC9A3R1 and SLC9A3R2. Interacts with CHP1, CHP2 and
CC SHANK2. Interacts with PDZK1 (via C-terminal PDZ domain) (By
CC similarity). Interacts with PDZD3 and interactions decrease in response
CC to elevated calcium ion levels. Interacts with AHCYL1; the interaction
CC is required for SLC9A3 activity (By similarity).
CC {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P26433,
CC ECO:0000250|UniProtKB:P48764, ECO:0000250|UniProtKB:Q28362}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P26433, ECO:0000250|UniProtKB:P48764}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P48764}. Note=In
CC intestinal epithelial cells, localizes to the ileal brush border.
CC Phosphorylation at Ser-663 by SGK1 is associated with increased
CC abundance at the cell membrane. Angiotensin-2 enhances apical
CC expression (By similarity). {ECO:0000250|UniProtKB:P48764,
CC ECO:0000250|UniProtKB:Q28362}.
CC -!- PTM: Phosphorylated by PKA, which inhibits activity. Phosphorylation at
CC Ser-659 by SGK1 is associated with increased abundance at the cell
CC membrane. {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P26433}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
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; AK033564; BAC28362.1; -; mRNA.
DR EMBL; AC154839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466563; EDL37085.1; -; Genomic_DNA.
DR CCDS; CCDS36731.1; -.
DR RefSeq; NP_001074529.1; NM_001081060.1.
DR RefSeq; XP_006517085.1; XM_006517022.3.
DR AlphaFoldDB; G3X939; -.
DR SMR; G3X939; -.
DR STRING; 10090.ENSMUSP00000038142; -.
DR GlyGen; G3X939; 1 site.
DR iPTMnet; G3X939; -.
DR PhosphoSitePlus; G3X939; -.
DR jPOST; G3X939; -.
DR MaxQB; G3X939; -.
DR PaxDb; G3X939; -.
DR PeptideAtlas; G3X939; -.
DR PRIDE; G3X939; -.
DR ProteomicsDB; 257252; -.
DR Antibodypedia; 22241; 324 antibodies from 26 providers.
DR DNASU; 105243; -.
DR Ensembl; ENSMUST00000036208; ENSMUSP00000038142; ENSMUSG00000036123.
DR Ensembl; ENSMUST00000221703; ENSMUSP00000152682; ENSMUSG00000036123.
DR GeneID; 105243; -.
DR KEGG; mmu:105243; -.
DR UCSC; uc007res.2; mouse.
DR UCSC; uc007ret.1; mouse.
DR CTD; 6550; -.
DR MGI; MGI:105064; Slc9a3.
DR VEuPathDB; HostDB:ENSMUSG00000036123; -.
DR eggNOG; KOG1966; Eukaryota.
DR GeneTree; ENSGT00940000158616; -.
DR HOGENOM; CLU_005912_4_2_1; -.
DR InParanoid; G3X939; -.
DR OMA; ECVKGIV; -.
DR OrthoDB; 389547at2759; -.
DR PhylomeDB; G3X939; -.
DR TreeFam; TF317212; -.
DR Reactome; R-MMU-425986; Sodium/Proton exchangers.
DR BioGRID-ORCS; 105243; 1 hit in 72 CRISPR screens.
DR PRO; PR:G3X939; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; G3X939; protein.
DR Bgee; ENSMUSG00000036123; Expressed in small intestine Peyer's patch and 83 other tissues.
DR ExpressionAtlas; G3X939; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; IDA:MGI.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
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 InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR PRINTS; PR01087; NAHEXCHNGR3.
DR SUPFAM; SSF55136; SSF55136; 1.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..829
FT /note="Sodium/hydrogen exchanger 3"
FT /id="PRO_0000433355"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 12..23
FT /note="Name=A/M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 50..68
FT /note="Name=B/M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..94
FT /note="Helical; Name=C/M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..107
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..128
FT /note="Helical; Name=D/M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..155
FT /note="Helical; Name=E/M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..175
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..197
FT /note="Helical; Name=F/M5A"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..227
FT /note="Helical; Name=G/M5B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..247
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..269
FT /note="Helical; Name=H/M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 286..304
FT /note="Helical; Name=I/M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..335
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 336..357
FT /note="Helical; Name=J/M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..385
FT /note="Helical; Name=K/M9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..400
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 401..421
FT /note="Name=L"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..430
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..451
FT /note="Helical; Name=M/M10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 586..663
FT /note="Interaction with PDZD3"
FT /evidence="ECO:0000250"
FT REGION 677..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26433"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26433"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26433"
FT MOD_RES 659
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:P26432"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 829 AA; 93104 MW; E2458CAE3F11B357 CRC64;
MWHRALGPGW KLLLALALTS LQGARGAEEE PSSDGSFQVV TFKWHHVQDP YIIALWILVA
SLAKIVFHLS HKVTSIVPES ALLIVLGLVL GGIVWAADHI ASFTLTPTLF FFYLLPPIVL
DAGYFMPNRL FFGNLGTILL YAVIGTIWNA ATTGLSLYGV FLSGLMGELK IGLLDFLLFG
SLIAAVDPVA VLAVFEEVHV NEVLFIIVFG ESLLNDAVTV VLYNVFESFV TLGGDAVTGV
DCVKGIVSFF VVSLGGTLVG VIFAFLLSLV TRFTKHVRII EPGFVFVISY LSYLTSEMLS
LSSILAITFC GICCQKYVKA NISEQSATTV RYTMKMLASG AETIIFMFLG ISAVNPDIWT
WNTAFVLLTL VFISVYRAIG VVLQTWILNR YRMVQLETID QVVMSYGGLR GAVAYALVVL
LDEKKVKEKN LFVSTTLIVV FFTVIFQGLT IKPLVQWLKV KRSEHREPKL NEKLHGRAFD
HILSAIEDIS GQIGHNYLRD KWSNFDRKFL SKVLMRRSAQ KSRDRILNVF HELNLKDAIS
YVAEGERRGS LAFIRSPSTD NMVNVDFNTP RPSTVEASVS YFLRENVSAV CLDMQSLEQR
RRSIRDTEDM VTHHTLQQYL YKPRQEYKHL YSRHELTPNE DEKQDKEIFH RTMRKRLESF
KSAKLGINQN KKAAKLYKRE RAQKRRNSSI PNGKLPMENL AHNYTIKEKD LELSEHEEAT
NYEEISGGIE FLASVTQDVA SDSGAGIDNP VFSPDEDLDP SILSRVPPWL SPGETVVPSQ
RARVQIPNSP SNFRRLTPFR LSNKSVDSFL QADGHEEQLQ PAAPESTHM
