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Protein

Sodium/hydrogen exchanger 3

Gene

Slc9a3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.By similarity

GO - Molecular functioni

  • PDZ domain binding Source: UniProtKB
  • sodium:proton antiporter activity Source: MGI

GO - Biological processi

  • circadian rhythm Source: Ensembl
  • receptor-mediated endocytosis Source: Ensembl
  • regulation of pH Source: MGI
  • regulation of sodium ion transport Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • sodium ion transmembrane transport Source: GOC
  • sodium ion transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiREACT_324002. Sodium/Proton exchangers.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/hydrogen exchanger 3Curated
Gene namesi
Name:Slc9a3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:105064. Slc9a3.

Subcellular locationi

  • Apical cell membrane By similarity; Multi-pass membrane protein By similarity

  • Note: In intestinal epithelial cells, localizes to the ileal brush border. Phosphorylation at Ser-663 by SGK1 is associated with increased abundance at the cell membrane. Angiotensin-2 enhances apical expression (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicCuratedAdd
BLAST
Intramembranei12 – 2312Name=A/M1Sequence AnalysisAdd
BLAST
Topological domaini24 – 4926CytoplasmicCuratedAdd
BLAST
Intramembranei50 – 6819Name=B/M2Sequence AnalysisAdd
BLAST
Topological domaini69 – 746CytoplasmicCurated
Transmembranei75 – 9420Helical; Name=C/M3Sequence AnalysisAdd
BLAST
Topological domaini95 – 10713ExtracellularCuratedAdd
BLAST
Transmembranei108 – 12821Helical; Name=D/M4Sequence AnalysisAdd
BLAST
Topological domaini129 – 1346CytoplasmicCurated
Transmembranei135 – 15521Helical; Name=E/M5Sequence AnalysisAdd
BLAST
Topological domaini156 – 17520ExtracellularCuratedAdd
BLAST
Transmembranei176 – 19722Helical; Name=F/M5ASequence AnalysisAdd
BLAST
Topological domaini198 – 2058CytoplasmicCurated
Transmembranei206 – 22722Helical; Name=G/M5BSequence AnalysisAdd
BLAST
Topological domaini228 – 24720ExtracellularCuratedAdd
BLAST
Transmembranei248 – 26922Helical; Name=H/M6Sequence AnalysisAdd
BLAST
Topological domaini270 – 28516CytoplasmicCuratedAdd
BLAST
Transmembranei286 – 30419Helical; Name=I/M7Sequence AnalysisAdd
BLAST
Topological domaini305 – 33531ExtracellularCuratedAdd
BLAST
Transmembranei336 – 35722Helical; Name=J/M8Sequence AnalysisAdd
BLAST
Topological domaini358 – 3647CytoplasmicCurated
Transmembranei365 – 38521Helical; Name=K/M9Sequence AnalysisAdd
BLAST
Topological domaini386 – 40015ExtracellularCuratedAdd
BLAST
Intramembranei401 – 42121Name=LSequence AnalysisAdd
BLAST
Topological domaini422 – 4309ExtracellularCurated
Transmembranei431 – 45121Helical; Name=M/M10Sequence AnalysisAdd
BLAST
Topological domaini452 – 829378CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • brush border membrane Source: UniProtKB
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane-bounded vesicle Source: MGI
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 829829Sodium/hydrogen exchanger 3PRO_0000433355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Modified residuei550 – 5501PhosphoserineBy similarity
Modified residuei603 – 6031PhosphoserineBy similarity
Modified residuei659 – 6591Phosphoserine; by SGK1By similarity

Post-translational modificationi

Phosphorylated by PKA, which inhibits activity. Phosphorylation at Ser-659 by SGK1 is associated with increased abundance at the cell membrane.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiG3X939.
PaxDbiQ8BZU0.

Expressioni

Gene expression databases

BgeeiQ8BZU0.
GenevisibleiG3X939. MM.

Interactioni

Subunit structurei

Binds SLC9A3R1 and SLC9A3R2. Interacts with CHP1, CHP2 and SHANK2. Interacts with PDZK1 (via C-terminal PDZ domain) (By similarity). Interacts with PDZD3 and interactions decrease in response to elevated calcium ion levels. Interacts with AHCYL1; the interaction is required for SLC9A3 activity (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000038142.

Structurei

3D structure databases

ProteinModelPortaliG3X939.
SMRiG3X939. Positions 175-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni586 – 66378Interaction with PDZD3By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0025.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000247044.
KOiK12040.
OMAiYTMKMLA.
OrthoDBiEOG7KQ20Z.
TreeFamiTF317212.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR018410. Na/H_exchanger_3/5.
IPR004709. NaH_exchanger.
IPR011256. Reg_factor_effector_dom.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01087. NAHEXCHNGR3.
SUPFAMiSSF55136. SSF55136. 1 hit.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.

Sequencei

Sequence statusi: Complete.

G3X939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWHRALGPGW KLLLALALTS LQGARGAEEE PSSDGSFQVV TFKWHHVQDP
60 70 80 90 100
YIIALWILVA SLAKIVFHLS HKVTSIVPES ALLIVLGLVL GGIVWAADHI
110 120 130 140 150
ASFTLTPTLF FFYLLPPIVL DAGYFMPNRL FFGNLGTILL YAVIGTIWNA
160 170 180 190 200
ATTGLSLYGV FLSGLMGELK IGLLDFLLFG SLIAAVDPVA VLAVFEEVHV
210 220 230 240 250
NEVLFIIVFG ESLLNDAVTV VLYNVFESFV TLGGDAVTGV DCVKGIVSFF
260 270 280 290 300
VVSLGGTLVG VIFAFLLSLV TRFTKHVRII EPGFVFVISY LSYLTSEMLS
310 320 330 340 350
LSSILAITFC GICCQKYVKA NISEQSATTV RYTMKMLASG AETIIFMFLG
360 370 380 390 400
ISAVNPDIWT WNTAFVLLTL VFISVYRAIG VVLQTWILNR YRMVQLETID
410 420 430 440 450
QVVMSYGGLR GAVAYALVVL LDEKKVKEKN LFVSTTLIVV FFTVIFQGLT
460 470 480 490 500
IKPLVQWLKV KRSEHREPKL NEKLHGRAFD HILSAIEDIS GQIGHNYLRD
510 520 530 540 550
KWSNFDRKFL SKVLMRRSAQ KSRDRILNVF HELNLKDAIS YVAEGERRGS
560 570 580 590 600
LAFIRSPSTD NMVNVDFNTP RPSTVEASVS YFLRENVSAV CLDMQSLEQR
610 620 630 640 650
RRSIRDTEDM VTHHTLQQYL YKPRQEYKHL YSRHELTPNE DEKQDKEIFH
660 670 680 690 700
RTMRKRLESF KSAKLGINQN KKAAKLYKRE RAQKRRNSSI PNGKLPMENL
710 720 730 740 750
AHNYTIKEKD LELSEHEEAT NYEEISGGIE FLASVTQDVA SDSGAGIDNP
760 770 780 790 800
VFSPDEDLDP SILSRVPPWL SPGETVVPSQ RARVQIPNSP SNFRRLTPFR
810 820
LSNKSVDSFL QADGHEEQLQ PAAPESTHM
Length:829
Mass (Da):93,104
Last modified:November 16, 2011 - v1
Checksum:iE2458CAE3F11B357
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033564 mRNA. Translation: BAC28362.1.
AC154839 Genomic DNA. No translation available.
CH466563 Genomic DNA. Translation: EDL37085.1.
RefSeqiNP_001074529.1. NM_001081060.1.
XP_006517085.1. XM_006517022.2.
UniGeneiMm.261564.

Genome annotation databases

EnsembliENSMUST00000036208; ENSMUSP00000038142; ENSMUSG00000036123.
GeneIDi105243.
KEGGimmu:105243.
UCSCiuc007res.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033564 mRNA. Translation: BAC28362.1.
AC154839 Genomic DNA. No translation available.
CH466563 Genomic DNA. Translation: EDL37085.1.
RefSeqiNP_001074529.1. NM_001081060.1.
XP_006517085.1. XM_006517022.2.
UniGeneiMm.261564.

3D structure databases

ProteinModelPortaliG3X939.
SMRiG3X939. Positions 175-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000038142.

Proteomic databases

MaxQBiG3X939.
PaxDbiQ8BZU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036208; ENSMUSP00000038142; ENSMUSG00000036123.
GeneIDi105243.
KEGGimmu:105243.
UCSCiuc007res.2. mouse.

Organism-specific databases

CTDi6550.
MGIiMGI:105064. Slc9a3.

Phylogenomic databases

eggNOGiCOG0025.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000247044.
KOiK12040.
OMAiYTMKMLA.
OrthoDBiEOG7KQ20Z.
TreeFamiTF317212.

Enzyme and pathway databases

ReactomeiREACT_324002. Sodium/Proton exchangers.

Miscellaneous databases

NextBioi357548.
PROiG3X939.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BZU0.
GenevisibleiG3X939. MM.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR018410. Na/H_exchanger_3/5.
IPR004709. NaH_exchanger.
IPR011256. Reg_factor_effector_dom.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01087. NAHEXCHNGR3.
SUPFAMiSSF55136. SSF55136. 1 hit.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiSL9A3_MOUSE
AccessioniPrimary (citable) accession number: G3X939
Secondary accession number(s): Q8BZU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 24, 2015
Last sequence update: November 16, 2011
Last modified: July 22, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The number, localization and denomination of hydrophobic domains in the Na+/H+ exchangers vary among authors.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.