Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sodium/hydrogen exchanger 7

Gene

SLC9A7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates electroneutral exchange of protons for Na+ and K+ across endomembranes. May contribute to Golgi volume and cation homeostasis.1 Publication

GO - Molecular functioni

  • potassium:proton antiporter activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • sodium:proton antiporter activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Potassium transport, Sodium transport, Transport

Keywords - Ligandi

Potassium, Sodium

Enzyme and pathway databases

ReactomeiR-HSA-425986. Sodium/Proton exchangers.

Protein family/group databases

TCDBi2.A.36.1.3. the monovalent cation:proton antiporter-1 (cpa1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/hydrogen exchanger 7
Alternative name(s):
Na(+)/H(+) exchanger 7
Short name:
NHE-7
Solute carrier family 9 member 7
Gene namesi
Name:SLC9A7
Synonyms:NHE7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17123. SLC9A7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei71 – 9121HelicalSequence analysisAdd
BLAST
Transmembranei96 – 11621HelicalSequence analysisAdd
BLAST
Transmembranei176 – 19621HelicalSequence analysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence analysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence analysisAdd
BLAST
Transmembranei278 – 29821HelicalSequence analysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence analysisAdd
BLAST
Transmembranei350 – 37021HelicalSequence analysisAdd
BLAST
Transmembranei372 – 39221HelicalSequence analysisAdd
BLAST
Transmembranei415 – 43521HelicalSequence analysisAdd
BLAST
Transmembranei443 – 46321HelicalSequence analysisAdd
BLAST
Transmembranei514 – 53421HelicalSequence analysisAdd
BLAST
Transmembranei612 – 63221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: GO_Central
  • recycling endosome membrane Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38200.

Polymorphism and mutation databases

BioMutaiSLC9A7.
DMDMi44888236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Sodium/hydrogen exchanger 7PRO_0000052363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei545 – 5451PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96T83.
MaxQBiQ96T83.
PaxDbiQ96T83.
PeptideAtlasiQ96T83.
PRIDEiQ96T83.
TopDownProteomicsiQ96T83.

PTM databases

iPTMnetiQ96T83.
PhosphoSiteiQ96T83.
SwissPalmiQ96T83.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ96T83.
CleanExiHS_SLC9A7.
ExpressionAtlasiQ96T83. baseline and differential.
GenevisibleiQ96T83. HS.

Organism-specific databases

HPAiHPA048938.

Interactioni

Subunit structurei

Interacts with SCAMP1, SCAMP2 and SCAMP5; may participate in its shuttling from trans-Golgi network to recycling endosomes.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi124198. 1 interaction.
IntActiQ96T83. 1 interaction.
STRINGi9606.ENSP00000330320.

Structurei

3D structure databases

ProteinModelPortaliQ96T83.
SMRiQ96T83. Positions 191-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1965. Eukaryota.
COG0025. LUCA.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000172307.
HOVERGENiHBG055575.
InParanoidiQ96T83.
KOiK12041.
OrthoDBiEOG7NW69D.
PhylomeDBiQ96T83.
TreeFamiTF318755.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR002090. Na/H_exchanger_6.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 2 hits.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01088. NAHEXCHNGR6.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96T83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPGDAARPG SGRATGAPPP RLLLLPLLLG WGLRVAAAAS ASSSGAAAED
60 70 80 90 100
SSAMEELATE KEAEESHRQD SVSLLTFILL LTLTILTIWL FKHRRVRFLH
110 120 130 140 150
ETGLAMIYGL IVGVILRYGT PATSGRDKSL SCTQEDRAFS TLLVNVSGKF
160 170 180 190 200
FEYTLKGEIS PGKINSVEQN DMLRKVTFDP EVFFNILLPP IIFHAGYSLK
210 220 230 240 250
KRHFFRNLGS ILAYAFLGTA VSCFIIGNLM YGVVKLMKIM GQLSDKFYYT
260 270 280 290 300
DCLFFGAIIS ATDPVTVLAI FNELHADVDL YALLFGESVL NDAVAIVLSS
310 320 330 340 350
SIVAYQPAGL NTHAFDAAAF FKSVGIFLGI FSGSFTMGAV TGVNANVTKF
360 370 380 390 400
TKLHCFPLLE TALFFLMSWS TFLLAEACGF TGVVAVLFCG ITQAHYTYNN
410 420 430 440 450
LSVESRSRTK QLFEVLHFLA ENFIFSYMGL ALFTFQKHVF SPIFIIGAFV
460 470 480 490 500
AIFLGRAAHI YPLSFFLNLG RRHKIGWNFQ HMMMFSGLRG AMAFALAIRD
510 520 530 540 550
TASYARQMMF TTTLLIVFFT VWIIGGGTTP MLSWLNIRVG VEEPSEEDQN
560 570 580 590 600
EHHWQYFRVG VDPDQDPPPN NDSFQVLQGD GPDSARGNRT KQESAWIFRL
610 620 630 640 650
WYSFDHNYLK PILTHSGPPL TTTLPAWCGL LARCLTSPQV YDNQEPLREE
660 670 680 690 700
DSDFILTEGD LTLTYGDSTV TANGSSSSHT ASTSLEGSRR TKSSSEEVLE
710 720
RDLGMGDQKV SSRGTRLVFP LEDNA
Length:725
Mass (Da):80,131
Last modified:December 1, 2001 - v1
Checksum:i14E50B197863E38F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298591 mRNA. Translation: AAK54508.1.
AL050307, AL022165 Genomic DNA. Translation: CAI43015.1.
AL022165, AL050307 Genomic DNA. Translation: CAI43029.1.
CCDSiCCDS14269.1.
RefSeqiNP_115980.1. NM_032591.2.
UniGeneiHs.91389.

Genome annotation databases

EnsembliENST00000328306; ENSP00000330320; ENSG00000065923.
GeneIDi84679.
KEGGihsa:84679.
UCSCiuc004dgu.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298591 mRNA. Translation: AAK54508.1.
AL050307, AL022165 Genomic DNA. Translation: CAI43015.1.
AL022165, AL050307 Genomic DNA. Translation: CAI43029.1.
CCDSiCCDS14269.1.
RefSeqiNP_115980.1. NM_032591.2.
UniGeneiHs.91389.

3D structure databases

ProteinModelPortaliQ96T83.
SMRiQ96T83. Positions 191-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124198. 1 interaction.
IntActiQ96T83. 1 interaction.
STRINGi9606.ENSP00000330320.

Protein family/group databases

TCDBi2.A.36.1.3. the monovalent cation:proton antiporter-1 (cpa1) family.

PTM databases

iPTMnetiQ96T83.
PhosphoSiteiQ96T83.
SwissPalmiQ96T83.

Polymorphism and mutation databases

BioMutaiSLC9A7.
DMDMi44888236.

Proteomic databases

EPDiQ96T83.
MaxQBiQ96T83.
PaxDbiQ96T83.
PeptideAtlasiQ96T83.
PRIDEiQ96T83.
TopDownProteomicsiQ96T83.

Protocols and materials databases

DNASUi84679.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328306; ENSP00000330320; ENSG00000065923.
GeneIDi84679.
KEGGihsa:84679.
UCSCiuc004dgu.3. human.

Organism-specific databases

CTDi84679.
GeneCardsiSLC9A7.
HGNCiHGNC:17123. SLC9A7.
HPAiHPA048938.
MIMi300368. gene.
neXtProtiNX_Q96T83.
PharmGKBiPA38200.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1965. Eukaryota.
COG0025. LUCA.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000172307.
HOVERGENiHBG055575.
InParanoidiQ96T83.
KOiK12041.
OrthoDBiEOG7NW69D.
PhylomeDBiQ96T83.
TreeFamiTF318755.

Enzyme and pathway databases

ReactomeiR-HSA-425986. Sodium/Proton exchangers.

Miscellaneous databases

GenomeRNAii84679.
PROiQ96T83.
SOURCEiSearch...

Gene expression databases

BgeeiQ96T83.
CleanExiHS_SLC9A7.
ExpressionAtlasiQ96T83. baseline and differential.
GenevisibleiQ96T83. HS.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR002090. Na/H_exchanger_6.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 2 hits.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01088. NAHEXCHNGR6.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel (Na+,K+)/H+ exchanger localized to the trans-Golgi network."
    Numata M., Orlowski J.
    J. Biol. Chem. 276:17387-17394(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Secretory carrier membrane proteins interact and regulate trafficking of the organellar (Na+,K+)/H+ exchanger NHE7."
    Lin P.J., Williams W.P., Luu Y., Molday R.S., Orlowski J., Numata M.
    J. Cell Sci. 118:1885-1897(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SCAMP1; SCAMP2 AND SCAMP5.

Entry informationi

Entry nameiSL9A7_HUMAN
AccessioniPrimary (citable) accession number: Q96T83
Secondary accession number(s): O75827, Q5JXP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Is not inhibited by amiloride but by benzamil and quinine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.