SL9A7_MOUSE
ID SL9A7_MOUSE Reviewed; 726 AA.
AC Q8BLV3; A2ACD5; A2ACD6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sodium/hydrogen exchanger 7;
DE AltName: Full=Na(+)/H(+) exchanger 7;
DE Short=NHE-7;
DE AltName: Full=Solute carrier family 9 member 7;
GN Name=Slc9a7; Synonyms=Nhe7;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Spleen;
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: Mediates electroneutral exchange of protons for Na(+) and
CC K(+) across endomembranes. May contribute to the regulation of Golgi
CC apparatus volume and pH. {ECO:0000250|UniProtKB:Q96T83}.
CC -!- SUBUNIT: Interacts with SCAMP1, SCAMP2 and SCAMP5; may participate in
CC its shuttling from trans-Golgi network to recycling endosomes.
CC {ECO:0000250|UniProtKB:Q96T83}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q96T83}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96T83}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q96T83}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96T83}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96T83}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96T83}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BLV3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLV3-2; Sequence=VSP_009498, VSP_009499;
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96T83}.
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; AK041169; BAC30848.1; -; mRNA.
DR EMBL; AL663098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058750; AAH58750.1; -; mRNA.
DR CCDS; CCDS40884.1; -. [Q8BLV3-1]
DR RefSeq; NP_796327.1; NM_177353.3. [Q8BLV3-1]
DR RefSeq; XP_006527679.1; XM_006527616.3. [Q8BLV3-1]
DR AlphaFoldDB; Q8BLV3; -.
DR SMR; Q8BLV3; -.
DR BioGRID; 231784; 4.
DR STRING; 10090.ENSMUSP00000072274; -.
DR GlyGen; Q8BLV3; 1 site.
DR iPTMnet; Q8BLV3; -.
DR PhosphoSitePlus; Q8BLV3; -.
DR MaxQB; Q8BLV3; -.
DR PaxDb; Q8BLV3; -.
DR PeptideAtlas; Q8BLV3; -.
DR PRIDE; Q8BLV3; -.
DR ProteomicsDB; 257253; -. [Q8BLV3-1]
DR ProteomicsDB; 257254; -. [Q8BLV3-2]
DR Antibodypedia; 25223; 122 antibodies from 24 providers.
DR DNASU; 236727; -.
DR Ensembl; ENSMUST00000072451; ENSMUSP00000072274; ENSMUSG00000037341. [Q8BLV3-1]
DR Ensembl; ENSMUST00000115393; ENSMUSP00000111051; ENSMUSG00000037341. [Q8BLV3-2]
DR GeneID; 236727; -.
DR KEGG; mmu:236727; -.
DR UCSC; uc009sst.1; mouse. [Q8BLV3-1]
DR UCSC; uc033jor.1; mouse. [Q8BLV3-2]
DR CTD; 84679; -.
DR MGI; MGI:2444530; Slc9a7.
DR VEuPathDB; HostDB:ENSMUSG00000037341; -.
DR eggNOG; KOG1965; Eukaryota.
DR GeneTree; ENSGT00940000153460; -.
DR HOGENOM; CLU_005912_7_0_1; -.
DR InParanoid; Q8BLV3; -.
DR OMA; NEHCWQY; -.
DR OrthoDB; 559433at2759; -.
DR PhylomeDB; Q8BLV3; -.
DR TreeFam; TF318755; -.
DR Reactome; R-MMU-425986; Sodium/Proton exchangers.
DR BioGRID-ORCS; 236727; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Slc9a7; mouse.
DR PRO; PR:Q8BLV3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BLV3; protein.
DR Bgee; ENSMUSG00000037341; Expressed in retinal neural layer and 57 other tissues.
DR ExpressionAtlas; Q8BLV3; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0015386; F:potassium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0015385; F:sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1905526; P:regulation of Golgi lumen acidification; ISS:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; ISS:UniProtKB.
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 InterPro; IPR002090; NHE-6/7/9.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR PRINTS; PR01088; NAHEXCHNGR6.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Cell membrane; Endosome; Glycoprotein;
KW Golgi apparatus; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..726
FT /note="Sodium/hydrogen exchanger 7"
FT /id="PRO_0000052364"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..70
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..175
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..251
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..323
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..443
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 483..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..514
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96T83"
FT REGION 675..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 540..548
FT /note="VGVEELSEE -> YRFWNMIDR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009498"
FT VAR_SEQ 549..726
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009499"
FT CONFLICT 46
FT /note="A -> E (in Ref. 3; AAH58750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 80289 MW; 852266CCEC363B9C CRC64;
MEPSDAARPG PGRAFRGLSP RLLLLPLLPV LLGRGLRAGA AASSGAAAED SSAMEELATE
KEAEESHRQD SVSLLTFILL LTLTILTIWL FKHRRVRFLH ETGLAMIYGL IVGVILRYGT
PATSGHDKSL SCTQEDRAFS TLLVNVSGKF FEYTLKGEIS PGKINNVEQN DMLRKVTFDP
EVFFNILLPP IIFHAGYSLK KRHFFRNLGS ILAYAFLGTA VSCFIIGNLM YGVVKLMKIV
GQLSDKFYYT DCLFFGAIIS ATDPVTVLAI FNELHADVDL YALLFGESVL NDAVAIVLSS
SIVAYQPAGL NTHAFDAAAF FKSVGIFLGI FSGSFTMGAV TGVVTALVTK FTKLHCFPLL
ETALFFLMSW STFLLAEACG FTGVVAVLFC GITQAHYTYN NLSVESRSRS KQLFEVLHFL
AENFIFSYMG LALFTFQKHV FSPIFIIGAF VAIFLGRAAH IYPLSFFLNL GRRHKIGWNF
QHMMMFSGLR GAMAFALAIR DTASYARQMM FTTTLLIVFF TVWVIGGGTT PMLSWLNIRV
GVEELSEEDQ NENRWQYFRV GVDPDQDPPP NNDSFQVLQG DGMDSVGGSR TKQESAWIFR
LWYIFDHNYL KPILTHSGPP LTTTLPAWCG LLARCLTSPQ VYDNQEPLRE DDSDFILTEG
DLTLTYGDST VTANGSSSSY TASTSLECGR RTKSSSEEVL ERDLGMGDQK VSSRGTPLVF
PLQENA
