SL9A1_BOVIN
ID SL9A1_BOVIN Reviewed; 817 AA.
AC Q28036;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sodium/hydrogen exchanger 1;
DE AltName: Full=Na(+)/H(+) exchanger 1;
DE Short=NHE-1;
DE AltName: Full=Solute carrier family 9 member 1;
GN Name=SLC9A1; Synonyms=NHE1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Zhu H., Zhang Q., Zhang X., Liu W., Trumbly R.J., Garlid K.D., Sun X.;
RT "Molecular cloning and characterization of Na+/H+ antiporter from Bovine
RT heart.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Oligomer (By similarity). Interacts with CALM in a calcium-
CC dependent manner (By similarity). Interacts with TESC (By similarity).
CC Interacts (via the juxtamembrane region of the cytoplasmic C-terminal
CC domain) with CHP1; the interaction occurs at the plasma membrane in a
CC calcium-dependent manner (By similarity). Interacts with CHP2; the
CC interaction occurs in a calcium-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P19634, ECO:0000250|UniProtKB:P26431}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cell membrane; Multi-pass
CC membrane protein. Note=Colocalizes with CHP1 and CHP2 at the reticulum
CC endoplasmic and plasma membrane. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Ubiquitination is reduced by CHP1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
CC -!- CAUTION: The region between transmembrane regions M4 and M5 and between
CC M6 and M7 (also termed intracellular loops IL2 and IL4, respectively)
CC seem to be localized at least in part in the membrane. The hydrophobic
CC region H10 is proposed to be located within the membrane.
CC {ECO:0000305}.
CC -!- CAUTION: The interacting region with TESC is conflicting: In human, it
CC has been reported that SLC9A1 interacts with TESC via the juxtamembrane
CC region of the cytoplasmic C-terminal domain, including residues 503-
CC 545. However, another publication has reported interaction with TESC
CC via residues 633-817, the region of the cytoplasmic C-terminus more
CC distal to the membrane. {ECO:0000305}.
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DR EMBL; U49432; AAA91483.1; -; mRNA.
DR RefSeq; NP_777258.1; NM_174833.2.
DR AlphaFoldDB; Q28036; -.
DR BMRB; Q28036; -.
DR SMR; Q28036; -.
DR STRING; 9913.ENSBTAP00000048292; -.
DR PaxDb; Q28036; -.
DR PRIDE; Q28036; -.
DR GeneID; 317654; -.
DR KEGG; bta:317654; -.
DR CTD; 6548; -.
DR eggNOG; KOG1966; Eukaryota.
DR InParanoid; Q28036; -.
DR OrthoDB; 389547at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; ISS:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; ISS:UniProtKB.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; 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; IPR001970; NHE-1-like.
DR InterPro; IPR032103; NHE_CaM-bd.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR PANTHER; PTHR10110:SF59; PTHR10110:SF59; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF16644; NEXCaM_BD; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR PRINTS; PR01085; NAHEXCHNGR1.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 2: Evidence at transcript level;
KW Antiport; Calmodulin-binding; Cell membrane; Endoplasmic reticulum;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..817
FT /note="Sodium/hydrogen exchanger 1"
FT /id="PRO_0000052345"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..127
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..174
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..211
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..247
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..276
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical; Name=M9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 382..402
FT /note="Name=H10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 403..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..430
FT /note="Helical; Name=M10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..470
FT /note="Helical; Name=M11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..499
FT /note="Helical; Name=M12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 44..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..545
FT /note="Interaction with TESC"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT REGION 515..545
FT /note="Interaction with CHP2"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT REGION 633..817
FT /note="Interaction with CALM1"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT REGION 633..817
FT /note="Interaction with TESC"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT REGION 744..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 161
FT /note="Channel pore-lining"
FT /evidence="ECO:0000250"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61165"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61165"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26431"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 817 AA; 91017 MW; 6617E99D3B012920 CRC64;
MLLWPGASGL PPPRIFPSLL VVVALVGLLP VLRSYGLQIS PTASTIRGSE PPRERSIGDV
TTAPPELAPE SRPVNHSFAE HSPKARKAFP VLGIDYQHVR IPFEIALWIL LACLMKIGFH
VIPTISSIVP ESCLLIVVGL LVGGLIKGVG ETPPILQSEV FFLFLLPPII LDAGYFLPLR
QFTENLGTIL IFAVVGTLWN AFFLGGLMYA VCLVGGEQIN NIGLLENLLF GSIISAVDPV
AVLAVFEEIH INELLHILVF GESLLNDAVT VVLYHLFEEF ANYDRVGIVD IILGFLSFFV
VSLGGVFVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL SGIMALIASG
VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV STVAGSHHWN WTFVISTLLF
CLIARVLGVL GLTWFINKFR IVKLTPKDQF IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF
LTAIITVIFF TVFVQGMTIR PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH
YGHHHWKDKL NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA
VSTVSMQNIH PKSLPAERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN RHTLVADPYE
EAWNQMLLRR QKARQLEQKI SNYLTVPAHK LDSPTMSRAR IGSDPLAYEP KADLPVITID
PASPQSPESV DLVNEELKGK VLGLSRDPGR LAEEEEDDNG PRWLTMRTKE PSSPGTDDVF
TPAPSDSPSS QRIQRCLSDP GPHPEPGEGE PFIPKGQ
