SL9A1_PIG
ID SL9A1_PIG Reviewed; 818 AA.
AC P48762;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1661081; DOI=10.1152/ajprenal.1991.261.6.f1088;
RA Reilly R.F., Hildebrandt F., Biemesderfer D., Sardet C., Pouyssegur J.,
RA Aronson P.S., Slayman C.W., Igarashi P.;
RT "cDNA cloning and immunolocalization of a Na(+)-H+ exchanger in LLC-PK1
RT renal epithelial cells.";
RL Am. J. Physiol. 261:F1088-F1094(1991).
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 633-818, the region of the cytoplasmic C-terminus more
CC distal to the membrane. {ECO:0000305}.
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DR EMBL; M89631; AAA31092.1; -; mRNA.
DR EMBL; S71135; AAB20633.1; -; mRNA.
DR PIR; A48858; A48858.
DR RefSeq; NP_001007104.1; NM_001007103.1.
DR AlphaFoldDB; P48762; -.
DR BMRB; P48762; -.
DR SMR; P48762; -.
DR STRING; 9823.ENSSSCP00000003872; -.
DR PaxDb; P48762; -.
DR PeptideAtlas; P48762; -.
DR GeneID; 397458; -.
DR KEGG; ssc:397458; -.
DR CTD; 6548; -.
DR eggNOG; KOG1966; Eukaryota.
DR InParanoid; P48762; -.
DR OrthoDB; 389547at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0015385; F:sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
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 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..818
FT /note="Sodium/hydrogen exchanger 1"
FT /id="PRO_0000052349"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..33
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..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..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 39..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..818
FT /note="Interaction with CALM1"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT REGION 633..818
FT /note="Interaction with TESC"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT REGION 739..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..797
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 752
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61165"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19634"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61165"
FT MOD_RES 799
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"
FT CONFLICT 683
FT /note="H -> Y (in Ref. 1; AAB20633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 90987 MW; 9329F7D9A51D3DC9 CRC64;
MLLWSGICGL SPPRIFPSLL VVVALVGLLP VLRSHGLQPS PTASTIRGSE PPRERSIGDV
TTAPPELAPE SRPVNHSVTE HGMKARKAFP VLGIDYTHVR TPFEISLWIL LACLMKIGFH
VIPTISSIVP ESCLLIVVGL LVGGLIKAVG ETPPFLQSEV FFLFLLPPII LDAGYFLPLR
QFTENLGTIL IFAVVGTLWN AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV
AVLAVFEEIH INELLHILVF GESLLNDAVT VVLYHLFEEF ANYDRVGIVD IVLGFLSFFV
VSLGGVFVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL SGIMALIASG
VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV STVAGSHHWN WTFVISTLLF
CLIARVLGVL GLTWFINKFR IVKLTPKDQF IIAYGGLRGA IAFSLGHLLD KNHFPMCDLF
LTAIITVIFF TVFVQGMTIR PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH
YGHHHWKDKL NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA
VSTVSMQNIH PKTLPTERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN RHTLVADPYE
EAWNQMLLRR QKARQLEQKI NNHLTVPAHK LDSPTMSRAR IGSDPLAYEP KADLPVITID
PASPQSPESV DLVNEELKGK VLGLSREPGR ATEEEDDDED HDGGLVMRTK EPSSPGTDDV
FTPAPSDSPS SQRIQRCLSD PGPHPEPGEG EPFIPKGQ
