SL9A2_RAT
ID SL9A2_RAT Reviewed; 813 AA.
AC P48763; Q16434;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sodium/hydrogen exchanger 2;
DE AltName: Full=H7;
DE AltName: Full=Na(+)/H(+) exchanger 2;
DE Short=NHE-2;
DE AltName: Full=Solute carrier family 9 member 2;
GN Name=Slc9a2; Synonyms=Nhe2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Stomach;
RX PubMed=7685026; DOI=10.1016/s0021-9258(19)50288-5;
RA Wang Z., Orlowski J., Shull G.E.;
RT "Primary structure and functional expression of a novel gastrointestinal
RT isoform of the rat Na/H exchanger.";
RL J. Biol. Chem. 268:11925-11928(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC STRAIN=Sprague-Dawley; TISSUE=Small intestine;
RX PubMed=7683411; DOI=10.1073/pnas.90.9.3938;
RA Collins J.F., Honda T., Knobel S., Bulus N.M., Conary J., Dubois R.,
RA Ghishan F.K.;
RT "Molecular cloning, sequencing, tissue distribution, and functional
RT expression of a Na+/H+ exchanger (NHE-2).";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3938-3942(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Liver;
RX PubMed=8595899; DOI=10.1006/geno.1995.0004;
RA Ghishan F.K., Knobel S.M., Summar M.;
RT "Molecular cloning, sequencing, chromosomal localization, and tissue
RT distribution of the human Na+/H+ exchanger (SLC9A2).";
RL Genomics 30:25-30(1995).
RN [4]
RP INTERACTION WITH CHP1 AND CHP2.
RX PubMed=12576672; DOI=10.1248/bpb.26.148;
RA Inoue H., Nakamura Y., Nagita M., Takai T., Masuda M., Nakamura N.,
RA Kanazawa H.;
RT "Calcineurin homologous protein isoform 2 (CHP2), Na+/H+ exchangers-binding
RT protein, is expressed in intestinal epithelium.";
RL Biol. Pharm. Bull. 26:148-155(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Seems to play an important role in colonic sodium absorption.
CC -!- SUBUNIT: Interacts with CHP1 and CHP2. {ECO:0000269|PubMed:12576672}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P48763-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P48763-2; Sequence=VSP_003394;
CC -!- TISSUE SPECIFICITY: Predominantly in small intestine, colon, and
CC stomach, with much lower levels in skeletal muscle, kidney, brain,
CC testis, uterus, heart and lung.
CC -!- PTM: Phosphorylated (Possible).
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
CC -!- CAUTION: The number, localization and denomination of hydrophobic
CC domains in the Na(+)/H(+) exchangers vary among authors. {ECO:0000305}.
CC -!- CAUTION: PubMed:8595899 sequence was originally thought to originate
CC from human. {ECO:0000305}.
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DR EMBL; L11236; AAA72350.1; -; mRNA.
DR EMBL; L11004; AAA75406.1; -; mRNA.
DR EMBL; S81591; AAB36180.1; -; mRNA.
DR PIR; A46748; A46748.
DR PIR; A57644; A57644.
DR RefSeq; NP_001106806.1; NM_001113335.1. [P48763-1]
DR RefSeq; NP_036785.2; NM_012653.2. [P48763-2]
DR AlphaFoldDB; P48763; -.
DR SMR; P48763; -.
DR IntAct; P48763; 2.
DR STRING; 10116.ENSRNOP00000021270; -.
DR ChEMBL; CHEMBL3886122; -.
DR GlyGen; P48763; 1 site.
DR iPTMnet; P48763; -.
DR PhosphoSitePlus; P48763; -.
DR PaxDb; P48763; -.
DR PRIDE; P48763; -.
DR Ensembl; ENSRNOT00000021270; ENSRNOP00000021270; ENSRNOG00000015567. [P48763-1]
DR GeneID; 24783; -.
DR KEGG; rno:24783; -.
DR UCSC; RGD:3719; rat. [P48763-1]
DR CTD; 6549; -.
DR RGD; 3719; Slc9a2.
DR eggNOG; KOG1966; Eukaryota.
DR GeneTree; ENSGT00940000156807; -.
DR HOGENOM; CLU_005912_4_3_1; -.
DR InParanoid; P48763; -.
DR OMA; DDHETMS; -.
DR OrthoDB; 316731at2759; -.
DR PhylomeDB; P48763; -.
DR TreeFam; TF317212; -.
DR Reactome; R-RNO-425986; Sodium/Proton exchangers.
DR PRO; PR:P48763; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000015567; Expressed in jejunum and 15 other tissues.
DR Genevisible; P48763; RN.
DR GO; GO:0016324; C:apical plasma membrane; TAS:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; ISO:RGD.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR004709; NaH_exchanger.
DR InterPro; IPR001953; NHE-2/4.
DR InterPro; IPR032103; NHE_CaM-bd.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF16644; NEXCaM_BD; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR PRINTS; PR01086; NAHEXCHNGR2.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..813
FT /note="Sodium/hydrogen exchanger 2"
FT /id="PRO_0000052354"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 14..34
FT /note="Name=A/M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 81..101
FT /note="Name=B/M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=C/M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=D/M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=E/M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=F/M5A"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=G/M5B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=H/M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Name=I/M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=J/M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=K/M9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 431..451
FT /note="Name=L"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical; Name=M13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 649..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7683411,
FT ECO:0000303|PubMed:8595899"
FT /id="VSP_003394"
FT CONFLICT 504
FT /note="H -> HW (in Ref. 3; AAB36180)"
FT /evidence="ECO:0000305"
FT CONFLICT 610..616
FT /note="LYQIRQR -> SLSNPPA (in Ref. 3; AAB36180)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="A -> P (in Ref. 3; AAB36180)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="V -> G (in Ref. 2; AAA75406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 813 AA; 91403 MW; 29727267D7085845 CRC64;
MGPSGTAHRM RAPLSWLLLL LLSLQVAVPA GALAETLLDA PGARGASSNP PSPASVVAPG
TTPFEESRLP VFTLDYPHVQ IPFEITLWIL LASLAKIGFH LYHKLPTIVP ESCLLIMVGL
LLGGIIFGVD EKSPPAMKTD VFFLYLLPPI VLDAGYFMPT RPFFENLGTI FWYAVVGTLW
NSIGIGLSLF GICQIEAFGL SDITLLQNLL FGSLISAVDP VAVLAVFENI HVNEQLYILV
FGESLLNDAV TVVLYNLFKS FCQMKTIQTV DVFAGIANFF VVGIGGVLIG ILLGFIAAFT
TRFTHNIRVI EPLFVFLYSY LSYITAEMFH LSGIMAITAC AMTMNKYVEE NVSQKSYTTI
KYFMKMLSSV SETLIFIFMG VSTVGKNHEW NWAFVCFTLA FCLIWRALGV FVLTQVINWF
RTIPLTFKDQ FIIAYGGLRG AICFALVFLL PATVFPRKKL FITAAIVVIF FTVFILGITI
RPLVEFLDVK RSNKKQQAVS EEIHCRFFDH VKTGIEDVCG HWGHNFWRDK FKKFDDKYLR
KLLIRENQPK SSIVSLYKKL EIKHAIEMAE TGMISTVPSF ASLNDCREEK IRKLTPGEMD
EIREILSRNL YQIRQRTLSY NRHNLTADTS ERQAKEILIR RRHSLRESLR KDNSLNRERR
ASTSTSRYLS LPKNTKLPEK LQKKNKVSNA DGNSSDSDMD GTTVLNLQPR ARRFLPDQFS
KKASPAYKME WKNEVDVGSA RAPPSVTPAP RSKEGGTQTP GVLRQPLLSK DQRFGRGRED
SLTEDVPPKP PPRLVRRASE PGNRKGRLGN EKP
