ID   SL9C2_HUMAN             Reviewed;        1124 AA.
AC   Q5TAH2; Q86UF3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Sodium/hydrogen exchanger 11;
DE   AltName: Full=Na(+)/H(+) exchanger 11;
DE            Short=NHE-11;
DE   AltName: Full=Solute carrier family 9 member 11;
DE   AltName: Full=Solute carrier family 9 member C2;
GN   Name=SLC9C2; Synonyms=SLC9A11;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-934.
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Involved in pH regulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: Contains an ion transport-like region is related to the
CC       membrane segments of voltage-gated ion channels. {ECO:0000250}.
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; AL139142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC042592; AAH42592.1; -; mRNA.
DR   CCDS; CCDS1308.1; -.
DR   RefSeq; NP_848622.2; NM_178527.3.
DR   AlphaFoldDB; Q5TAH2; -.
DR   SMR; Q5TAH2; -.
DR   STRING; 9606.ENSP00000356687; -.
DR   TCDB; 2.A.36.7.4; the monovalent cation:proton antiporter-1 (cpa1) family.
DR   GlyCosmos; Q5TAH2; 2 sites, No reported glycans.
DR   GlyGen; Q5TAH2; 2 sites.
DR   iPTMnet; Q5TAH2; -.
DR   PhosphoSitePlus; Q5TAH2; -.
DR   BioMuta; SLC9C2; -.
DR   DMDM; 74745831; -.
DR   jPOST; Q5TAH2; -.
DR   MassIVE; Q5TAH2; -.
DR   PaxDb; 9606-ENSP00000356687; -.
DR   PeptideAtlas; Q5TAH2; -.
DR   ProteomicsDB; 64851; -.
DR   Antibodypedia; 47078; 25 antibodies from 13 providers.
DR   DNASU; 284525; -.
DR   Ensembl; ENST00000367714.4; ENSP00000356687.3; ENSG00000162753.13.
DR   GeneID; 284525; -.
DR   KEGG; hsa:284525; -.
DR   MANE-Select; ENST00000367714.4; ENSP00000356687.3; NM_178527.4; NP_848622.2.
DR   UCSC; uc001giz.3; human.
DR   AGR; HGNC:28664; -.
DR   CTD; 284525; -.
DR   DisGeNET; 284525; -.
DR   GeneCards; SLC9C2; -.
DR   HGNC; HGNC:28664; SLC9C2.
DR   HPA; ENSG00000162753; Tissue enriched (testis).
DR   MIM; 620338; gene.
DR   neXtProt; NX_Q5TAH2; -.
DR   OpenTargets; ENSG00000162753; -.
DR   PharmGKB; PA134865165; -.
DR   VEuPathDB; HostDB:ENSG00000162753; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   GeneTree; ENSGT00940000162785; -.
DR   HOGENOM; CLU_003400_0_0_1; -.
DR   InParanoid; Q5TAH2; -.
DR   OMA; GYWCARI; -.
DR   OrthoDB; 1220385at2759; -.
DR   PhylomeDB; Q5TAH2; -.
DR   TreeFam; TF328865; -.
DR   PathwayCommons; Q5TAH2; -.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 284525; 10 hits in 1142 CRISPR screens.
DR   ChiTaRS; SLC9C2; human.
DR   GeneWiki; SLC9A11; -.
DR   GenomeRNAi; 284525; -.
DR   Pharos; Q5TAH2; Tdark.
DR   PRO; PR:Q5TAH2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5TAH2; Protein.
DR   Bgee; ENSG00000162753; Expressed in right uterine tube and 104 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10110; SODIUM/HYDROGEN EXCHANGER; 1.
DR   PANTHER; PTHR10110:SF91; SODIUM_HYDROGEN EXCHANGER 11; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   Genevisible; Q5TAH2; HS.
PE   2: Evidence at transcript level;
KW   Antiport; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW   Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1124
FT                   /note="Sodium/hydrogen exchanger 11"
FT                   /id="PRO_0000295706"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        612..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        641..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        674..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        706..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          642..723
FT                   /note="Ion transport-like"
FT                   /evidence="ECO:0000250"
FT   BINDING         867..999
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         481
FT                   /note="T -> M (in dbSNP:rs7551131)"
FT                   /id="VAR_033331"
FT   VARIANT         505
FT                   /note="A -> G (in dbSNP:rs16846206)"
FT                   /id="VAR_033332"
FT   VARIANT         934
FT                   /note="R -> S (in dbSNP:rs17854214)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033333"
SQ   SEQUENCE   1124 AA;  129053 MW;  5D1E20BB33AEDD65 CRC64;
     MSSYFWAQNE SNRPDLLCGQ PADYLVEEKH FTTLVCFIVV LGGLLKMCLK NCEVIVLTIL
     SLSGFVIGHM AYNSVEVHQI VYPLLRTSSF SLYSYFSPLI IFMVALDVEF YTLKKMFWQV
     LLTGLISFST ASIIIGYVVI KFNKDSWDLQ SCLLFSITLG IIDPLRSVNS LKTIGISKIY
     IDLIRGESLI ICSIASIFFG NFRGNRIHFS IFRDLHVGIE LSYDILGSII FGYWCAKIIQ
     CILADVFSNM LTNIILCFSM VYMTFYIVEF LGMSGTLALA AVGLNLDSLT FKPKIELVIT
     KFLRIFSSVY EHLIYAFFGI VIGCGELSHY EFHTIPFIFI LFTTVNLVRL LTILLVSPIL
     MHSNYEYNWR WGVVITWSGI KGVFNLLWAP DVYNLAERKV EVPQMFILYV QVISLLTMGI
     NSYVMTQSAR KLDLCVLSLP RQMILQNATQ HIQEIVQNTI TLFKTEKILT NVNWTLVEDK
     TRIEYIPFSH VSHNDMKTES TTDEALMEEA RLHVAAIQMS SFEKQRNNGI LEIEAARILI
     GAAKCYYSIQ GKFMSIYDVS TYMRTRSWLI KFKNVLTFLE YCIEKIHFIP PESNTFLTFI
     FHIVFSEEFE YTGQIINLIY IYPMIIHLWP MARGLNVSAL ISINYYFMFL YVLESTLKII
     ILKRKYFQQC WNTLEFFILV IGIIDIFCVY FVKLRPDNLA LIQLTVIMGY LRIIRFLPLF
     KIIVPILIRI ADVQIKKRLS LMYSITKGYI KSQEDAKLLI KQIAVCESIY QKLCEILETN
     KQDAVKELVL MEHEGRDVVI ALKTKQAIRN VIAKALKNLT FLCSRGIIDK HEVIEINKVL
     LKKLKALNNF PKAIPPPTPD IYLHNIIWLE GKDVLIDFFK ERAKLACFDS GDTICKGGEM
     PQGIYLIISG MAILHSLSPT FGIESNQRCD RGSRDMFTEF CTTGDIIGEL SCLLKREIEY
     TVICETSLQA CFISLEDLYE GFDAFWPSLE YKIWLKLALS TAYQYFESSL IDEDLRFQNC
     VMFNQAYVET LSSYSDMIID NMTMKFVIIV YGSVIDTKTE EPYFAPCIIP TTCEQVQGTS
     DLSKLLIIQA SELTQRNSNT NVMASVNTVF EQPGKNINGR QKMS
//