SL9C2_HUMAN
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 03-AUG-2022, entry version 134.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 GlyGen; Q5TAH2; 2 sites.
DR iPTMnet; Q5TAH2; -.
DR PhosphoSitePlus; Q5TAH2; -.
DR BioMuta; SLC9C2; -.
DR DMDM; 74745831; -.
DR jPOST; Q5TAH2; -.
DR MassIVE; Q5TAH2; -.
DR PaxDb; Q5TAH2; -.
DR PeptideAtlas; Q5TAH2; -.
DR PRIDE; Q5TAH2; -.
DR ProteomicsDB; 64851; -.
DR Antibodypedia; 47078; 21 antibodies from 12 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 CTD; 284525; -.
DR DisGeNET; 284525; -.
DR GeneCards; SLC9C2; -.
DR HGNC; HGNC:28664; SLC9C2.
DR HPA; ENSG00000162753; Tissue enhanced (brain, choroid plexus, testis).
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; GISKMYT; -.
DR OrthoDB; 99426at2759; -.
DR PhylomeDB; Q5TAH2; -.
DR TreeFam; TF328865; -.
DR PathwayCommons; Q5TAH2; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 284525; 10 hits in 1064 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 102 other tissues.
DR Genevisible; Q5TAH2; HS.
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; 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; 1.20.120.350; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
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
