SL9C1_MOUSE
ID SL9C1_MOUSE Reviewed; 1175 AA.
AC Q6UJY2; E0CX34; Q7M6Y7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sodium/hydrogen exchanger 10;
DE AltName: Full=Na(+)/H(+) exchanger 10;
DE Short=NHE-10;
DE AltName: Full=Solute carrier family 10 member 10;
DE AltName: Full=Solute carrier family 9 member C1;
DE AltName: Full=Sperm-specific Na(+)/H(+) exchanger;
DE Short=sNHE;
GN Name=Slc9c1; Synonyms=Gm610, Slc9a10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/SvEv;
RX PubMed=14634667; DOI=10.1038/ncb1072;
RA Wang D., King S.M., Quill T.A., Doolittle L.K., Garbers D.L.;
RT "A new sperm-specific Na+/H+ exchanger required for sperm motility and
RT fertility.";
RL Nat. Cell Biol. 5:1117-1122(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION.
RX PubMed=12783626; DOI=10.1186/1471-2164-4-22;
RA Oduru S., Campbell J.L., Karri S., Hendry W.J., Khan S.A., Williams S.C.;
RT "Gene discovery in the hamster: a comparative genomics approach for gene
RT annotation by sequencing of hamster testis cDNAs.";
RL BMC Genomics 4:22-22(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH SAC.
RX PubMed=17517652; DOI=10.1073/pnas.0611296104;
RA Wang D., Hu J., Bobulescu I.A., Quill T.A., McLeroy P., Moe O.W.,
RA Garbers D.L.;
RT "A sperm-specific Na+/H+ exchanger (sNHE) is critical for expression and in
RT vivo bicarbonate regulation of the soluble adenylyl cyclase (sAC).";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9325-9330(2007).
CC -!- FUNCTION: Sperm-specific sodium/hydrogen exchanger involved in
CC intracellular pH regulation of spermatozoa. Required for sperm motility
CC and fertility. Involved in sperm cell hyperactivation, a step needed
CC for sperm motility which is essential late in the preparation of sperm
CC for fertilization. Required for the expression and bicarbonate
CC regulation of the soluble adenylyl cyclase (sAC).
CC {ECO:0000269|PubMed:14634667, ECO:0000269|PubMed:17517652}.
CC -!- SUBUNIT: Interacts with soluble adenylyl cyclase (sAC).
CC {ECO:0000269|PubMed:17517652}.
CC -!- INTERACTION:
CC Q6UJY2; Q8C0T9: Adcy10; NbExp=2; IntAct=EBI-15639080, EBI-15639026;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:14634667}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14634667}.
CC -!- TISSUE SPECIFICITY: Testis-specific. Specifically present in the
CC principal piece of sperm tail (at protein level).
CC {ECO:0000269|PubMed:14634667}.
CC -!- DOMAIN: The ion transport-like region is related to the membrane
CC segments of voltage-gated ion channels. Its function is unknown.
CC -!- DISRUPTION PHENOTYPE: Mice are normal but males are sterile. Male
CC sterility is due to defects in sperm motility inability to fertilize
CC intact eggs. Moreover, spermatozoa fail to develop the cAMP-dependent
CC protein tyrosine phosphorylation that coincides with the functional
CC maturation occurring upon incubation in capacitating conditions in
CC vitro. cAMP analogs almost completely rescue the motility and
CC infertility phenotypes. {ECO:0000269|PubMed:14634667}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88278.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=DAA01464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY368685; AAQ88278.1; ALT_FRAME; mRNA.
DR EMBL; AC124636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK001330; DAA01464.1; ALT_SEQ; mRNA.
DR CCDS; CCDS28198.2; -.
DR RefSeq; NP_932774.3; NM_198106.4.
DR AlphaFoldDB; Q6UJY2; -.
DR SMR; Q6UJY2; -.
DR DIP; DIP-60951N; -.
DR IntAct; Q6UJY2; 1.
DR STRING; 10090.ENSMUSP00000124969; -.
DR TCDB; 2.A.36.7.7; the monovalent cation:proton antiporter-1 (cpa1) family.
DR GlyGen; Q6UJY2; 1 site.
DR iPTMnet; Q6UJY2; -.
DR PhosphoSitePlus; Q6UJY2; -.
DR jPOST; Q6UJY2; -.
DR MaxQB; Q6UJY2; -.
DR PaxDb; Q6UJY2; -.
DR PRIDE; Q6UJY2; -.
DR ProteomicsDB; 257195; -.
DR Antibodypedia; 52176; 19 antibodies from 14 providers.
DR DNASU; 208169; -.
DR Ensembl; ENSMUST00000159945; ENSMUSP00000124969; ENSMUSG00000033210.
DR GeneID; 208169; -.
DR KEGG; mmu:208169; -.
DR UCSC; uc007ziq.2; mouse.
DR CTD; 285335; -.
DR MGI; MGI:2685456; Slc9c1.
DR VEuPathDB; HostDB:ENSMUSG00000033210; -.
DR eggNOG; KOG1965; Eukaryota.
DR GeneTree; ENSGT00940000162055; -.
DR HOGENOM; CLU_003400_1_0_1; -.
DR InParanoid; Q6UJY2; -.
DR OMA; CGNNIFE; -.
DR OrthoDB; 99426at2759; -.
DR PhylomeDB; Q6UJY2; -.
DR TreeFam; TF328865; -.
DR BioGRID-ORCS; 208169; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Slc9c1; mouse.
DR PRO; PR:Q6UJY2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6UJY2; protein.
DR Bgee; ENSMUSG00000033210; Expressed in spermatocyte and 3 other tissues.
DR ExpressionAtlas; Q6UJY2; baseline and differential.
DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
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 GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; IPR028483; N/H_exchanger_10.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR PANTHER; PTHR10110:SF87; PTHR10110:SF87; 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 1: Evidence at protein level;
KW Antiport; Cell membrane; Cell projection; Cilium; Developmental protein;
KW Differentiation; Flagellum; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Spermatogenesis;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1175
FT /note="Sodium/hydrogen exchanger 10"
FT /id="PRO_0000295705"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 618..698
FT /note="Ion transport-like"
FT REGION 1137..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 890..1026
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="M -> T (in Ref. 1; AAQ88278)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="M -> L (in Ref. 1; AAQ88278)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="N -> T (in Ref. 1; AAQ88278)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="V -> I (in Ref. 1; AAQ88278)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="A -> T (in Ref. 1; AAQ88278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="Y -> F (in Ref. 1; AAQ88278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1175 AA; 135545 MW; 4D65DAE082BF517F CRC64;
MEMEEISENL TASHSIKLTN MWLELLKSVF LSTPQDLPEI ILILSLICTV GAFLNMHLKD
FPIPLPVILF LIGCCFEILS FASTQIQIYA DAIQWMDPDI FFGIFTPVII FNVAFDMDIY
MLQKLFWQIL VITIPGFLIN YTLILWYLQS VNKLSLKTVP WLLFSAVLIS SDPMLTSASI
RDLGLSRSLT NLINGESLLT SVLSLVIYSG VVHIRFKSKS VNHTLAHKVM STAWSYIVES
FITGIVFTKV IQLWMATIFG DDVNHITLIF SVLYLIFYVC ELVGMSGIFT LATIGLFLNS
TSFKPGVEAF LLEFWNCLSF IGFLMVFTFI GLLIPAHTYL HISFSDVYYS LNIYFTLIVL
RLLVFLLMSP ILSRLGHGFS WRWAFIMVWS EMKGTPNINM ALLLAYSDIS LGSERERSQI
LFHGVSVCVI TLIVNRFILP MAVTKLGLRD VTSTKYKSVY YTFQHFQELT KSTAMALKFD
KDLANADWNM VDNAIILQNP YAMNQEEITE HQKVKCPDCN KEIDETLNIE AMELTNRRLL
SAQIASYQRQ YRNEVLSQSA VQVLVGAAGS FGEKKGEYMS PENIKNFSES KKLLSFLRKL
LLNWVYNTKK DKGVPSRYMF LHACHRIVFT NEFEYTGYLV VLMSTYPMII CWISRLKDIY
DNEIKCANYY FLAFYILEAL LKVAAMRKEF FSHTWLLFEL GITLVGVLDI ILIETDSISY
NFDLTETVVF MNVIRLLRIL RILKLVTPKL LQIIDKRMSQ QISFRYSILK GYVQGEMDVL
NIIDQIASSK QTKQILLKRV MRNMEHAMKE LGYLEYDHPE IAVTMKTKEE INVMLNMARE
IVKAFRSKGI IHKVEGTEIN KLIMAKKIQV LDLQSVIQPF NVEEAPCNIP WLSEDPEAIT
FIQEKAKVVT FDCGNNIFEE GDEPEGIYVI ISGMVKLKRS KPHLEMERVS AESEIKIHPL
PHTEYLLSGE IIGELNCLTK ERMQYSATCK TVVETYFIPI SHLYEGFEKR CPNMKHKMWQ
KIGLAITAQK IREHLSFEDW NYKLQLKLCN AFIRDIPKSM KTDIYDETVT HVVLIHGSAE
DCQLRKIYKA PFLIPVTCHQ IQGMEDFTKV MIIQTSIAVR KFRWNVRKYI PPRRISMKPD
SERESFETLD ETSEEDNGKK ENQENEELIE ENINI
