ID SL9C1_HUMAN Reviewed; 1177 AA. AC Q4G0N8; Q6ZRP4; Q7RTP2; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 2. DT 22-APR-2020, entry version 123. DE RecName: Full=Sodium/hydrogen exchanger 10; DE AltName: Full=Na(+)/H(+) exchanger 10; DE Short=NHE-10; DE AltName: Full=Solute carrier family 9 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=SLC9A10; 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 MRNA] (ISOFORM 1), AND VARIANTS VAL-158; RP VAL-286; MET-348; VAL-364; ALA-424; ILE-705; LYS-732; ILE-768 AND SER-826. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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). 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). 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) (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with soluble adenylyl cyclase (sAC). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q4G0N8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q4G0N8-2; Sequence=VSP_027010; CC -!- DOMAIN: The ion transport-like region is related to the membrane CC segments of voltage-gated ion channels. Its function is unknown (By CC similarity). {ECO:0000250}. 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=DAA01462.1; Type=Erroneous gene model prediction; Evidence={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; AK128084; BAC87265.1; -; mRNA. DR EMBL; BC044801; AAH44801.1; -; mRNA. DR EMBL; BK001328; DAA01462.1; ALT_SEQ; mRNA. DR CCDS; CCDS33817.1; -. [Q4G0N8-1] DR CCDS; CCDS82818.1; -. [Q4G0N8-2] DR RefSeq; NP_001307460.1; NM_001320531.1. [Q4G0N8-2] DR RefSeq; NP_898884.1; NM_183061.2. [Q4G0N8-1] DR BioGrid; 130083; 1. DR IntAct; Q4G0N8; 1. DR STRING; 9606.ENSP00000306627; -. DR TCDB; 2.A.36.7.5; the monovalent cation:proton antiporter-1 (cpa1) family. DR iPTMnet; Q4G0N8; -. DR PhosphoSitePlus; Q4G0N8; -. DR BioMuta; SLC9C1; -. DR DMDM; 158563886; -. DR jPOST; Q4G0N8; -. DR MassIVE; Q4G0N8; -. DR PaxDb; Q4G0N8; -. DR PeptideAtlas; Q4G0N8; -. DR PRIDE; Q4G0N8; -. DR ProteomicsDB; 62117; -. [Q4G0N8-1] DR ProteomicsDB; 62118; -. [Q4G0N8-2] DR Antibodypedia; 52176; 15 antibodies. DR Ensembl; ENST00000305815; ENSP00000306627; ENSG00000172139. [Q4G0N8-1] DR Ensembl; ENST00000487372; ENSP00000420688; ENSG00000172139. [Q4G0N8-2] DR Ensembl; ENST00000642317; ENSP00000495147; ENSG00000285044. [Q4G0N8-1] DR Ensembl; ENST00000647463; ENSP00000495048; ENSG00000285044. [Q4G0N8-2] DR GeneID; 285335; -. DR KEGG; hsa:285335; -. DR UCSC; uc003dyu.4; human. [Q4G0N8-1] DR CTD; 285335; -. DR DisGeNET; 285335; -. DR GeneCards; SLC9C1; -. DR HGNC; HGNC:31401; SLC9C1. DR HPA; ENSG00000172139; Tissue enriched (testis). DR MIM; 612738; gene. DR neXtProt; NX_Q4G0N8; -. DR OpenTargets; ENSG00000172139; -. DR PharmGKB; PA134914619; -. DR eggNOG; KOG1965; Eukaryota. DR eggNOG; COG0025; LUCA. DR GeneTree; ENSGT00940000162055; -. DR HOGENOM; CLU_003400_1_0_1; -. DR InParanoid; Q4G0N8; -. DR KO; K14726; -. DR OMA; MVFTFTG; -. DR OrthoDB; 99426at2759; -. DR PhylomeDB; Q4G0N8; -. DR TreeFam; TF328865; -. DR Reactome; R-HSA-2672351; Stimuli-sensing channels. DR ChiTaRS; SLC9C1; human. DR GeneWiki; SLC9A10; -. DR GenomeRNAi; 285335; -. DR Pharos; Q4G0N8; Tdark. DR PRO; PR:Q4G0N8; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q4G0N8; protein. DR Bgee; ENSG00000172139; Expressed in testis and 48 other tissues. DR ExpressionAtlas; Q4G0N8; baseline and differential. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005216; F:ion channel activity; IEA:InterPro. 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; IEA:Ensembl. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. 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; IPR005821; Ion_trans_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; PF00520; Ion_trans; 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 Alternative splicing; Antiport; Cell membrane; Cell projection; Cilium; KW Developmental protein; Differentiation; Flagellum; Glycoprotein; KW Ion transport; Membrane; Polymorphism; Reference proteome; Sodium; KW Sodium transport; Spermatogenesis; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..1177 FT /note="Sodium/hydrogen exchanger 10" FT /id="PRO_0000295704" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 73..93 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 103..123 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 138..158 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 167..187 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 204..224 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 301..321 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 333..353 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 364..384 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 405..425 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 613..633 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 646..666 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 675..695 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 707..727 FT /note="Helical" FT /evidence="ECO:0000255" FT NP_BIND 870..1003 FT /note="cNMP" FT REGION 598..678 FT /note="Ion transport-like" FT CARBOHYD 278 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 294..341 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027010" FT VARIANT 158 FT /note="I -> V (in dbSNP:rs9828502)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033324" FT VARIANT 286 FT /note="I -> V (in dbSNP:rs9872691)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033325" FT VARIANT 348 FT /note="I -> M (in dbSNP:rs9809404)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033326" FT VARIANT 364 FT /note="I -> V (in dbSNP:rs9809384)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_050233" FT VARIANT 424 FT /note="T -> A (in dbSNP:rs6768523)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033327" FT VARIANT 705 FT /note="T -> I (in dbSNP:rs4434123)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033328" FT VARIANT 732 FT /note="Q -> K (in dbSNP:rs6781844)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033329" FT VARIANT 768 FT /note="S -> I (in dbSNP:rs9288938)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_033330" FT VARIANT 826 FT /note="G -> S (in dbSNP:rs28516377)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_061369" FT CONFLICT 74 FT /note="M -> I (in Ref. 1; BAC87265)" FT /evidence="ECO:0000305" FT CONFLICT 785 FT /note="E -> D (in Ref. 1; BAC87265)" FT /evidence="ECO:0000305" FT CONFLICT 788 FT /note="I -> T (in Ref. 1; BAC87265)" FT /evidence="ECO:0000305" SQ SEQUENCE 1177 AA; 135206 MW; FD04B5B41D0EA2DC CRC64; MAGIFKEFFF STEDLPEVIL TLSLISSIGA FLNRHLEDFP IPVPVILFLL GCSFEVLSFT SSQVQRYANA IQWMSPDLFF RIFTPVVFFT TAFDMDTYML QKLFWQILLI SIPGFLVNYI LVLWHLASVN QLLLKPTQWL LFSAILVSSD PMLTAAAIRD LGLSRSLISL INGESLMTSV ISLITFTSIM DFDQRLQSKR NHTLAEEIVG GICSYIIASF LFGILSSKLI QFWMSTVFGD DVNHISLIFS ILYLIFYICE LVGMSGIFTL AIVGLLLNST SFKAAIEETL LLEFWTFLSR IAFLMVFTFF GLLIPAHTYL YIEFVDIYYS LNIYLTLIVL RFLTLLLISP VLSRVGHEFS WRWIFIMVCS EMKGMPNINM ALLLAYSDLY FGSDKEKSQI LFHGVLVCLI TLVVNRFILP VAVTILGLRD ATSTKYKSVC CTFQHFQELT KSAASALKFD KDLANADWNM IEKAITLENP YMLNEEETTE HQKVKCPHCN KEIDEIFNTE AMELANRRLL SAQIASYQRQ YRNEILSQSA VQVLVGAAES FGEKKGKCMS LDTIKNYSES QKTVTFARKL LLNWVYNTRK EKEGPSKYFF FRICHTIVFT EEFEHVGYLV ILMNIFPFII SWISQLNVIY HSELKHTNYC FLTLYILEAL LKIAAMRKDF FSHAWNIFEL AITLIGILHV ILIEIDTIKY IFNETEVIVF IKVVQFFRIL RIFKLIAPKL LQIIDKRMSH QKTFWYGILK GYVQGEADIM TIIDQITSSK QIKQMLLKQV IRNMEHAIKE LGYLEYDHPE IAVTVKTKEE INVMLNMATE ILKAFGLKGI ISKTEGAGIN KLIMAKKKEV LDSQSIIRPL TVEEVLYHIP WLDKNKDYIN FIQEKAKVVT FDCGNDIFEE GDEPKGIYII ISGMVKLEKS KPGLGIDQMV ESKEKDFPII DTDYMLSGEI IGEINCLTNE PMKYSATCKT VVETCFIPKT HLYDAFEQCS PLIKQKMWLK LGLAITARKI REHLSYEDWN YNMQLKLSNI YVVDIPMSTK TDIYDENLIY VILIHGAVED CLLRKTYRAP FLIPITCHQI QSIEDFTKVV IIQTPINMKT FRRNIRKFVP KHKSYLTPGL IGSVGTLEEG IQEERNVKED GAHSAATARS PQPCSLLGTK FNCKESPRIN LRKVRKE //