SL9B1_MOUSE
ID SL9B1_MOUSE Reviewed; 565 AA.
AC Q8C0X2; B5AFL0; Q8C1I8; Q8R3N0; Q9CPR9; Q9D400;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Sodium/hydrogen exchanger 9B1;
DE AltName: Full=Na(+)/H(+) exchanger-like domain-containing protein 1;
DE Short=NHE domain-containing protein 1;
DE AltName: Full=Sodium/hydrogen exchanger-like domain-containing protein 1;
DE AltName: Full=Solute carrier family 9 subfamily B member 1;
DE AltName: Full=Testis specific sodium-hydrogen exchanger {ECO:0000303|PubMed:19409551, ECO:0000303|PubMed:20036903};
DE Short=MtsNHE {ECO:0000303|PubMed:19409551, ECO:0000303|PubMed:20036903};
GN Name=Slc9b1 {ECO:0000312|MGI:MGI:1921696};
GN Synonyms=Nha1 {ECO:0000303|PubMed:27010853}, Nhedc1;
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] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19409551; DOI=10.1016/j.fertnstert.2009.03.056;
RA Liu T., Huang J.C., Lu C.L., Yang J.L., Hu Z.Y., Gao F., Liu Y.X.;
RT "Immunization with a DNA vaccine of testis-specific sodium-hydrogen
RT exchanger by oral feeding or nasal instillation reduces fertility in female
RT mice.";
RL Fertil. Steril. 93:1556-1566(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=20036903; DOI=10.2741/e115;
RA Liu T., Huang J.C., Zuo W.L., Lu C.L., Chen M., Zhang X.S., Li Y.C.,
RA Cai H., Zhou W.L., Hu Z.Y., Gao F., Liu Y.X.;
RT "A novel testis-specific Na+/H+ exchanger is involved in sperm motility and
RT fertility.";
RL Front. Biosci. 2:566-581(2010).
RN [5]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=27010853; DOI=10.1038/cddis.2016.65;
RA Chen S.R., Chen M., Deng S.L., Hao X.X., Wang X.X., Liu Y.X.;
RT "Sodium-hydrogen exchanger NHA1 and NHA2 control sperm motility and male
RT fertility.";
RL Cell Death Dis. 7:E2152-E2152(2016).
CC -!- FUNCTION: Sperm-specific Na(+)/H(+) exchanger involved in intracellular
CC pH regulation of spermatozoa (PubMed:20036903). Involved in sperm
CC motility and fertility (PubMed:20036903, PubMed:27010853,
CC PubMed:19409551). {ECO:0000269|PubMed:19409551,
CC ECO:0000269|PubMed:20036903, ECO:0000269|PubMed:27010853}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:19409551, ECO:0000269|PubMed:20036903,
CC ECO:0000269|PubMed:27010853}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8C0X2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0X2-2; Sequence=VSP_030186, VSP_030187;
CC Name=3;
CC IsoId=Q8C0X2-3; Sequence=VSP_030185;
CC Name=4;
CC IsoId=Q8C0X2-4; Sequence=VSP_030183, VSP_030184;
CC Name=5;
CC IsoId=Q8C0X2-5; Sequence=VSP_030181, VSP_030182;
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:20036903). Expressed in the
CC spermatids and spermatozoa (at protein level) (PubMed:20036903).
CC Specifically present in the principal piece of sperm tail (at protein
CC level) (PubMed:20036903, PubMed:27010853, PubMed:19409551).
CC {ECO:0000269|PubMed:19409551, ECO:0000269|PubMed:20036903,
CC ECO:0000269|PubMed:27010853}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal but males shown reduced fertility
CC caused by diminished sperm motility (PubMed:27010853). Addition of cAMP
CC analogs almost completely rescue the motility and infertility
CC phenotypes in vitro (PubMed:27010853). Double knockout of SLC9B1 and
CC SLC9B2 results in male infertility with a severe sperm mobility
CC reduction, indicating that these two gene are functionally redundant
CC (PubMed:27010853). {ECO:0000269|PubMed:27010853}.
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; EU846100; ACF60498.1; -; mRNA.
DR EMBL; AK007064; BAB24849.1; -; mRNA.
DR EMBL; AK015318; BAB29794.1; -; mRNA.
DR EMBL; AK016883; BAC25498.1; -; mRNA.
DR EMBL; AK016917; BAB30495.1; -; mRNA.
DR EMBL; AK029525; BAC26494.1; -; mRNA.
DR EMBL; BC025002; AAH25002.1; -; mRNA.
DR CCDS; CCDS17855.2; -. [Q8C0X2-1]
DR RefSeq; XP_006502267.1; XM_006502204.1.
DR AlphaFoldDB; Q8C0X2; -.
DR SMR; Q8C0X2; -.
DR STRING; 10090.ENSMUSP00000077644; -.
DR iPTMnet; Q8C0X2; -.
DR PhosphoSitePlus; Q8C0X2; -.
DR PaxDb; Q8C0X2; -.
DR PRIDE; Q8C0X2; -.
DR ProteomicsDB; 261062; -. [Q8C0X2-1]
DR ProteomicsDB; 261063; -. [Q8C0X2-2]
DR ProteomicsDB; 261064; -. [Q8C0X2-3]
DR ProteomicsDB; 261065; -. [Q8C0X2-4]
DR ProteomicsDB; 261066; -. [Q8C0X2-5]
DR UCSC; uc008rlf.1; mouse. [Q8C0X2-4]
DR UCSC; uc008rlj.3; mouse. [Q8C0X2-3]
DR MGI; MGI:1921696; Slc9b1.
DR eggNOG; KOG3826; Eukaryota.
DR InParanoid; Q8C0X2; -.
DR PhylomeDB; Q8C0X2; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 74446; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Slc9b1; mouse.
DR PRO; PR:Q8C0X2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C0X2; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR030187; SLC9B1.
DR PANTHER; PTHR31102:SF5; PTHR31102:SF5; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Cell membrane; Cell projection; Cilium;
KW Fertilization; Flagellum; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..565
FT /note="Sodium/hydrogen exchanger 9B1"
FT /id="PRO_0000314009"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 77..114
FT /note="KVPGRRETQTKETQTTEIERKETKKKRGTNSYCPPQGT -> SCTHCTMDST
FT LGPYRSRSSPWWKFVWTCSYFLQCFPWG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030181"
FT VAR_SEQ 115..565
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030182"
FT VAR_SEQ 123..145
FT /note="AALIALWTLLWALIGQEVLPGGN -> MSNKKCTWGENEKYKMQMIRLTV
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030183"
FT VAR_SEQ 146..565
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030184"
FT VAR_SEQ 270..565
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030185"
FT VAR_SEQ 364..378
FT /note="ERLTQRRAFLVLSMC -> AASTLAYMDLEDWSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030186"
FT VAR_SEQ 379..565
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030187"
FT CONFLICT 167
FT /note="K -> R (in Ref. 2; BAB30495 and 3; AAH25002)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="Q -> G (in Ref. 2; BAC25498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 61958 MW; 7ECBC2E03DC90655 CRC64;
MSEHDVESNK KDDGFQSSVT VEMSKDPDSF HEETVEPKPE LKEPEPKEPE PKEPERKEPE
RKEPERKEPE RKEPERKVPG RRETQTKETQ TTEIERKETK KKRGTNSYCP PQGTINKTIT
DGAALIALWT LLWALIGQEV LPGGNLFGLV VIFYSAFLGG KILEFIKIPV VPPLPPLIGM
LLAGFTIRNV PIIYEFVHIP TTWSSALRNT ALTIILVRAG LGLDPQALKH LKGVCLRLSF
GPCFLEACSA ALFSHFIMNF PWQWGFLLGF VLGAVSPAVV VPNMLMLQEN GYGVEKGIPT
LLVAASSMDD IVAITGFNTF LSIVFSSGSV ISNILSSLRD VLIGVLVGIV MGVFVQYFPS
GDQERLTQRR AFLVLSMCIS AVLGCQHIGL HGSGGLVTLV LSFMAAKRWA EEKVGIQKIV
ANTWNVFQPL LFGLVGTEVS VESLESKTIG MCLATLGLAL SVRILSTFVL MSFANFRFKE
KVFIALSWIP KATVQAVLGP LALETARVMA PHLEGYAKAV MTVAFLAILI TAPNGALLIG
ILGPKILEQS EVTFPLKVEL SNFHH
