SLC9B2
entrez
133308
canonical
uniprot
Q86UD5
canonical
ensembl
ENSG00000164038
resolver
ensp
ENSP00000354574
resolver
ensp
ENSP00000378265
resolver
ensp
ENSP00000422477
resolver
ensp
ENSP00000425385
resolver
ensp
ENSP00000560751
resolver
ensp
ENSP00000560752
resolver
ensp
ENSP00000560755
resolver
ensp
ENSP00000560758
resolver
ensp
ENSP00000677452
resolver
enst
ENST00000503103
resolver
enst
ENST00000503230
resolver
enst
ENST00000890692
resolver
enst
ENST00000890696
resolver
genesymbol
SLC9B2
resolver
genesymbol_syn
NHA2
resolver
genesymbol_syn
NHEDC2
resolver
hgnc
HGNC:25143
resolver
uniprot
B5ME52
resolver
uniprot
B7Z488
resolver
uniprot
B7Z676
resolver
uniprot
E9PE63
resolver
uniprot
F6X1G7
resolver
uniprot
Q6ZMD8
resolver
uniprot
Q96D95
resolver
uniprot_entry
B7Z488_HUMAN
resolver
uniprot_entry
B7Z676_HUMAN
resolver
uniprot_entry
E9PE63_HUMAN
resolver
uniprot_entry
F6X1G7_HUMAN
resolver
uniprot_entry
SL9B2_HUMAN
resolver
uniprot_sec
B5ME52
resolver
uniprot_sec
Q6ZMD8
resolver
uniprot_sec
Q96D95
resolver
activity_regulation
ACTIVITY REGULATION: Allosterically inhibited by the N-terminal domain (PubMed:36177733). Inhibited by phloretin (PubMed:18000046, PubMed:36177733). {ECO:0000269|PubMed:18000046, ECO:0000269|PubMed:36177733}.
uniprot
proteins
amino_acid_sequence
MGDEDKRITYEDSEPSTGMNYTPSMHQEAQEETVMKLKGIDANEPTEGSILLKSSEKKLQETPTEANHVQRLRQMLACPPHGLLDRVITNVTIIVLLWAVVWSITGSECLPGGNLFGIIILFYCAIIGGKLLGLIKLPTLPPLPSLLGMLLAGFLIRNIPVINDNVQIKHKWSSSLRSIALSIILVRAGLGLDSKALKKLKGVCVRLSMGPCIVEACTSALLAHYLLGLPWQWGFILGFVLGAVSPAVVVPSMLLLQGGGYGVEKGVPTLLMAAGSFDDILAITGFNTCLGIAFSTGSTVFNVLRGVLEVVIGVATGSVLGFFIQYFPSRDQDKLVCKRTFLVLGLSVLAVFSSVHFGFPGSGGLCTLVMAFLAGMGWTSEKAEVEKIIAVAWDIFQPLLFGLIGAEVSIASLRPETVGLCVATVGIAVLIRILTTFLMVCFAGFNLKEKIFISFAWLPKATVQAAIGSVALDTARSHGEKQLEDYGMDVLTVAFLSILITAPIGSLLIGLLGPRLLQKVEHQNKDEEVQGETSVQV
uniprot
proteins
function
FUNCTION: Electroneutral Na(+) Li(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane (PubMed:18000046, PubMed:18508966, PubMed:22948142, PubMed:28154142, PubMed:36177733). Uses the proton gradient/membrane potential to extrude sodium (PubMed:22948142). Contributes to the regulation of intracellular pH and sodium homeostasis (By similarity). Also able to mediate Na(+)/Li(+) antiporter activity in kidney (PubMed:22948142). May play a physiological role in renal tubular function and blood pressure homeostasis (By similarity). Plays an important role for insulin secretion and clathrin-mediated endocytosis in beta-cells (By similarity). Involved in sperm motility and fertility (By similarity). It is controversial whether SLC9B2 plays a role in osteoclast differentiation or not (By similarity). {ECO:0000250|UniProtKB:Q5BKR2, ECO:0000269|PubMed:18000046, ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:22948142, ECO:0000269|PubMed:28154142, ECO:0000269|PubMed:36177733}.
uniprot
proteins
mass_dalton
57564
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="E->A,K: Decreases Na(+) Li(+)/H(+) antiporter activity."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 56; /note="E->A,K: Decreases Na(+) Li(+)/H(+) antiporter activity."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 57; /note="K->A: Does not affect Na(+) Li(+)/H(+) antiporter activity; when associated with A-58."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 57; /note="K->E: Decreases Na(+) Li(+)/H(+) antiporter activity; when associated with K-58."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 58; /note="K->A: Does not affect tNa(+) Li(+)/H(+) antiporter activity; when associated with A-57."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 58; /note="K->E: Decreases Na(+) Li(+)/H(+) antiporter activity; when associated with K-57."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 215; /note="E->R: Abolishes Na(+) Li(+)/H(+) antiporter activity. Shifts the specificity of the transporter from Na(+) to Li(+); when associated with E-432. Decreases plasma membrane localization. Partially retained in the ER; when associated with E-432."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 238; /note="G->R: Abolishes Na(+) Li(+)/H(+) antiporter activity. Changes subcellular localization. Retained in the ER."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 240; /note="V->L: Does not affect plasma membrane localization. Change in the substrate specificity with a preference for Li(+) over Na(+)."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 246; /note="P->A: Does not affect plasma membrane localization. Less sensitive to phloretin inhibition."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 246; /note="P->G: Does not affect plasma membrane localization. Abolishes antiporter activity. Less sensitive to phloretin inhibition."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 246; /note="P->S: Does not affect plasma membrane localization. Less sensitive to phloretin inhibition."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 246; /note="P->T: Does not affect plasma membrane localization. Less sensitive to phloretin inhibition."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 278..279; /note="DD->CC: Loss of ion transport activity; Does not rescue insulin secretion defect induced by knockdown of SLC9B2 in Min6 cells."; /evidence="ECO:0000269|PubMed:18000046, ECO:0000269|PubMed:23720317"; MUTAGEN 278; /note="D->G: Abolishes Na(+) Li(+)/H(+) antiporter activity. Does not affect plasma membrane localization."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 382; /note="K->E: Does not affect plasma membrane localization. Decreases the substrate specificity for Li(+)."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 406; /note="A->E: Does not affect plasma membrane localization. Decreases Na(+) Li(+)/H(+) antiporter activity."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 432; /note="R->E: Abolishes Na(+) Li(+)/H(+) antiporter activity. Shifts the specificity from Na(+) to Li(+); when associated with R-215. Decreases plasma membrane localization; when associated with R-215. Partially retained in the ER; when associated with R-215."; /evidence="ECO:0000269|PubMed:36177733"; MUTAGEN 432; /note="R->K,H: Loss of ion transport activity."; /evidence="ECO:0000269|PubMed:28154142"; MUTAGEN 432; /note="R->Q: Does not affect plasma membrane localization. Decreases the substrate specificity for Li(+)."; /evidence="ECO:0000269|PubMed:36177733
uniprot
proteins
protein_family
Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
18000046
uniprot
proteins
pubmed
18508966
uniprot
proteins
pubmed
22948142
uniprot
proteins
pubmed
23720317
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28071645
uniprot
proteins
pubmed
28154142
uniprot
proteins
pubmed
36177733
uniprot
proteins
sequence_length
537
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18000046, ECO:0000269|PubMed:36177733}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Apical cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Note=Strong colocalization with LAMP1 and TCIRG1 in osteoclasts. In beta-cells colocalizes with RAB4A and SYP. Localizes to the basolateral membrane of polarized osteoclasts. {ECO:0000250|UniProtKB:Q5BKR2}.
uniprot
proteins
transmembrane_region
TRANSMEM 87..104; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 114..133; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 145..161; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 172..189; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 201..227; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 234..242; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 271..290; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 301..324; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 340..357; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 362..373; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 391..411; /note="Helical; Name=11"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 418..440; /note="Helical; Name=12"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 462..473; /note="Helical; Name=13"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0"; TRANSMEM 487..509; /note="Helical; Name=14"; /evidence="ECO:0000250|UniProtKB:A0A6P3HVI0
uniprot
proteins