SL9B2_PONAB
ID SL9B2_PONAB Reviewed; 537 AA.
AC Q5R6B8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Sodium/hydrogen exchanger 9B2;
DE AltName: Full=Na(+)/H(+) exchanger NHA2;
DE AltName: Full=Na(+)/H(+) exchanger-like domain-containing protein 2;
DE Short=NHE domain-containing protein 2;
DE AltName: Full=Sodium/hydrogen exchanger-like domain-containing protein 2;
DE AltName: Full=Solute carrier family 9 subfamily B member 2;
GN Name=SLC9B2; Synonyms=NHA2, NHEDC2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Na+/H+ antiporter that extrudes Na(+) or Li(+) in exchange
CC for external protons across the membrane. Contributes to the regulation
CC of intracellular pH, Na(+) content and organellar volume. Plays an
CC important role for insulin secretion and clathrin-mediated endocytosis
CC in beta-cells. Involved in sperm motility and fertility. It is
CC controversial whether SLC9B2 plays a role in osteoclast differentiation
CC or not (By similarity). {ECO:0000250|UniProtKB:Q5BKR2,
CC ECO:0000250|UniProtKB:Q86UD5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5BKR2};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5BKR2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5BKR2}. Cell
CC projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q5BKR2};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Strong colocalization with LAMP1 and TCIRG1 in
CC osteoclasts. In beta-cells colocalizes with RAB4A and SYP. Localizes to
CC the basolateral membrane of polarized osteoclasts.
CC {ECO:0000250|UniProtKB:Q5BKR2}.
CC -!- MISCELLANEOUS: Inhibited by phloretin but not the classical SLC9A-
CC inhibitor amiloride. {ECO:0000250|UniProtKB:Q86UD5}.
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; CR860573; CAH92698.1; -; mRNA.
DR RefSeq; NP_001126579.1; NM_001133107.1.
DR AlphaFoldDB; Q5R6B8; -.
DR SMR; Q5R6B8; -.
DR STRING; 9601.ENSPPYP00000016719; -.
DR Ensembl; ENSPPYT00000033199; ENSPPYP00000023935; ENSPPYG00000014970.
DR GeneID; 100173571; -.
DR KEGG; pon:100173571; -.
DR CTD; 133308; -.
DR eggNOG; KOG3826; Eukaryota.
DR GeneTree; ENSGT00390000013285; -.
DR InParanoid; Q5R6B8; -.
DR OrthoDB; 833306at2759; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0010348; F:lithium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0015385; F:sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR037072; SLC9B2.
DR PANTHER; PTHR31102:SF14; PTHR31102:SF14; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 2: Evidence at transcript level;
KW Antiport; Cell membrane; Cell projection; Cilium; Cytoplasmic vesicle;
KW Endosome; Flagellum; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..537
FT /note="Sodium/hydrogen exchanger 9B2"
FT /id="PRO_0000331272"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 278
FT /note="Important for cation transport"
FT /evidence="ECO:0000250|UniProtKB:Q86UD5"
FT SITE 279
FT /note="Important for cation transport"
FT /evidence="ECO:0000250|UniProtKB:Q86UD5"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UD5"
SQ SEQUENCE 537 AA; 57541 MW; 6DBB62855FA3B055 CRC64;
MGDEDKRITY EDSEPSTGMN YTPSMHQETQ EETVMKLKGI DANEPTEGSI LLKSSEKKLQ
ETPTEANHVQ RLRQMLACPP HGLLDRVVTN VTIIVLLWAV IWSITGSECL PGGNLFGIII
LFYCAIIGGK LLGLIKLPTL PPLPSLLGML LAGFLIRNIP VINDNVQIKH KWSSSLRSIA
LSIILVRAGL GLDSKALKKL KGVCVRLSMG PCIVEACTSA LLAHYLLGLP WQWGFILGFV
LGAVSPAVVV PSMLLLQGGG YGVEKGVPTL LMAAGSFDDI LAITGFNTCL GIAFSTGSTV
FNVLRGVLEV VIGVATGSVL GFFIQYFPSC DQDKLVCKRT FLVLGLSVLA VFSSVHFGFP
GSGGLCTLVM AFLAGMGWTS EKAEVEKIIA VAWDIFQPLL FGLIGAEVSI ASLRPETVGL
CVATVGIAVL IRILTTFLMV CFAGFNLKEK IFISFAWLPK ATVQAAIGSV ALDTARSHGE
KQLEDYGMDV LTVAFLSILI TAPIGSLLIG LLGPRLLQKV EHQNKDEEVQ GETSVQV
