SLC4A8
entrez
9498
canonical
uniprot
Q2Y0W8
canonical
ensembl
ENSG00000050438
resolver
ensp
ENSP00000351483
resolver
ensp
ENSP00000405812
resolver
ensp
ENSP00000441520
resolver
ensp
ENSP00000442561
resolver
ensp
ENSP00000547916
resolver
ensp
ENSP00000592480
resolver
ensp
ENSP00000679746
resolver
ensp
ENSP00000786158
resolver
genesymbol
SLC4A8
resolver
genesymbol_syn
KIAA0739
resolver
genesymbol_syn
NBC
resolver
genesymbol_syn
NBC3
resolver
genesymbol_syn
NDCBE1
resolver
hgnc
HGNC:11034
resolver
uniprot
A0MMZ1
resolver
uniprot
B4DHY0
resolver
uniprot
E7EML0
resolver
uniprot
F5GZ31
resolver
uniprot
F5H7F5
resolver
uniprot
O94843
resolver
uniprot
O95233
resolver
uniprot
Q004B4
resolver
uniprot
Q8N3U2
resolver
uniprot
Q8TC60
resolver
uniprot
Q9UKX8
resolver
uniprot_entry
S4A8_HUMAN
resolver
uniprot_sec
A0MMZ1
resolver
uniprot_sec
B4DHY0
resolver
uniprot_sec
E7EML0
resolver
uniprot_sec
F5GZ31
resolver
uniprot_sec
F5H7F5
resolver
uniprot_sec
O94843
resolver
uniprot_sec
O95233
resolver
uniprot_sec
Q004B4
resolver
uniprot_sec
Q8N3U2
resolver
uniprot_sec
Q8TC60
resolver
uniprot_sec
Q9UKX8
resolver
activity_regulation
ACTIVITY REGULATION: [Isoform 1]: Activity is inhibited by 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters). {ECO:0000269|PubMed:18577713}.; ACTIVITY REGULATION: [Isoform 3]: Activity is inhibited by 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters). {ECO:0000269|PubMed:11133997, ECO:0000269|PubMed:18577713}.; ACTIVITY REGULATION: [Isoform 4]: Activity is inhibited by 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters) (PubMed:18577713). Zinc-binding negatively regulates its activity (Probable). {ECO:0000269|PubMed:18577713, ECO:0000305|PubMed:28935959}.; ACTIVITY REGULATION: [Isoform 5]: Activity is inhibited by 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters). {ECO:0000269|PubMed:18577713}.
uniprot
proteins
amino_acid_sequence
MPAAGSNEPDGVLSYQRPDEEAVVDQGGTSTILNIHYEKEELEGHRTLYVGVRMPLGRQSHRHHRTHGQKHRRRGRGKGASQGEEGLEALAHDTPSQRVQFILGTEEDEEHVPHELFTELDEICMKEGEDAEWKETARWLKFEEDVEDGGERWSKPYVATLSLHSLFELRSCLINGTVLLDMHANSIEEISDLILDQQELSSDLNDSMRVKVREALLKKHHHQNEKKRNNLIPIVRSFAEVGKKQSDPHLMDKHGQTVSPQSVPTTNLEVKNGVNCEHSPVDLSKVDLHFMKKIPTGAEASNVLVGEVDILDRPIVAFVRLSPAVLLSGLTEVPIPTRFLFILLGPVGKGQQYHEIGRSMATIMTDEIFHDVAYKAKERDDLLAGIDEFLDQVTVLPPGEWDPSIRIEPPKNVPSQEKRKMPGVPNGNVCHIEQEPHGGHSGPELQRTGRLFGGLVLDIKRKAPWYWSDYRDALSLQCLASFLFLYCACMSPVITFGGLLGEATEGRISAIESLFGASMTGIAYSLFAGQALTILGSTGPVLVFEKILFKFCKDYALSYLSLRACIGLWTAFLCIVLVATDASSLVCYITRFTEEAFASLICIIFIYEAIEKLIHLAETYPIHMHSQLDHLSLYYCRCTLPENPNNHTLQYWKDHNIVTAEVHWANLTVSECQEMHGEFMGSACGHHGPYTPDVLFWSCILFFTTFILSSTLKTFKTSRYFPTRVRSMVSDFAVFLTIFTMVIIDFLIGVPSPKLQVPSVFKPTRDDRGWIINPIGPNPWWTVIAAIIPALLCTILIFMDQQITAVIINRKEHKLKKGCGYHLDLLMVAIMLGVCSIMGLPWFVAATVLSITHVNSLKLESECSAPGEQPKFLGIREQRVTGLMIFVLMGCSVFMTAILKFIPMPVLYGVFLYMGVSSLQGIQFFDRLKLFGMPAKHQPDFIYLRHVPLRKVHLFTLIQLTCLVLLWVIKASPAAIVFPMMVLALVFVRKVMDLCFSKRELSWLDDLMPESKKKKLDDAKKKAKEEEEAEKMLEIGGDKFPLESRKLLSSPGKNISCRCDPSEINISDEMPKTTVWKALSMNSGNAKEKSLFN
uniprot
proteins
function
FUNCTION: Mediates electroneutral sodium- and carbonate-dependent chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1 (PubMed:18577713). Plays a major role in pH regulation in neurons (By similarity). Mediates sodium reabsorption in the renal cortical collecting ducts (By similarity). {ECO:0000250|UniProtKB:Q8JZR6, ECO:0000269|PubMed:18577713}.
uniprot
proteins
mass_dalton
122938
uniprot
proteins
mutagenesis
MUTAGEN Q2Y0W8-4:80; /note="W->F: Significant reduction in zinc binding."; /evidence="ECO:0000269|PubMed:28935959"; MUTAGEN Q2Y0W8-4:167; /note="H->A: Significant reduction in zinc binding."; /evidence="ECO:0000269|PubMed:28935959"; MUTAGEN Q2Y0W8-4:169; /note="H->A: Significant reduction in zinc binding."; /evidence="ECO:0000269|PubMed:28935959
uniprot
proteins
protein_family
Anion exchanger (TC 2.A.31) family
uniprot
proteins
pubmed
10362779
uniprot
proteins
pubmed
11133997
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17715183
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18577713
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
28935959
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1093
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:17715183}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6RVG2}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6RVG2}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 479..499; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 524..544; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 566..586; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 596..616; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 688..708; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 732..752; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 779..799; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 825..845; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 882..902; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 905..925; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 963..983; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins