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0B3AT_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSLC4A1
DescriptionBand 3 anion transport protein (anion exchange protein 1) (ae 1) (solute carrier family 4 member 1) (cd233 antigen).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0015380 anion exchanger activity (TAS)
0008509 anion transporter activity (TAS)
0006820 anion transport (TAS)
0006873 cell ion homeostasis (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Bicarbonate (HCO3-) transport mechanisms are the principal regulators of pHin animal cells. Such transport also plays a vital role in acid-basemovements in the stomach.ancreas.ntestine.idney.eproductive organsand the central nervous system. Functional studies have suggested fourdifferent HCO3- transport modes. Anion exchanger proteins exchangeHCO3- for Cl- in a reversible.lectroneutral manner .Na+/HCO3- co-transportproteins mediate the coupled movement of Na+ and HCO3- across plasmamembranes.ften in an electrogenic manner . Na-driven Cl-/HCO3- exchangeand K+/HCO3- exchange activities have also been detected incertain cell types.lthough the molecular identities of the proteinsresponsible remain to be determined.Sequence analysis of the families of HCO3- transporters that have beencloned to date (revealsthat they are homologous. This is not entirely unexpected.iven that theyall transport HCO3- and are inhibited by a class of pharmacological agentscalled disulphonic stilbenes . They share around ~25-30% sequenceidentity.hich is distributed along their entire sequence length.nd havesimilar predicted membrane topologies.uggesting they have ~10transmembrane (TM) domains.This domain is found at the C-terminus of many bicarbonate transport proteins. It is also found in some plant proteins responsible for boron transport . In these proteins it covers almost the entire length of the sequence.
  IPR011531:HCO3-transporter, c-terminal
Bicarbonate (HCO3-) transport mechanisms are the principal regulators of pHin animal cells. Such transport also plays a vital role in acid-basemovements in the stomach.ancreas.ntestine.idney.eproductive organsand the central nervous system. Functional studies have suggested fourdifferent HCO3- transport modes. Anion exchanger proteins exchangeHCO3- for Cl- in a reversible.lectroneutral manner .Na+/HCO3- co-transportproteins mediate the coupled movement of Na+ and HCO3- across plasmamembranes.ften in an electrogenic manner . Na-driven Cl-/HCO3- exchangeand K+/HCO3- exchange activities have also been detected incertain cell types.lthough the molecular identities of the proteinsresponsible remain to be determined.Sequence analysis of the two families of HCO3- transporters that have beencloned to date (the anion exchangers and Na+/HCO3- co-transporters) revealsthat they are homologous. This is not entirely unexpected.iven that theyboth transport HCO3- and are inhibited by a class of pharmacological agentscalled disulphonic stilbenes . They share around ~25-30% sequenceidentity.hich is distributed along their entire sequence length.nd havesimilar predicted membrane topologies.uggesting they have ~10transmembrane (TM) domains.
  IPR013769:HCO3- transporter, cytoplasmic
Anion exchange proteins are thought to participate in pH and cell volumeregulation. They are glycosylated.lasma-membrane transport proteins thatexchange hydrogen carbonate (HCO3-) for chloride (Cl-) in a reversible.lectroneutral manner . To date three anion exchanger isoforms havebeen identified (AE1-3).E1 being the previously-characterised erythrocyteband 3 protein. They share a predicted topology of 12-14 transmembrane (TM)domains.ut have differing distribution patterns and cellular localisation.The best characterised isoform.E1.s known to be the most abundantmembrane protein in mature erythrocytes. It has a molecular mass of ~95 kDaand consists of two major domains. The N-terminal 390 residues form a water-soluble.ighly elongated domain that serves as an attachment site for thebinding of the membrane skeleton and other cytoplasmic proteins. Theremainder of the protein is a 55-kDa hydrophobic domain that is responsiblefor catalysing anion exchange. The function of the analogous domains of AE2and AE3 remains to be determined .Naturally-occurring mutations have been characterised in the AE1 gene.hichgive rise to forms of several human diseases: included are spherocytosis.ffecting red blood cells.nd familial distal renal tubular acidosis.kidney disease associated with the formation of kidney stones .
  IPR001717:Anion exchange protein
Anion exchange proteins are thought to participate in pH and cell volumeregulation. They are glycosylated.lasma-membrane transport proteins thatexchange hydrogen carbonate (HCO3-) for chloride (Cl-) in a reversible.lectroneutral manner . To date three anion exchanger isoforms havebeen identified (AE1-3).E1 being the previously-characterised erythrocyteband 3 protein. They share a predicted topology of 12-14 transmembrane (TM)domains.ut have differing distribution patterns and cellular localisation.The best characterised isoform.E1.s known to be the most abundantmembrane protein in mature erythrocytes. It has a molecular mass of ~95 kDaand consists of two major domains. The N-terminal 390 residues form a water-soluble.ighly elongated domain that serves as an attachment site for thebinding of the membrane skeleton and other cytoplasmic proteins. Theremainder of the protein is a 55-kDa hydrophobic domain that is responsiblefor catalysing anion exchange. The function of the analogous domains of AE2and AE3 remains to be determined .Naturally-occuring mutations have been characterised in the AE1 gene.hichgive rise to forms of several inherited human diseases. Around 20% ofhereditary spherocytosis cases arise from heterozygosity for AE1 mutations.nd result in the absence or decrease of the mutant protein in the red cellmembrane. Similarly.amilial distal renal tubular acidosis. conditionassociated with kidney stones.as been shown to be associated withmutations of AE1 of the renal collecting duct alpha-intercalated cell.ndit has been postulated that such mutations may affect the targeting of theAE1 protein.hich is usually directed to the basolateral membrane ofthese cells .Some of the proteins in this group are responsible for the molecular basis of the blood group antigens.urface markers on the outside of the red blood cell membrane. Most of these markers are proteins.ut some are carbohydrates attached to lipids or proteins [Reid M.E..omas-Francis C. The Blood Group Antigen FactsBook Academic Press.ondon / San Diego.1997)]. Band 3 anion transport protein (Anion exchange protein 1) belongs to the Diego blood group system and is associated with Di(a/b).r(a/b).d(a).b(a and WARR antigens.
  IPR002977:Anion exchanger, isoform 1
Bicarbonate (HCO3-) transport mechanisms are the principal regulators of pHin animal cells. Such transport also plays a vital role in acid-basemovements in the stomach.ancreas.ntestine.idney.eproductive organsand the central nervous system. Functional studies have suggested fourdifferent HCO3- transport modes. Anion exchanger proteins exchangeHCO3- for Cl- in a reversible.lectroneutral manner .Na+/HCO3- co-transportproteins mediate the coupled movement of Na+ and HCO3- across plasmamembranes.ften in an electrogenic manner . Na-driven Cl-/HCO3- exchangeand K+/HCO3- exchange activities have also been detected incertain cell types.lthough the molecular identities of the proteinsresponsible remain to be determined.Sequence analysis of the two families of HCO3- transporters that have beencloned to date (the anion exchangers and Na+/HCO3- co-transporters) revealsthat they are homologous. This is not entirely unexpected.iven that theyboth transport HCO3- and are inhibited by a class of pharmacological agentscalled disulphonic stilbenes . They share around ~25-30% sequenceidentity.hich is distributed along their entire sequence length.nd havesimilar predicted membrane topologies.uggesting they have ~10transmembrane (TM) domains.
  IPR003020:HCO3- transporter, eukaryote
IPR011531:HCO3_cotransp 
Evalue:-1e+125 
Location:371-839IPR013769:Band_3_cyto 
Evalue:-151.602066040039 
Location:86-329
SequencesProtein: B3AT_HUMAN (911 aa)
mRNA: NM_000342
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
KO assignmentK06573
  Level 3 annotation:
    solute carrier family 4, anion exchanger, member 1
  Level 2 annotation:
    Other ion-coupled transporters
    CD molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 290 residues, 39682565-39683432Exon2: 60 residues, 39684052-39684226Exon3: 58 residues, 39684312-39684482Exon4: 86 residues, 39686011-39686265Exon5: 57 residues, 39687389-39687556Exon6: 32 residues, 39688100-39688190Exon7: 60 residues, 39688566-39688740Exon8: 67 residues, 39690243-39690438Exon9: 51 residues, 39690552-39690701Exon10: 67 residues, 39690879-39691074Exon11: 72 residues, 39691306-39691517Exon12: 62 residues, 39692056-39692238Exon13: 30 residues, 39692390-39692475Exon14: 43 residues, 39692702-39692826Exon15: 47 residues, 39693297-39693433Exon16: 62 residues, 39693528-39693709Exon17: 22 residues, 39694468-39694530Exon18: 32 residues, 39695529-39695620Exon19: 29 residues, 39695745-39695828Exon20: 17 residues, 39700947-39700993Exon21: 2 residues, -Jump to B3AT_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4294 39509646-39556540 ~-47K 15975(HDAC5)(-)Loci: 4295 39682565-39700993 ~-18K 15992(SLC4A1)(-)Loci: 4296 39752520-39757666 ~-5K 15997(-)Loci: 3010 40098011-40104116 ~-6K 16007(+)Loci: 4297 40237112-40263147 ~-26K 16016(GJA7)(-)Loci: 4298 40338518-40348394 ~-10K 16022(GFAP)(-)Loci: 3009 39437557-39441961 ~-4K 15971(NAGS)(+)Link out to UCSC