SLC4A1
entrez
6521
canonical
uniprot
P02730
canonical
ensembl
ENSG00000004939
resolver
ensp
ENSP00000262418
resolver
genesymbol
SLC4A1
resolver
genesymbol_syn
AE1
resolver
genesymbol_syn
DI
resolver
genesymbol_syn
EPB3
resolver
hgnc
HGNC:11027
resolver
uniprot
G4V2I6
resolver
uniprot
P78487
resolver
uniprot
Q1ZZ45
resolver
uniprot
Q4KKW9
resolver
uniprot
Q4VB84
resolver
uniprot
Q9UCY7
resolver
uniprot
Q9UDJ1
resolver
uniprot_entry
B3AT_HUMAN
resolver
uniprot_sec
G4V2I6
resolver
uniprot_sec
P78487
resolver
uniprot_sec
Q1ZZ45
resolver
uniprot_sec
Q4KKW9
resolver
uniprot_sec
Q4VB84
resolver
uniprot_sec
Q9UCY7
resolver
uniprot_sec
Q9UDJ1
resolver
activity_regulation
ACTIVITY REGULATION: Phenyl isothiocyanate inhibits anion transport in vitro.
uniprot
proteins
amino_acid_sequence
MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV
uniprot
proteins
disease_involvement
DISEASE: Ovalocytosis, Southeast Asian (SAO) [MIM:166900]: An autosomal dominant hematologic disorder characterized by ovalocytic erythrocytes that are rigid and exhibit reduced expression of many erythrocyte antigens. Clinical manifestations include mild hemolysis, intermittent jaundice and gallstones. However, the disorder is most often asymptomatic. {ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:1722314}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spherocytosis 4 (SPH4) [MIM:612653]: An autosomal dominant form of spherocytosis, a group of hematologic disorders characterized by the presence of numerous abnormally shaped erythrocytes which are generally spheroidal. Affected individuals have anemia, jaundice, and splenomegaly. Clinical severity is variable. Some individuals are asymptomatic, whereas others have severe hemolytic anemia requiring erythrocyte transfusion. {ECO:0000269|PubMed:10580570, ECO:0000269|PubMed:10745622, ECO:0000269|PubMed:10942416, ECO:0000269|PubMed:11380459, ECO:0000269|PubMed:1378323, ECO:0000269|PubMed:15813913, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:7530501, ECO:0000269|PubMed:8547122, ECO:0000269|PubMed:8640229, ECO:0000269|PubMed:8943874, ECO:0000269|PubMed:9012689, ECO:0000269|PubMed:9207478, ECO:0000269|PubMed:9233560, ECO:0000269|PubMed:9973643}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Renal tubular acidosis, distal, 1 (DRTA1) [MIM:179800]: An autosomal dominant disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification. {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:9312167, ECO:0000269|PubMed:9600966}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Renal tubular acidosis, distal, 4, with hemolytic anemia (DRTA4) [MIM:611590]: An autosomal recessive disease characterized by the association of hemolytic anemia with distal renal tubular acidosis, the reduced ability to acidify urine resulting in variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:15211439, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:36320073, ECO:0000269|PubMed:9854053}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cryohydrocytosis (CHC) [MIM:185020]: An autosomal dominant disorder of red cell membrane permeability characterized by cold-induced changes in cell volume, resulting in cold-sensitive stomatocytosis, and increased erythrocyte osmotic fragility and autohemolysis at 4 degrees Celsius. Patients present with mild to moderate hemolytic anemia, splenomegaly, fatigue, and pseudohyperkalemia due to a potassium leak from the erythrocytes. {ECO:0000269|PubMed:16227998}. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307). {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307, ECO:0000269|PubMed:35835865}.; FUNCTION: (Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305). {ECO:0000269|PubMed:12692305, ECO:0000269|PubMed:14630931}.
uniprot
proteins
mass_dalton
101792
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="E->A,R: Impairs expression at the cell membrane."; /evidence="ECO:0000269|PubMed:24121512"; MUTAGEN 283; /note="R->A,E,S: Impairs expression at the cell membrane."; /evidence="ECO:0000269|PubMed:24121512"; MUTAGEN 642; /note="N->D: Loss of N-glycosylation site."; /evidence="ECO:0000269|PubMed:24121512"; MUTAGEN 681; /note="E->Q: Impairs expression at the cell membrane."; /evidence="ECO:0000269|PubMed:24121512
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation. {ECO:0000269|PubMed:10942405, ECO:0000269|PubMed:1998697}.; PTM: Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation. {ECO:0000269|PubMed:10942405, ECO:0000269|PubMed:1998697}.; PTM: N-glycosylated. {ECO:0000269|PubMed:26542571}.
uniprot
proteins
protein_family
Anion exchanger (TC 2.A.31) family
uniprot
proteins
pubmed
10580570
uniprot
proteins
pubmed
10738034
uniprot
proteins
pubmed
10745622
uniprot
proteins
pubmed
10861210
uniprot
proteins
pubmed
10926824
uniprot
proteins
pubmed
10942405
uniprot
proteins
pubmed
10942416
uniprot
proteins
pubmed
11049968
uniprot
proteins
pubmed
11061863
uniprot
proteins
pubmed
11155072
uniprot
proteins
pubmed
11208088
uniprot
proteins
pubmed
11380459
uniprot
proteins
pubmed
12692305
uniprot
proteins
pubmed
1352774
uniprot
proteins
pubmed
1378323
uniprot
proteins
pubmed
14630931
uniprot
proteins
pubmed
14734552
uniprot
proteins
pubmed
15211439
uniprot
proteins
pubmed
1527044
uniprot
proteins
pubmed
1538405
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15813913
uniprot
proteins
pubmed
16227998
uniprot
proteins
pubmed
16252102
uniprot
proteins
pubmed
1678289
uniprot
proteins
pubmed
1722314
uniprot
proteins
pubmed
1885574
uniprot
proteins
pubmed
1998697
uniprot
proteins
pubmed
20151848
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21849667
uniprot
proteins
pubmed
2204832
uniprot
proteins
pubmed
23219802
uniprot
proteins
pubmed
24121512
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2594752
uniprot
proteins
pubmed
26049106
uniprot
proteins
pubmed
26542571
uniprot
proteins
pubmed
2790053
uniprot
proteins
pubmed
28387307
uniprot
proteins
pubmed
3223947
uniprot
proteins
pubmed
3372523
uniprot
proteins
pubmed
35835865
uniprot
proteins
pubmed
36320073
uniprot
proteins
pubmed
6345535
uniprot
proteins
pubmed
6615451
uniprot
proteins
pubmed
701248
uniprot
proteins
pubmed
7506871
uniprot
proteins
pubmed
7530501
uniprot
proteins
pubmed
7665627
uniprot
proteins
pubmed
7812009
uniprot
proteins
pubmed
8045253
uniprot
proteins
pubmed
8168533
uniprot
proteins
pubmed
8206915
uniprot
proteins
pubmed
8343110
uniprot
proteins
pubmed
8471774
uniprot
proteins
pubmed
8508760
uniprot
proteins
pubmed
8527430
uniprot
proteins
pubmed
8547122
uniprot
proteins
pubmed
8640229
uniprot
proteins
pubmed
8943874
uniprot
proteins
pubmed
9012689
uniprot
proteins
pubmed
9191821
uniprot
proteins
pubmed
9207478
uniprot
proteins
pubmed
9233560
uniprot
proteins
pubmed
9312167
uniprot
proteins
pubmed
9454576
uniprot
proteins
pubmed
9600966
uniprot
proteins
pubmed
9709005
uniprot
proteins
pubmed
9709782
uniprot
proteins
pubmed
9765907
uniprot
proteins
pubmed
9845551
uniprot
proteins
pubmed
9854053
uniprot
proteins
pubmed
9973643
uniprot
proteins
sequence_length
911
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:26542571, ECO:0000269|PubMed:7506871}; Multi-pass membrane protein {ECO:0000269|PubMed:26542571}. Basolateral cell membrane {ECO:0000269|PubMed:7506871}; Multi-pass membrane protein {ECO:0000269|PubMed:7506871}. Note=Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney. {ECO:0000269|PubMed:7506871}.
uniprot
proteins
transmembrane_region
TRANSMEM 404..427; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 436..456; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 460..476; /note="Discontinuously helical; Name=3"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 486..506; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 519..541; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 571..591; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 603..623; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 664..684; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 701..719; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 720..737; /note="Discontinuously helical; Name=10"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 761..781; /note="Helical; Name=11"; /evidence="ECO:0000269|PubMed:26542571"; TRANSMEM 782..800; /note="Helical; Name=12"; /evidence="ECO:0000269|PubMed:26542571
uniprot
proteins