ID Q9UEY6_HUMAN Unreviewed; 1241 AA. AC Q9UEY6; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035}; GN Name=SLC4A2 {ECO:0000313|EMBL:AAF19583.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAF19583.2}; RN [1] {ECO:0000313|EMBL:AAF19583.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=9027488; DOI=10.1006/geno.1996.4467; RA Medina J.F., Acin A., Prieto J.; RT "Molecular cloning and characterization of the human AE2 anion exchanger RT (SLC4A2) gene."; RL Genomics 39:74-85(1997). RN [2] {ECO:0000313|EMBL:AAF19583.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=10623603; DOI=10.1006/bbrc.1999.1951; RA Medina J.F., Lecanda J., Acin A., Ciesielczyk P., Prieto J.; RT "Tissue-specific N-terminal isoforms from overlapping alternate promoters RT of the human AE2 anion exchanger gene."; RL Biochem. Biophys. Res. Commun. 267:228-235(2000). CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + CC hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00034408}; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004424}. Basolateral cell membrane CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004554}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane CC {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00034693}. Membrane CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU362035}. CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family. CC {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AH008864; AAF19583.2; -; Genomic_DNA. DR EMBL; U76667; AAF19583.2; JOINED; Genomic_DNA. DR AlphaFoldDB; Q9UEY6; -. DR PeptideAtlas; Q9UEY6; -. DR ChiTaRS; SLC4A2; human. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022853; F:active monoatomic ion transmembrane transporter activity; IEA:UniProt. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:UniProt. DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro. DR GO; GO:0098660; P:inorganic ion transmembrane transport; IEA:UniProt. DR Gene3D; 1.10.287.570; Helical hairpin bin; 1. DR InterPro; IPR001717; Anion_exchange. DR InterPro; IPR002978; Anion_exchange_2. DR InterPro; IPR018241; Anion_exchange_CS. DR InterPro; IPR013769; Band3_cytoplasmic_dom. DR InterPro; IPR011531; HCO3_transpt-like_TM_dom. DR InterPro; IPR003020; HCO3_transpt_euk. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR NCBIfam; TIGR00834; ae; 1. DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1. DR PANTHER; PTHR11453:SF14; ANION EXCHANGE PROTEIN 2; 1. DR Pfam; PF07565; Band_3_cyto; 1. DR Pfam; PF00955; HCO3_cotransp; 1. DR PRINTS; PR00165; ANIONEXCHNGR. DR PRINTS; PR01188; ANIONEXHNGR2. DR PRINTS; PR01231; HCO3TRNSPORT. DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1. DR PROSITE; PS00219; ANION_EXCHANGER_1; 1. DR PROSITE; PS00220; ANION_EXCHANGER_2; 1. PE 3: Inferred from homology; KW Anion exchange {ECO:0000256|ARBA:ARBA00022681}; KW Antiport {ECO:0000256|ARBA:ARBA00022449}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU362035}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035}; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU362035}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU362035}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}. FT TRANSMEM 709..730 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 751..774 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 794..819 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 826..844 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 901..918 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 934..954 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 991..1010 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1031..1055 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1091..1110 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1116..1136 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT DOMAIN 352..619 FT /note="Band 3 cytoplasmic" FT /evidence="ECO:0000259|Pfam:PF07565" FT DOMAIN 680..1169 FT /note="Bicarbonate transporter-like transmembrane" FT /evidence="ECO:0000259|Pfam:PF00955" FT REGION 1..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 288..320 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 449..470 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..55 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 62..99 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..320 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1241 AA; 136981 MW; D2FDA72E20D70D64 CRC64; MSSAPRRPAK GADSFCTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGETPT IEEGEEDEDE ASEAEGARAL TQPSPVSTPS SVQFFLQEDD SADRKAERTS PSSPAPLPHQ EATPRASKGA QAGTQVEEAE AEAVAVASGT AGGDDGGASG RPLPKAQPGH RSYNLQERRR IGSMTGAEQA LLPRVPTDEI EAQTLATADL DLMKSHRFED VPGVRRHLVR KNAKGSTQSG REGREPGPTP RARPRAPHKP HEVFVELNEL LLDKNQEPQW RETARWIKFE EDVEEETERW GKPHVASLSF RSLLELRRTL AHGAVLLDLD QQTLPGVAHQ VVEQMVISDQ IKAEDRANVL RALLLKHSHP SDEKDFSFPR NISAGSLGSL LGHHHGQGAE SDPHVTEPLM GGVPETRLEV ERERDVPPPA PPAGITRSKS KHELKLLEKI PENAEATVVL VGCVEFLSRP TMAFVRLREA VELDAVLEVP VPVRFLFLLL GPSSANMDYH EIGRSISTLM SDKQFHEAAY LADEREDLLT AINAFLDCSV VLPPSEVQGE ELLRSVAHFQ RQMLKKREEQ GRLLPTGAGL EPKSAQDKAL LQMVEAAGAA EDDPLRRTGR PFGGLIRDVR RRYPHYLSDF RDALDPQCLA AVIFIYFAAL SPAITFGGLL GEKTQDLIGV SELIMSTALQ GVVFCLLGAQ PLLVIGFSGP LLVFEEAFFS FCSSNHLEYL VGRVWIGFWL VFLALLMVAL EGSFLVRFVS RFTQEIFAFL ISLIFIYETF YKLVKIFQEH PLHGCSASNS SEVDGGENMT WAGARPTLGP GNRSLAGQSG QGKPRGQPNT ALLSLVLMAG TFFIAFFLRK FKNSRFFPGR IRRVIGDFGV PIAILIMVLV DYSIEDTYTQ KLSVPSGFSV TAPEKRGWVI NPLGEKSPFP VWMMVASLLP AILVFILIFM ETQITTLIIS KKERMLQKGS GFHLDLLLIV AMGGICALFG LPWLAAATVR SVTHANALTV MSKAVAPGDK PKIQEVKEQR VTGLLVALLV GLSIVIGDLL RQIPLAVLFG IFLYMGVTSL NGIQFYERLH LLLMPPKHHP DVTYVKKVRT LRMHLFTALQ LLCLALLWAV MSTAASLAFP FILILTVPLR MVVLTRIFTD REMKCLDANE AEPVFDEREG VDEYNEMPMP V //