ID Q90710_CHICK Unreviewed; 1219 AA. AC Q90710; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035}; GN Name=AE2 {ECO:0000313|EMBL:AAC59881.1}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAC59881.1}; RN [1] {ECO:0000313|EMBL:AAC59881.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Proventriculus {ECO:0000313|EMBL:AAC59881.1}; RX PubMed=8621532; DOI=10.1074/jbc.271.15.8895; RA Cox K.H., Adair-Kirk T.L., Cox J.V.; RT "Variant AE2 anion exchanger transcripts accumulate in multiple cell types RT in the chicken gastric epithelium."; RL J. Biol. Chem. 271:8895-8902(1996). 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; U48889; AAC59881.1; -; mRNA. DR RefSeq; NP_990294.1; NM_204963.1. DR AlphaFoldDB; Q90710; -. DR GeneID; 395809; -. DR KEGG; gga:395809; -. DR CTD; 6522; -. DR VEuPathDB; HostDB:geneid_395809; -. DR OMA; RYQRMPT; -. DR OrthoDB; 1013180at2759; -. DR PhylomeDB; Q90710; -. 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:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro. 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 2: Evidence at transcript level; 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 701..722 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 743..766 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 786..811 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 818..836 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 880..897 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 913..933 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 970..989 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1010..1034 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1070..1089 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1096..1115 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT TRANSMEM 1147..1175 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362035" FT DOMAIN 343..616 FT /note="Band 3 cytoplasmic" FT /evidence="ECO:0000259|Pfam:PF07565" FT DOMAIN 672..1146 FT /note="Bicarbonate transporter-like transmembrane" FT /evidence="ECO:0000259|Pfam:PF00955" FT REGION 1..255 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 287..310 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 471..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..82 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..137 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..182 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..237 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..310 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1219 AA; 135289 MW; 25F42A73C3483B21 CRC64; MSRSPVSSEL HHIVSSAIES PEPPAPGPAS PPLAEEEEKD LNKALGVERF EEILSDAHPR SVEEPGRIYG EEDFEYHRQS SLHIHHPLSA HLPPDARRKK GVPKKGRKKR GRAAAPGENP PIEEGEEDEE EACDTETERS AEELRGGPAE GVQFFLQEDE VTERRAEEPP APPAPPGPTA EPHGATAPAA ASPGAEEGRA ADGGAVPEDG GSPGRPAARA TEHRSYNLHE RRRIGSMTGA DEAQYQKVPT DESEAQTLAS ADLDYMKSHR FEDVPGVRRH LVRKSAKAQV VHVGKEHREQ SARPRRSDRQ PHEVFVELNE LVLDKNQELQ WKETARWIKF EEDVEEETDR WGKPHVASLS FRSLLELRKT LSHGAVLLDL DQKTLPGVAH QVVEQMVITD QIRAEDRANV LRALLLKHSH PSDEKEFSFP RNISAGSLGS LLVHHHSTNH VGEGGEPAVT EPLIAGHGAE HDARVDVERE REVPTPAPPA GITRSKSKHE LKLLEKIPDN AEATVVLVGC VEFLDQPTMA FVRLQEAVEL DSVLEVPVPV RFLFLLLGPS STHMDYHEIG RSISTLMSDK QFHEAAYLAD DRHDLLTAIN EFLDCSVVVP PSEVQGEELR SVAHFQREML KKREEQEKRM LLEPKSPEEK ALLKLKVAED EDEDDPLRRT GRPFGGLIRD VRRRYPHYLS DFRDALNPQC IAAVIFIYFA ALSPAITFGG LLGEKTQDLI GVSELIISTS LQGVLFCLLG AQPLLVIGFS GPLLVFEEAF FTFCTSNGLE YLVGRVWIGF WLILIVLLMV ACEGSFLVRF VSRFTQEIFA FLISLIFIYE TFSKLGKIFQ EHPLHGCAQP NGTAWSNGTA APNGTAQRGA AKVTGQPNTA LLSLVLMAGT FFIAFFLRKF KNSRFFPGRI RRLIGDFGVP IAILVMVLVD YSIRDTYTQK LSVPSGFSVT APDKRGWVIN PLGERSDFPV WMMVASGLPA VLVFILIFME TQITTLIISK KERMLQKGSG FHLDLLLIVA MGGFFALFGL PWLAAATVRS VTHANALTVM SKAVAPGDKP KIQEVKEQRV TGLLVAVLVG LSIVIGELLR QIPLAVLFGI FLYMGVTSLN GIQFYERLQL LLMPPKHHPD VPYVKKVRTR MHLFTGLQLA CLAVLWAVMS TVASLAFPFI LILTVPVRMC LLSRIFTDRE MKCLDADEAE PILDEREGVD EYNEMPMPV //