ID B3A3_RAT Reviewed; 1227 AA. AC P23348; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 27-MAR-2024, entry version 149. DE RecName: Full=Anion exchange protein 3; DE Short=AE 3; DE Short=Anion exchanger 3; DE AltName: Full=Band 3-related protein 3; DE Short=B3RP-3; DE AltName: Full=Neuronal band 3-like protein; DE AltName: Full=Solute carrier family 4 member 3; GN Name=Slc4a3; Synonyms=Ae3, B3rp3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=2294114; DOI=10.1016/s0021-9258(19)40253-6; RA Kudrycki K.E., Newman P.R., Shull G.E.; RT "cDNA cloning and tissue distribution of mRNAs for two proteins that are RT related to the band 3 Cl-/HCO3-exchanger."; RL J. Biol. Chem. 265:462-471(1990). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-170; SER-175 AND RP SER-198, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [3] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY RP REGULATION. RX PubMed=10548554; DOI=10.1042/bj3440221; RA Sterling D., Casey J.R.; RT "Transport activity of AE3 chloride/bicarbonate anion-exchange proteins and RT their regulation by intracellular pH."; RL Biochem. J. 344:221-229(1999). CC -!- FUNCTION: Sodium-independent anion exchanger which mediates the CC electroneutral exchange of chloride for bicarbonate ions across the CC cell membrane. May be involved in the regulation of intracellular pH, CC and the modulation of cardiac action potential (By similarity). CC {ECO:0000250|UniProtKB:P48751, ECO:0000269|PubMed:10548554}. 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:0000269|PubMed:10548554}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10548554}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in the brain and heart. CC {ECO:0000269|PubMed:2294114}. CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family. CC {ECO:0000305}. 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; J05167; AAA40798.1; -; mRNA. DR PIR; B34911; B34911. DR RefSeq; NP_058745.1; NM_017049.1. DR AlphaFoldDB; P23348; -. DR SMR; P23348; -. DR BioGRID; 246905; 1. DR STRING; 10116.ENSRNOP00000027337; -. DR GlyCosmos; P23348; 1 site, No reported glycans. DR GlyGen; P23348; 1 site. DR iPTMnet; P23348; -. DR PhosphoSitePlus; P23348; -. DR PaxDb; 10116-ENSRNOP00000027337; -. DR GeneID; 24781; -. DR KEGG; rno:24781; -. DR UCSC; RGD:3712; rat. DR AGR; RGD:3712; -. DR CTD; 6508; -. DR RGD; 3712; Slc4a3. DR eggNOG; KOG1172; Eukaryota. DR InParanoid; P23348; -. DR OrthoDB; 1013180at2759; -. DR PhylomeDB; P23348; -. DR Reactome; R-RNO-425381; Bicarbonate transporters. DR PRO; PR:P23348; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISO:RGD. DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:RGD. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015701; P:bicarbonate transport; ISO:RGD. DR GO; GO:0061337; P:cardiac conduction; ISO:RGD. DR GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD. DR GO; GO:0045851; P:pH reduction; ISS:UniProtKB. DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISS:UniProtKB. DR GO; GO:0051453; P:regulation of intracellular pH; ISO:RGD. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.287.570; Helical hairpin bin; 1. DR InterPro; IPR001717; Anion_exchange. DR InterPro; IPR002979; Anion_exchange_3. 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:SF15; ANION EXCHANGE PROTEIN 3; 1. DR Pfam; PF07565; Band_3_cyto; 1. DR Pfam; PF00955; HCO3_cotransp; 1. DR PRINTS; PR00165; ANIONEXCHNGR. DR PRINTS; PR01189; ANIONEXHNGR3. 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 1: Evidence at protein level; KW Anion exchange; Antiport; Cell membrane; Glycoprotein; Ion transport; KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..1227 FT /note="Anion exchange protein 3" FT /id="PRO_0000079222" FT TOPO_DOM 1..707 FT /note="Cytoplasmic" FT TRANSMEM 708..730 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 736..773 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 793..815 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 825..846 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 888..905 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 906..920 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 921..941 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 975..997 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1023..1044 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1078..1123 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1150..1186 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..255 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 286..312 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 428..497 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 708..1227 FT /note="Membrane (anion exchange)" FT COMPBIAS 7..23 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 62..77 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 98..113 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..151 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 435..453 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..497 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 175 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 294 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P16283" FT LIPID 1160 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 868 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 1227 AA; 135407 MW; 3EB1620EE011730E CRC64; MANGVIPPPG GPSPLPQVRV PLEEPPLGPD VEEEDDDLGK TLAVSRFGDL ISKTPAWDPE KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRLPP TSARHARRKR KKEKTSAPPS EGTPPIQEEG GAGAEEEEEE EEEEEGESEA EPVEPPPPGP PQKAKFSIGS DEDDSPGLSI KAPCAKALPS VGLPSDQSPQ RSGSSPSPRA RASRISTEKS RPWSPSASYD LRERLCPGSA LGNPGPEQRV PTDEAEAQML GSADLDDMKS HRLEDNPGVR RHLVKKPSRI QGGRGSPSGL APILRRKKKK KKLDRRPHEV FVELNELMLD RSQEPHWRET ARWIKFEEDV EEETERWGKP HVASLSFRSL LELRRTIAQG AALLDLEQTT LPGIAHLVVE TMIVSDQIRP EDRASVLRTL LLKHSHPNDD KDSGFFPRNP SSSSVNSVLG NHHPTPSHGP DGAVPTMADD LGEPAPLWPH DPDAKEKPLH MPGGDGHRGK SLKLLEKIPE DAEATVVLVG SVPFLEQPAA AFVRLSEAVL LESVLEVPVP VRFLFVMLGP SHTSTDYHEL GRSIATLMSD KLFHEAAYQA DDRQDLLGAI SEFLDGSIVI PPSEVEGRDL LRSVAAFQRE LLRKRREREQ TKVEMTTRGG YVAPGKELSL EMGGSEATSE DDPLQRTGSV FGGLVRDVKR RYPHYPSDLR DALHSQCVAA VLFIYFAALS PAITFGGLLG EKTEGLMGVS ELIVSTAVLG VLFSLLGAQP LLVVGFSGPL LVFEEAFFKF CRAQDLEYLT GRVWVGLWLV VFVLALVAAE GSFLVRYISP FTQEIFAFLI SLIFIYETFH KLYKVFTEHP LLPFYPPEEA LEPGLELNSS ALPPTEGPPG PRNQPNTALL SLILMLGTFL IAFFLRKFRN SRFLGGKARR VIGDFGIPIS ILVMVLVDYS ITDTYTQKLT VPTGLSVTSP HKRTWFIPPL GSARPFPPWM MVAAAVPALL VLILIFMETQ ITALIVSQKA RRLLKGSGFH LDLLLIGSLG GLCGLFGLPW LTAATVRSVT HVNALTVMRT AIAPGDKPQI QEVREQRVTG VLIASLVGLS IVMGAVLRRI PLAVLFGIFL YMGVTSLSGI QLSQRLLLIF MPAKHHPEQP YVTKVKTWRM HLFTFIQLGC IALLWVVKST VASLAFPFLL LLTVPLRRCL LPRLFQDREL QALDSEDAEP NFDEDGQDEY NELHMPV //