ID   B3AT_RAT                Reviewed;         927 AA.
AC   P23562;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 3.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Band 3 anion transport protein;
DE   AltName: Full=Anion exchange protein 1 {ECO:0000305};
DE            Short=AE 1;
DE            Short=Anion exchanger 1;
DE   AltName: Full=Solute carrier family 4 member 1;
DE   AltName: CD_antigen=CD233;
GN   Name=Slc4a1 {ECO:0000312|RGD:3710}; Synonyms=Ae1;
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 [GENOMIC DNA] OF 46-927, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=2722777; DOI=10.1016/s0021-9258(18)83167-2;
RA   Kudrycki K.E., Shull G.E.;
RT   "Primary structure of the rat kidney band 3 anion exchange protein deduced
RT   from a cDNA.";
RL   J. Biol. Chem. 264:8185-8192(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-45.
RX   PubMed=8456965; DOI=10.1152/ajprenal.1993.264.3.f540;
RA   Kudrycki K.E., Shull G.E.;
RT   "Rat kidney band 3 Cl-/HCO3- exchanger mRNA is transcribed from an
RT   alternative promoter.";
RL   Am. J. Physiol. 264:F540-F547(1993).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-199 AND SER-222, AND
RP   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).
CC   -!- FUNCTION: Functions both as a transporter that mediates electroneutral
CC       anion exchange across the cell membrane and as a structural protein.
CC       Component of the ankyrin-1 complex of the erythrocyte membrane;
CC       required for normal flexibility and stability of the erythrocyte
CC       membrane and for normal erythrocyte shape via the interactions of its
CC       cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and
CC       hemoglobin. Functions as a transporter that mediates the 1:1 exchange
CC       of inorganic anions across the erythrocyte membrane. Mediates chloride-
CC       bicarbonate exchange in the kidney, and is required for normal
CC       acidification of the urine. {ECO:0000250|UniProtKB:P02730}.
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:0000250|UniProtKB:P02730};
CC   -!- SUBUNIT: A dimer in solution, but in its membrane environment, it
CC       exists primarily as a mixture of dimers and tetramers and spans the
CC       membrane asymmetrically. Component of the ankyrin-1 complex in the
CC       erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB
CC       and AQP1. Interacts with STOM; this interaction positively regulates
CC       SLC4A1 activity. Interacts with GYPA; a GYPA monomer is bound at each
CC       end of the SLC4A1 dimer forming an heterotetramer. Three SLC4A1 dimers
CC       (Band 3-I, Band 3-II and Band 3-III) participates in the ankyrin-1
CC       complex. Interacts (via the cytoplasmic domain) with EPB42; this
CC       interaction is mediated by the SLC4A1 Band 3-I dimer. Interacts (via
CC       the cytoplasmic domain) directly with ANK1; this interaction is
CC       mediated by the SLC4A1 Band 3-II and Band 3-III dimers.
CC       {ECO:0000250|UniProtKB:P02730}.
CC   -!- SUBUNIT: [Isoform 2]: Interacts with TMEM139.
CC       {ECO:0000250|UniProtKB:P02730}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P02730};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Basolateral
CC       cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P02730}. Note=Detected in the
CC       erythrocyte cell membrane and on the basolateral membrane of alpha-
CC       intercalated cells in the collecting duct in the kidney.
CC       {ECO:0000250|UniProtKB:P02730}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Erythrocyte;
CC         IsoId=P23562-1; Sequence=Displayed;
CC       Name=2; Synonyms=Kidney;
CC         IsoId=P23562-2; Sequence=VSP_000455;
CC   -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:2722777}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40800.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; J04793; AAA40800.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L02943; AAA40801.1; -; mRNA.
DR   PIR; A33810; A33810.
DR   PIR; A48854; A48854.
DR   RefSeq; NP_036783.2; NM_012651.2.
DR   RefSeq; XP_008766168.1; XM_008767946.2. [P23562-1]
DR   AlphaFoldDB; P23562; -.
DR   SMR; P23562; -.
DR   IntAct; P23562; 1.
DR   STRING; 10116.ENSRNOP00000028445; -.
DR   GlyCosmos; P23562; 1 site, No reported glycans.
DR   GlyGen; P23562; 1 site.
DR   iPTMnet; P23562; -.
DR   PhosphoSitePlus; P23562; -.
DR   SwissPalm; P23562; -.
DR   PaxDb; 10116-ENSRNOP00000028445; -.
DR   PeptideAtlas; P23562; -.
DR   GeneID; 24779; -.
DR   KEGG; rno:24779; -.
DR   UCSC; RGD:3710; rat. [P23562-1]
DR   AGR; RGD:3710; -.
DR   CTD; 6521; -.
DR   RGD; 3710; Slc4a1.
DR   eggNOG; KOG1172; Eukaryota.
DR   InParanoid; P23562; -.
DR   OrthoDB; 1013180at2759; -.
DR   PhylomeDB; P23562; -.
DR   Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-RNO-425381; Bicarbonate transporters.
DR   PRO; PR:P23562; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0170014; C:ankyrin-1 complex; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0030863; C:cortical cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR   GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030018; C:Z disc; IDA:RGD.
DR   GO; GO:0003779; F:actin binding; IPI:RGD.
DR   GO; GO:0030506; F:ankyrin binding; ISO:RGD.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR   GO; GO:0030492; F:hemoglobin binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; ISS:UniProtKB.
DR   GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; ISO:RGD.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR   GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR   GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; ISO:RGD.
DR   GO; GO:0035811; P:negative regulation of urine volume; ISO:RGD.
DR   GO; GO:0045852; P:pH elevation; ISO:RGD.
DR   GO; GO:0017121; P:plasma membrane phospholipid scrambling; ISO:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:RGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   GO; GO:0010447; P:response to acidic pH; IEP:RGD.
DR   GO; GO:0014823; P:response to activity; IDA:RGD.
DR   GO; GO:0010446; P:response to alkaline pH; IEP:RGD.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IDA:RGD.
DR   GO; GO:0010037; P:response to carbon dioxide; IDA:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP: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; IPR002977; Anion_exchange_1.
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:SF12; BAND 3 ANION TRANSPORT PROTEIN; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01187; ANIONEXHNGR1.
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   Acetylation; Alternative splicing; Anion exchange; Cell membrane;
KW   Glycoprotein; Ion transport; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..927
FT                   /note="Band 3 anion transport protein"
FT                   /id="PRO_0000079211"
FT   TOPO_DOM        1..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        421..444
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        445..452
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        453..473
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        474..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        477..493
FT                   /note="Discontinuously helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        494..502
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        503..523
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        524..535
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        536..558
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        559..586
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        587..607
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        608..618
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        619..639
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        640..679
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        680..700
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        701..716
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        717..735
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        736..753
FT                   /note="Discontinuously helical; Name=10"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        754..776
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        777..797
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        798..816
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        817..854
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   INTRAMEM        855..885
FT                   /note="Discontinuously helical"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        886..927
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   REGION          69..303
FT                   /note="Globular"
FT                   /evidence="ECO:0000250"
FT   REGION          190..199
FT                   /note="Interaction with ANK1"
FT                   /evidence="ECO:0000250"
FT   REGION          317..370
FT                   /note="Dimerization arm"
FT                   /evidence="ECO:0000250"
FT   REGION          367..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         31
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   MOD_RES         56
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         372
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   MOD_RES         920
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   LIPID           859
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         1..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000455"
SQ   SEQUENCE   927 AA;  103173 MW;  681A228474E5E9DE CRC64;
     MGDMQDHEKV LEIPDRDSEE ELEHVIEQIA YRDLDIPVTE MQESEALPTE QTATDYIPTS
     TSTSHPSSSQ VYVELQELMM DQRNQELQWV EAAHWIGLEE NLREDGVWGR PHLSYLTFWS
     LLELQKVFSK GTFLLDLAET SLAGVANKLL DSFIYEDQIR PQDRDELLRA LLLKRSHAED
     LKDLEGVKPA VLTRSGAPSE PLLPHQPSLE TKLYCAQAEG GSEEPSPSGI LKIPPNSETT
     LVLVGRASFL VKPVLGFVRL KEAVPLEDLV LPEPVSFLLV LLGPEAPHID YTQLGRAAAT
     LMTERVFRVT ASLAQSRGEL LSSLDSFLDC SLVLPPTEAP SEKALLNLVP VQKELLRKRY
     LPRPAKPDPN LYEALDGGKE GPGDEDDPLR RTGRIFGGLI RDIRRRYPYY LSDITDALSP
     QVLAAVIFIY FAALSPAVTF GGLLGEKTRN LMGVSELLIS TAVQGILFAL LGAQPLLVLG
     FSGPLLVFEE AFYSFCESNN LEYIVGRAWI GFWLILLVVL VVAFEGSFLV QYISRYTQEI
     FSFLISLIFI YETFSKLIKI FQDYPLQESY APVVMKPKPQ GPVPNTALLS LVLMVGTFLL
     AMMLRKFKNS TYFPGKLRRV IGDFGVPISI LIMVLVDTFI KNTYTQKLSV PDGLKVSNSS
     ARGWVIHPLG LYNHFPKWMM FASVLPALLV FILIFLESQI TTLIVSKPER KMIKGSGFHL
     DLLLVVGMGG VAALFGMPWL SATTVRSVTH ANALTVMGKA SGPGAAAQIQ EVKEQRISGL
     LVSVLVGLSI LMEPILSRIP LAVLFGIFLY MGITSLSGIQ LFDRILLLFK PPKYHPDVPF
     VKRVKTWRMH LFTGIQIICL AVLWVVKSTP ASLALPFVLI LTVPLRRLLL PLIFRELELQ
     CLDGDDAKVT FDEAEGLDEY DEVPMPV
//