ID   B3AT_ONCMY              Reviewed;         918 AA.
AC   P32847;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Band 3 anion exchange protein;
DE   AltName: Full=Anion exchange protein 1;
DE            Short=AE 1;
DE            Short=Anion exchanger 1;
DE   AltName: Full=Solute carrier family 4 member 1;
GN   Name=slc4a1; Synonyms=ae1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1637296; DOI=10.1042/bj2850017;
RA   Hubner S., Michel F., Rudloff V., Appelhans H.;
RT   "Amino acid sequence of band-3 protein from rainbow trout erythrocytes
RT   derived from cDNA.";
RL   Biochem. J. 285:17-23(1992).
CC   -!- FUNCTION: Functions both as a transporter that mediates electroneutral
CC       anion exchange across the cell membrane and as a structural protein.
CC       Major integral membrane glycoprotein 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, it spans the membrane asymmetrically and
CC       appears to be tetrameric. {ECO:0000250|UniProtKB:P02730}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P02730};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
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DR   EMBL; X61699; CAA43868.1; -; mRNA.
DR   PIR; S24318; S24318.
DR   RefSeq; NP_001118189.1; NM_001124717.1.
DR   AlphaFoldDB; P32847; -.
DR   SMR; P32847; -.
DR   TCDB; 2.A.31.1.4; the anion exchanger (ae) family.
DR   GlyCosmos; P32847; 2 sites, No reported glycans.
DR   GeneID; 100136769; -.
DR   KEGG; omy:100136769; -.
DR   OrthoDB; 1013180at2759; -.
DR   Proteomes; UP000694395; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; ISS:UniProtKB.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; ISS:UniProtKB.
DR   GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
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; 2.
DR   Pfam; PF00955; HCO3_cotransp; 1.
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   2: Evidence at transcript level;
KW   Anion exchange; Cell membrane; Glycoprotein; Ion transport; Lipoprotein;
KW   Membrane; Palmitate; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..918
FT                   /note="Band 3 anion exchange protein"
FT                   /id="PRO_0000079213"
FT   TOPO_DOM        1..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        393..416
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        417..424
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        425..445
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        446..448
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        449..465
FT                   /note="Discontinuously helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        466..474
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        475..495
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        496..507
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        508..530
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        531..583
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        584..604
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        605..615
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        616..636
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        637..676
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        677..697
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        698..713
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        714..732
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        733..750
FT                   /note="Discontinuously helical; Name=10"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        751..769
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        770..790
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TRANSMEM        791..809
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        810..847
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   INTRAMEM        848..878
FT                   /note="Discontinuously helical"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   TOPO_DOM        879..918
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02730"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           852
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   918 AA;  101894 MW;  37E163141FBDC16A CRC64;
     MENDLSFGED VMSYEEESDS AFPSPIRPTP PGHSGNYDLE QSRQEEDSNQ AIQSIVVHTD
     PEAYLNLNTN ANTRGDAQAY VELNELMGNS WQETGRWVGY EENFNPGTGK WGPSHVSYLT
     FKSLIQLRKI MSTGAIILDL QASSLSAVAE KVVDELRTKG EIRAADRDGL LRALLQRRSQ
     SEGAVAQPLG GDIEMQTFSV TKQRDTTDSV EASIVLSGVM DSLEKPAVAF VRLGDSVVIE
     GALEAPVPVR FVFVLVGPSQ GGVDYHESGR AMAALMADWV FSLEAYLAPT NKELTNAIAD
     FMDCGIVIPP TEIQDEGMLQ PIIDFQKKML KDRLRPSDTR IIFGGGAKAD EADEEPREDP
     LARTGIPFGG MIKDMKRRYR HYISDFTDAL DPQVLAAVIF IYFAALSPAI TFGGLLADKT
     EHMMGVSELM ISTCVQGIIF AFIAAQPTLV IGFSGPLLVF EEAFFAFCKS QEIEYIVGRI
     WVGLWLVIIV VVIVAVEGSF LVKFISRFTQ EIFSILISLI FIYETFSKLG KIFKAHPLVL
     NYEHLNDSLD NPFHPVVKEH IEYHEDGNKT VHEVIHERAY PNTALLSMCL MFGCFFIAYF
     LRQFKNGHFL PGPIRRMIGD FGVPIAIFFM IAVDITIEDA YTQKLVVPKG LMVSNPNARG
     WFINPLGEKK PFPAWMMGAC CVPALLVFIL IFLESQITTL IVSKPERKMV KGSGFHLDLL
     ILVTMGGIAS LFGVPWLSAA TVRSVTHANA LTVMSKGPKP EIEKVLEQRI SGMLVAAMVG
     VSILLEPILK MIPMTALFGI FLYMGITSLS GIQMWDRMLL LIVPRKYYPA DAYAQRVTTM
     KMHLFTLIQM VCLGALWMVK MSAFSLALPF VLILTIPLRM AITGTLFTDK EMKCLDASDG
     KVKFEEEPGE DMYESPLP
//