B3AT_ONCMY
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 25-MAY-2022, entry version 107.
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 -!- SUBUNIT: A dimer in solution, it spans the membrane asymmetrically and
CC appears to be tetrameric. {ECO:0000250}.
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 GeneID; 100136769; -.
DR KEGG; omy:100136769; -.
DR OrthoDB; 265068at2759; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR Gene3D; 3.40.930.10; -; 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 PANTHER; PTHR11453; PTHR11453; 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; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 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
