ID B3AT_CHICK Reviewed; 922 AA.
AC P15575;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=Band 3 anion transport protein;
DE AltName: Full=Solute carrier family 4 member 1;
GN Name=SLC4A1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=3185555; DOI=10.1128/mcb.8.10.4416-4424.1988;
RA Kim H.R.C., Yew N.S., Ansorge W., Voss H., Schwager C., Vennstroem B.,
RA Zenke M., Engel J.D.;
RT "Two different mRNAs are transcribed from a single genomic locus encoding
RT the chicken erythrocyte anion transport proteins (band 3).";
RL Mol. Cell. Biol. 8:4416-4424(1988).
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}. 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 -!- TISSUE SPECIFICITY: Erythrocytes. {ECO:0000269|PubMed:3185555}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; M23404; AAA48753.1; -; mRNA.
DR PIR; A30816; A30816.
DR RefSeq; NP_001277483.1; NM_001290554.1.
DR AlphaFoldDB; P15575; -.
DR SMR; P15575; -.
DR STRING; 9031.ENSGALP00000045469; -.
DR GlyCosmos; P15575; 1 site, No reported glycans.
DR PaxDb; 9031-ENSGALP00000041211; -.
DR GeneID; 396532; -.
DR KEGG; gga:396532; -.
DR CTD; 6521; -.
DR VEuPathDB; HostDB:geneid_396532; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; P15575; -.
DR PhylomeDB; P15575; -.
DR PRO; PR:P15575; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
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 GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
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; 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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..922
FT /note="Band 3 anion transport protein"
FT /id="PRO_0000079212"
FT TOPO_DOM 1..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 417..440
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 441..448
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 449..469
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 470..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 473..489
FT /note="Discontinuously helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 490..498
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 499..519
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 520..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 532..554
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 555..581
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 582..602
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 603..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 614..634
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 635..674
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 675..695
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 696..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 712..730
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 731..748
FT /note="Discontinuously helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 749..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 772..792
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 793..811
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 812..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT INTRAMEM 850..880
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 881..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 102223 MW; FF4ECAD6D60CF0CF CRC64;
MEGPGQDTED ALRRSLDPEG YEDTKGSRTS LGTMSNPLVS DVDLEAAGSR QPTAHRDTYE
GYVELHELVL DSRKDPCWME AGRWLHLEES MEPGGAWGSH LPLLTYHSLL ELHRAFAKGV
VLLDVAANSL AAVAHVLLDQ LIYEGQLKPQ HRDDVLRALL LRHKHPSEAE SVWTLPAAQL
QCSDGEQKDA DERALLRDQR AVEMRELHGA GQSPSRAQLG PQLHQQLPED TEATLVLVAC
AAFLEQPLLA LVRLGAPCPD AVLAVPLPVR FVLTVLGPDS PRLSYHEIRR AAATVMADRV
FRRDAYLCGG RAELLGGLQG FLEASIVLPP QEVPSEQHLH ALIPLQRHAV RRRYQHPDTV
RSPGGPTAPK DTGDKGQAPQ DDDPLLRTRR PFGGLVRDIR RRYPKYLSDI RDALNPQCLA
AVIFIYFAAL SPAITFGGLL GEKTRGMMGV SELLLSTSVQ CLLFSLLSAQ PLLVVGFSGP
LLVFEEAFFR FCEDHGLEYI VGRVWIGFWL ILLVLLVVAC EGTVLVRYLS RYTQEIFSFL
ISLIFIYETF AKLVTIFEAH PLQQSYDTDV STEPSVPKPN TALLSLVLMA GTFFLALFLR
QFKNSVFLPG KVRRLIGDFG VPISIFVMAL ADFFIKDTYT QKLKVPRGLE VTNGTARGWF
IHPMGSATPF PIWMMFASPV PALLVFILIF LETQITTLIV SKPERKLVKG SGFHLDLLLI
VAMGGLAALF GMPWLSATTV RTITHANALT VVGKSAVPGE RAHIVEVKEQ RLSGLLVAVL
IGVSILMEPI LKYIPLAVLF GIFLYMGVTS LFGIQLFDRI LLLLMPPKYH PKEPYVTRVK
TWRITSSPLT QILVVALLWG VKVSPASLRC PFVLVLTVPL RRLLLPRIFS EIELKCLDTD
DAVVTFEEAE GQDVYNEVQM PS
//
