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   03-AUG-2022, entry version 126.
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].
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   -!- 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}. 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.
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.ENSGALP00000041211; -.
DR   GeneID; 396532; -.
DR   KEGG; gga:396532; -.
DR   CTD; 6521; -.
DR   VEuPathDB; HostDB:geneid_396532; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   InParanoid; P15575; -.
DR   OrthoDB; 265068at2759; -.
DR   PhylomeDB; P15575; -.
DR   PRO; PR:P15575; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR   GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
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; 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