B3AT_RAT
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 03-AUG-2022, entry version 167.
DE RecName: Full=Band 3 anion transport 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;
DE AltName: CD_antigen=CD233;
GN Name=Slc4a1; 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.
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 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, but in its membrane environment, it
CC exists primarily as a mixture of dimers and tetramers and spans the
CC membrane asymmetrically. Interacts (via cytoplasmic N-terminal domain)
CC with ANK1 (via N-terminal ANK repeats); tetramer formation is critical
CC for ankyrin association. Interacts with STOM. Isoform 2 interacts with
CC TMEM139. {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.
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 GlyGen; P23562; 1 site.
DR iPTMnet; P23562; -.
DR PhosphoSitePlus; P23562; -.
DR PaxDb; P23562; -.
DR PeptideAtlas; P23562; -.
DR PRIDE; P23562; -.
DR GeneID; 24779; -.
DR KEGG; rno:24779; -.
DR UCSC; RGD:3710; rat. [P23562-1]
DR CTD; 6521; -.
DR RGD; 3710; Slc4a1.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; P23562; -.
DR OrthoDB; 265068at2759; -.
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: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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IPI:RGD.
DR GO; GO:0015301; F:anion:anion antiporter activity; ISS:UniProtKB.
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:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0030492; F:hemoglobin binding; ISO:RGD.
DR GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI: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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; ISS:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; ISO:RGD.
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:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; ISO:RGD.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; 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:0009414; P:response to water deprivation; IEP:RGD.
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 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
