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Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (Solute carrier family 4 member 1) (CD antigen CD233)

 B3AT_RAT                Reviewed;         927 AA.
P23562;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 3.
22-NOV-2017, entry version 149.
RecName: Full=Band 3 anion transport protein;
AltName: Full=Anion exchange protein 1;
Short=AE 1;
Short=Anion exchanger 1;
AltName: Full=Solute carrier family 4 member 1;
AltName: CD_antigen=CD233;
Name=Slc4a1; Synonyms=Ae1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-927.
TISSUE=Kidney;
PubMed=2722777;
Kudrycki K.E., Shull G.E.;
"Primary structure of the rat kidney band 3 anion exchange protein
deduced from a cDNA.";
J. Biol. Chem. 264:8185-8192(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-45.
PubMed=8456965;
Kudrycki K.E., Shull G.E.;
"Rat kidney band 3 Cl-/HCO3- exchanger mRNA is transcribed from an
alternative promoter.";
Am. J. Physiol. 264:F540-F547(1993).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-199 AND SER-222,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Functions both as a transporter that mediates
electroneutral anion exchange across the cell membrane and as a
structural protein. Major integral membrane glycoprotein of the
erythrocyte membrane; required for normal flexibility and
stability of the erythrocyte membrane and for normal erythrocyte
shape via the interactions of its cytoplasmic domain with
cytoskeletal proteins, glycolytic enzymes, and hemoglobin.
Functions as a transporter that mediates the 1:1 exchange of
inorganic anions across the erythrocyte membrane. Mediates
chloride-bicarbonate exchange in the kidney, and is required for
normal acidification of the urine. {ECO:0000250|UniProtKB:P02730}.
-!- SUBUNIT: A dimer in solution, but in its membrane environment, it
exists primarily as a mixture of dimers and tetramers and spans
the membrane asymmetrically. Interacts (via cytoplasmic N-terminal
domain) with ANK1 (via N-terminal ANK repeats); tetramer formation
is critical for ankyrin association. Interacts with STOM. Isoform
2 interacts with TMEM139. {ECO:0000250|UniProtKB:P02730}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P02730}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P02730}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P02730}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P02730}. Note=Detected in the erythrocyte
cell membrane and on the basolateral membrane of alpha-
intercalated cells in the collecting duct in the kidney.
{ECO:0000250|UniProtKB:P02730}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Erythrocyte;
IsoId=P23562-1; Sequence=Displayed;
Name=2; Synonyms=Kidney;
IsoId=P23562-2; Sequence=VSP_000455;
-!- TISSUE SPECIFICITY: Kidney.
-!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA40800.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J04793; AAA40800.1; ALT_INIT; Genomic_DNA.
EMBL; L02943; AAA40801.1; -; mRNA.
PIR; A33810; A33810.
PIR; A48854; A48854.
RefSeq; NP_036783.2; NM_012651.2.
RefSeq; XP_008766168.1; XM_008767946.2. [P23562-1]
UniGene; Rn.32202; -.
ProteinModelPortal; P23562; -.
SMR; P23562; -.
STRING; 10116.ENSRNOP00000028445; -.
iPTMnet; P23562; -.
PhosphoSitePlus; P23562; -.
PaxDb; P23562; -.
PeptideAtlas; P23562; -.
PRIDE; P23562; -.
GeneID; 24779; -.
KEGG; rno:24779; -.
UCSC; RGD:3710; rat. [P23562-1]
CTD; 6521; -.
RGD; 3710; Slc4a1.
eggNOG; KOG1172; Eukaryota.
eggNOG; ENOG410XPHD; LUCA.
HOGENOM; HOG000280683; -.
HOVERGEN; HBG004326; -.
InParanoid; P23562; -.
KO; K06573; -.
PhylomeDB; P23562; -.
PRO; PR:P23562; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0030863; C:cortical cytoskeleton; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0030018; C:Z disc; IDA:RGD.
GO; GO:0003779; F:actin binding; IPI:RGD.
GO; GO:0015301; F:anion:anion antiporter activity; ISS:UniProtKB.
GO; GO:0030506; F:ankyrin binding; ISO:RGD.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
GO; GO:0006820; P:anion transport; ISS:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:RGD.
GO; GO:0051259; P:protein oligomerization; IDA:RGD.
GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
GO; GO:0010447; P:response to acidic pH; IEP:RGD.
GO; GO:0014823; P:response to activity; IDA:RGD.
GO; GO:0010446; P:response to alkaline pH; IEP:RGD.
GO; GO:0046685; P:response to arsenic-containing substance; IDA:RGD.
GO; GO:0010037; P:response to carbon dioxide; IDA:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0009414; P:response to water deprivation; IEP:RGD.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR001717; Anion_exchange.
InterPro; IPR002977; Anion_exchange_1.
InterPro; IPR018241; Anion_exchange_CS.
InterPro; IPR013769; Band3_cytoplasmic_dom.
InterPro; IPR011531; HCO3_transpt_C.
InterPro; IPR003020; HCO3_transpt_euk.
InterPro; IPR016152; PTrfase/Anion_transptr.
PANTHER; PTHR11453; PTHR11453; 1.
Pfam; PF07565; Band_3_cyto; 1.
Pfam; PF00955; HCO3_cotransp; 2.
PRINTS; PR00165; ANIONEXCHNGR.
PRINTS; PR01187; ANIONEXHNGR1.
PRINTS; PR01231; HCO3TRNSPORT.
SUPFAM; SSF55804; SSF55804; 1.
TIGRFAMs; TIGR00834; ae; 1.
PROSITE; PS00219; ANION_EXCHANGER_1; 1.
PROSITE; PS00220; ANION_EXCHANGER_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Anion exchange; Cell membrane;
Complete proteome; Glycoprotein; Ion transport; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 927 Band 3 anion transport protein.
/FTId=PRO_0000079211.
TOPO_DOM 1 420 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 421 444 Helical; Name=1.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 445 452 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 453 473 Helical; Name=2.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 474 476 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 477 493 Discontinuously helical; Name=3.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 494 502 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 503 523 Helical; Name=4.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 524 535 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 536 558 Helical; Name=5.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 559 586 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 587 607 Helical; Name=6.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 608 618 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 619 639 Helical; Name=7.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 640 679 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 680 700 Helical; Name=8.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 701 716 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 717 735 Helical; Name=9.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 736 753 Discontinuously helical; Name=10.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 754 776 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 777 797 Helical; Name=11.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 798 816 Helical; Name=12.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 817 854 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
INTRAMEM 855 885 Discontinuously helical.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 886 927 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
REGION 69 303 Globular. {ECO:0000250}.
REGION 190 199 Interaction with ANK1. {ECO:0000250}.
REGION 317 370 Dimerization arm. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 31 31 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 56 56 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 920 920 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
LIPID 859 859 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 658 658 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
VAR_SEQ 1 79 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000455.
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


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