B3A4_RAT
ID B3A4_RAT Reviewed; 953 AA.
AC Q8K4V2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Anion exchange protein 4;
DE Short=AE 4;
DE Short=Anion exchanger 4;
DE AltName: Full=Solute carrier family 4 member 9;
GN Name=Slc4a9; Synonyms=Ae4;
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 [MRNA], FUNCTION, AND CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=12225984; DOI=10.1152/ajpcell.00512.2001;
RA Ko S.B.H., Luo X., Hager H., Rojek A., Choi J.Y., Licht C., Suzuki M.,
RA Muallem S., Nielsen S., Ishibashi K.;
RT "AE4 is a DIDS-sensitive Cl(-)/HCO(-)(3) exchanger in the basolateral
RT membrane of the renal CCD and the SMG duct.";
RL Am. J. Physiol. 283:C1206-C1218(2002).
CC -!- FUNCTION: Probable apical anion exchanger of the alpha-intercalated
CC cells of kidney. May participate in HCO3(-) absorption.
CC {ECO:0000269|PubMed:12225984}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Note=In contrast to the rabbit ortholog, it is present on
CC basolateral membrane of cortical collecting duct kidney cells.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and gastrointestinal tract. In
CC kidney, it is highly expressed in the cortex, expressed at intermediate
CC level in the outer medulla and not expressed in the inner medulla. It
CC is expressed in the cecum, while it is absent in other segments of
CC gastrointestinal tract.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AB024339; BAC10662.1; -; mRNA.
DR RefSeq; NP_690921.1; NM_152938.1.
DR AlphaFoldDB; Q8K4V2; -.
DR SMR; Q8K4V2; -.
DR STRING; 10116.ENSRNOP00000025137; -.
DR GlyGen; Q8K4V2; 2 sites.
DR iPTMnet; Q8K4V2; -.
DR PhosphoSitePlus; Q8K4V2; -.
DR PaxDb; Q8K4V2; -.
DR GeneID; 266612; -.
DR KEGG; rno:266612; -.
DR UCSC; RGD:628811; rat.
DR CTD; 83697; -.
DR RGD; 628811; Slc4a9.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q8K4V2; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q8K4V2; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR PRO; PR:Q8K4V2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA:RGD.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IDA:RGD.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
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; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
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; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW Anion exchange; Antiport; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..953
FT /note="Anion exchange protein 4"
FT /id="PRO_0000079225"
FT TOPO_DOM 1..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 20..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..953
FT /note="Membrane (anion exchange)"
FT REGION 916..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 536..538
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 579..591
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
SQ SEQUENCE 953 AA; 105320 MW; 625A98A969821F85 CRC64;
MKLPGQEDFE GSDAHENVCS EQLDGDLGPG SGLDGPSDID NGKAQGCKDP LLFIQLNELL
GWPQALEWRE TGRWLLFEEK LDIGAGRWSA PHVPTLALPS LQKLRGLLAE GIVLLDCPAR
SLLELVEQVV RVESLSPELR GQLQALLLQR PQHHIQTTGI RPCRRSNAFR KASRDEDTLL
KHQNPLRQKL PPGAEAAAVL AGELGFLEQP LAAFVRLQNP VVLEPLTEVV LPSRFFCLLL
GPSTLGRSYH ETGRAAAVLL SDPQFQWSVR RASNLHDLLA ALDAFLQEVT ALPPGRWDRT
ARIPPPKCLP SQHKRFPSKL QEVTSLSRQS AALAENKHHH GPHTPIPELQ RTGRLFGGLV
QDVRRKACWY PSDFLDALHP QCFSAVLYIY LATVTNAITF GGLLGDATEG AQGVLESFLG
TAVAGATFCL MAGQPLTILS STGPVLVFER LLFSFSRDYS LDYLPFRLWV GIWVATFCLA
LVATEASLLV RYFTRFTEEG FCALISLIFI YDAVGKMLNL IRAYPIQRPG SPAYSCFCQY
PGTGGNASEF DSTMFKDTED VLNVHPGLVN ASFLPPSECI RQGGYPRGPS CHTVPDIAFF
SLLLFFTSFL CAIALKHVKN SRLFPSVVRK VFSDFSSVLA ILLGCGLDAF LGLATPKLLV
PTEFKPTLPG RGWLVSPFGA NPWWLSVAAA LPALLLSILI FMDQQITAVI LNRAEYRLQK
GAGFHLDLFC VAVLMLFTSA LGLPWYVSAT VISLAHMDSL RRESKACVPG EDPNFLGIRE
QRLTGLVVFI LTGVSIFLAP VLKFIPMPVL YGIFLYMGVA ALSSMQFMKR VQLLLMPRKH
QPDVLLLRHV PLIRVHLFTA IQLACLGLLW VIKSTPAAIV FPLMLLGLVA VRKALEWIFS
PQELLWLDEL MPEEEKTIPE NRPEPEHLFS GNDSENSELM YQPKAPEINI SVN
