B3A4_RABIT
ID B3A4_RABIT Reviewed; 955 AA.
AC Q9GKY1; Q9GKY2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 25-MAY-2022, entry version 106.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=11102437; DOI=10.1074/jbc.m004513200;
RA Tsuganezawa H., Kobayashi K., Iyori M., Araki T., Koizumi A., Watanabe S.,
RA Kaneko A., Fukao T., Monkawa T., Yoshida T., Kim D.K., Kanai Y., Endou H.,
RA Hayashi M., Saruta T.;
RT "A new member of the HCO3-transporter superfamily is an apical anion
RT exchanger of beta-intercalated cells in the kidney.";
RL J. Biol. Chem. 276:8180-8189(2001).
CC -!- FUNCTION: Probable apical anion exchanger of the beta-intercalated
CC cells of kidney. May participate in HCO3(-) secretion.
CC {ECO:0000269|PubMed:11102437}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane
CC protein. Note=In contrast to the rat ortholog, it is present on apical
CC membrane of cortical kidney cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AE4a;
CC IsoId=Q9GKY1-1; Sequence=Displayed;
CC Name=2; Synonyms=AE4b;
CC IsoId=Q9GKY1-2; Sequence=VSP_007088;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Expressed in certain
CC types of cells in the kidney cortex.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AB038263; BAB18935.1; -; mRNA.
DR EMBL; AB038264; BAB18936.1; -; mRNA.
DR RefSeq; NP_001075474.1; NM_001082005.1. [Q9GKY1-1]
DR AlphaFoldDB; Q9GKY1; -.
DR SMR; Q9GKY1; -.
DR STRING; 9986.ENSOCUP00000013683; -.
DR TCDB; 2.A.31.2.5; the anion exchanger (ae) family.
DR PRIDE; Q9GKY1; -.
DR GeneID; 100008621; -.
DR KEGG; ocu:100008621; -.
DR CTD; 83697; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q9GKY1; -.
DR OrthoDB; 265068at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
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 Alternative splicing; Anion exchange; Antiport; Cell membrane;
KW Disulfide bond; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..955
FT /note="Anion exchange protein 4"
FT /id="PRO_0000079224"
FT TOPO_DOM 1..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..595
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 871..891
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..955
FT /note="Membrane (anion exchange)"
FT REGION 918..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 538..540
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 581..593
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 317..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11102437"
FT /id="VSP_007088"
SQ SEQUENCE 955 AA; 105033 MW; 04E595A2BFC415B7 CRC64;
MKLPGQEELE AACACENVPV GQLDSGPSSG PCPDDPSDTG SRELGPPEDP PLFLQLNELL
GWPQTLEWRE MGRWVLFEEK LEVDAGRWSA PHVPTLALPS LQNLRSLLAE GLVLLDCPAQ
NLLELVEQVT RVESLSPELR GQLQALLLQR PQHHTQTTGS RPCWGPAQSR KAAHNKEAPM
QQQCQSPLRQ KLPPGAEAGA VLAGELGFLA QPLAAFVRLR DPVWLGPLTE VPLPSRFFCL
LLGPPMLGKG YHELGRAAAV LLSDPHFQWS VRRASNLHDL LTALDAFLEE VTVLPPGRWD
PTARIPPPRC LPSRHKRPPL HLQKVKGLSV PHRTQAEDRH RNGPLAPSPE LQRTGRLFGG
LVQDVRRKAS WYPSDFSDAL HPQCVSAVLY IYLATVTNAI TFGGLLGDAT DGAQGVLESL
LGTAVAGAAF CLMAGQPLTV LSSTGPVLVF ERLLFAFCRD YSLDYLPFRL WVGIWVAVFC
LALVATEASV LVRYFTRFTE EGFCALISLI FIYDAVGKML NLAHAYPIQR PGSLAYGCLC
QFPGPGGNES QWTRPRPQSR DDLLSVDLGL VNASLLPPHE CVQQGGYPRG PGCHTVPDIA
FFSLLLFLTS FLFAIALKHM KTSRFFPSVV RKVLSDFSSI LAILLGCGLD ALLGLAMPKL
MVPREFKPTL PGRGWLVPPF GANPWWLSVA AALPALLLSI LIFMDQQITA VILNRVEYRL
RKGAGFHLDL FCVALLMLLT SVLGLPWYVS ATVLSLAHMD SLRRESRACA PGEPHSFLGI
REQRLTGLAV FTLTGVSIFL APVLKFIPMP VLYGIFLYMG VAALSSIQFM KRVQLMLMPA
KHQPDLLLLR HVPLSRVHLF TAIQLACLGL LWIIKSTPAA IIFPLMLLGL VGVRKALEWV
FSPQELLWLD ELMPEEERNV PEKGLEPGHS FSGSDSEDSE LMYQPKAPEI NISVN
