ID   B3A3_PLEMO              Reviewed;        1232 AA.
AC   B1MTL0;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   13-SEP-2023, entry version 51.
DE   RecName: Full=Anion exchange protein 3;
DE            Short=AE 3;
DE            Short=Anion exchanger 3;
DE   AltName: Full=Solute carrier family 4 member 3;
GN   Name=SLC4A3;
OS   Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC   Pitheciidae; Callicebinae; Plecturocebus.
OX   NCBI_TaxID=9523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA   Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA   Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA   Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA   Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA   Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA   Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA   Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA   Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA   Tsipouri V., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sodium-independent anion exchanger which mediates the
CC       electroneutral exchange of chloride for bicarbonate ions across the
CC       cell membrane. May be involved in the regulation of intracellular pH,
CC       and the modulation of cardiac action potential.
CC       {ECO:0000250|UniProtKB:P48751}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC         hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P16283};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16283};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
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DR   EMBL; DP000640; ACA64872.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1MTL0; -.
DR   SMR; B1MTL0; -.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; ISS:UniProtKB.
DR   GO; GO:0045851; P:pH reduction; ISS:UniProtKB.
DR   GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISS:UniProtKB.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002979; Anion_exchange_3.
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   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF15; ANION EXCHANGE PROTEIN 3; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01189; ANIONEXHNGR3.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE   3: Inferred from homology;
KW   Anion exchange; Antiport; Cell membrane; Ion transport; Lipoprotein;
KW   Membrane; Methylation; Palmitate; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1232
FT                   /note="Anion exchange protein 3"
FT                   /id="PRO_0000385514"
FT   TOPO_DOM        1..708
FT                   /note="Cytoplasmic"
FT   TRANSMEM        709..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        737..774
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        794..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        826..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        893..910
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        911..925
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        926..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        980..1002
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1028..1049
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1083..1128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1155..1191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..1232
FT                   /note="Membrane (anion exchange)"
FT   COMPBIAS        9..23
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..113
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..151
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16283"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16283"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23348"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16283"
FT   MOD_RES         295
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P16283"
FT   LIPID           1165
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1232 AA;  135882 MW;  28A41DF3201753AC CRC64;
     MANGVIPPPG GASPLPQVRV PLEEPPLSPD VEEEDDDLGK TLAVSRFGDL ISKPPAWDPE
     KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRLPP TSGRHTRRKR KKEKTSVPPS
     EGTPPIQEEG GAGVDEEEEE EEEEEGESEA EPVEPPPSGS PPKAKFSIGS DEDDSPGLPG
     RAAVTKPLPS VGPRTDKSPQ HSGSFPSPRA RASRLAGEKS RPWSPSASYD LRERLCPGSA
     LGNPGGPEQQ VPTDEAEAQM LGSADLDDMK SHRLEDNPGV RRHLVKKPSR TQGGRGSPSG
     LAPILRRKKK KKKLDRRPHE VFVELNELML DRSQEPHWRE TARWIKFEED VEEETERWGK
     PHVASLSFRS LLELRRTIAH GAALLDLEQT TLPGIAHLVV ETMIVSDQIR PEDRASVLRT
     LLLKHSHPND DKDSGFFPRN PSSSSMNSVL GNHHPTPSHG PDGAVPTMAD DLGEPAPLWP
     HDPDAKEKPL HMPGGDSHRG KSLKLLEKIP EDAEATVVLV GCVPFLEQPA AAFVRLNEAV
     LLESVLEVPV PVRFLFVMLG PSHTSTDYHE LGRSIATLMS DKLFHEAAYQ ADDRQDLLSA
     ISEFLDGSIV IPPSEVEGRD LLRSVAAFQR ELLRKRRERE QTKVEMTTRG GYTAPGKELS
     LELGGSEATP EDDPLLRTGS IFGGLVRDVR RRYPYYPSDL RDALHSQCVA AVLFIYFAAL
     SPAITFGGLL GEKTEGLMGV SELIVSTAVL GVLFSLLGAQ PLLVVGFSGP LLVFEEAFFK
     FCRAQDLEYL TGRVWVGLWL VVFVLALVAA EGSFLVRYIS PFTQEIFAFL ISLIFIYETF
     YKLYKVFTEH PLLPFYPPEG ALEGSLEAGL EPNGSALPPT EGPRGPRNQP NTALLSLILM
     LGTFFIAFFL RKFRNSRFLG GKARRIIGDF GIPISILVMV LVDYSITDTY TQKLTVPTGL
     SVTSPDKRSW FIPPLGSARP FPPWMMVAAA VPALLVLILI FMETQITALI VSQKARRLLK
     GSGFHLDLLL IGSLGGLCGL FGLPWLTAAT VRSVTHVNAL TVMRTAIAPG DKPQIQEVRE
     QRVTGVLIAS LVGLSIVMGA VLRRIPLAVL FGIFLYMGVT SLSGIQLSQR LLLILMPAKH
     HPEQPYVTKV KTWRMHLFTC IQLGCIALLW VVKSTAASLA FPFLLLLTVP LRHCLLPRLF
     QDRELQALDS EDAEPNFDED GQDEYNELHM PV
//