B3A3_PLEMO
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 25-MAY-2022, entry version 46.
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: Plasma membrane anion exchange protein of wide distribution.
CC Mediates at least a part of the Cl(-)/HCO3(-) exchange in cardiac
CC myocytes. Both BAE3 and CAE3 forms transport Cl(-) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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: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; 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 PANTHER; PTHR11453; PTHR11453; 1.
DR PANTHER; PTHR11453:SF15; PTHR11453:SF15; 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; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 3: Inferred from homology;
KW Anion exchange; Antiport; Ion transport; Lipoprotein; Membrane;
KW Methylation; Palmitate; Phosphoprotein; Transmembrane; Transmembrane helix;
KW 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
