ID F6V957_CALJA Unreviewed; 1241 AA.
AC F6V957;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A3 {ECO:0000313|Ensembl:ENSCJAP00000042135.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000042135.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000042135.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000042135.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00034408};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362035}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F6V957; -.
DR Ensembl; ENSCJAT00000061354.4; ENSCJAP00000042135.4; ENSCJAG00000011943.5.
DR GeneTree; ENSGT00940000159765; -.
DR OMA; HKLWRPP; -.
DR Proteomes; UP000008225; Chromosome 6.
DR Bgee; ENSCJAG00000011943; Expressed in heart and 5 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IEA:Ensembl.
DR GO; GO:0061337; P:cardiac conduction; IEA:Ensembl.
DR GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IEA:Ensembl.
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 {ECO:0000256|ARBA:ARBA00022681};
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362035};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362035};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}.
FT TRANSMEM 709..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 743..774
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 794..819
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 826..844
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 893..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 930..947
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 984..1002
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1023..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1083..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1109..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 350..618
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 681..1161
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
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 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"
SQ SEQUENCE 1241 AA; 136833 MW; DA6DF3337C5408F6 CRC64;
MANGVIPPPG GASPLPQVRV PLEEPPLSPD VEEEDDDLGK TLAVSRFGDL ISKPPAWDPE
KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRLPP TSARHNRRKR KKEKTSAPPS
EETPPIQEEG GAGVDEEEEE EEEEEGESEA EPGEPPPSGS PPKAKFSIGS DEDDSPGLPG
RAAITKPLPS VGPHIDRSPQ HSGSSPSPRA 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
LELGGPEATP EDDPLLRTGS IFGGLVRDVR RRYPHYPSDL RDALHSQCVA AVLFIYFAAL
SPAITFGGLL GEKTEGLMGV SELIVSTAVL GVLFSLLGAQ PLLVVGFSGP LLVFEEAFFK
FCRAQDLEYL TGRVWVGLWL VVFVLVLVAA 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 PEMGRSGTVL C
//
