ID A0A2K6N3X0_RHIBE Unreviewed; 1233 AA.
AC A0A2K6N3X0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A3 {ECO:0000313|Ensembl:ENSRBIP00000042713.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000042713.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000042713.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000042713.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A2K6N3X0; -.
DR STRING; 61621.ENSRBIP00000042713; -.
DR Ensembl; ENSRBIT00000066756.1; ENSRBIP00000042713.1; ENSRBIG00000044594.1.
DR GeneTree; ENSGT00940000159765; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0022853; F:active monoatomic ion transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR GO; GO:0061337; P:cardiac conduction; IEA:Ensembl.
DR GO; GO:0098660; P:inorganic ion transmembrane transport; IEA:UniProt.
DR GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; 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:UP000233180};
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 710..732
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 744..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 795..820
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 827..845
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 894..911
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 931..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 985..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1024..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1084..1103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1110..1134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 351..619
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 682..1162
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 39..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1233 AA; 136128 MW; 60FD5D7474D758BD CRC64;
VLSRGCLGLQ VRVPLEEPPL SPDVEEEDDD LGKTLAVSRF GDLISKPPAW DPEKPSRSYS
ERDFEFHRHT SHHTHHPLSA RLPPPHKLRR LPPTSARHTR RKRKKEKTSA PPSEGTPPIQ
EEGGAGVDEE EEEEEEEEGE SEAEPVEPPP SGTPQKAKFS IGSDEDDSPG LSGRAAVTKP
LPSVGPRTDK SPQHSSSRAQ PRATDSPSPR ARASRLAGEK SRPWSPSASY DLRERLCPGS
ALGNPGGPEQ QVPTDEAEAQ MLGSADLDDM KSHRLEDNPG VRRHLVKKPS RTQGGRGSPS
GLAPILRRKK KKKKLDRRPH EVFVELNELM LDRSQEPHWR ETARWIKFEE DVEEETERWG
KPHVASLSFR SLLELRRTIA HGAALLDLEQ TTLPGIAHLV VETMIVSDQI RPEDRASVLR
TLLLKHSHPN DDKDSGFFPR NPSSSSMNSV LGNHHPTPSH GPDGAVPTMA DDLGEPAPLW
PHDPDAKEKP LHMPGGDGHR GKSLKLLEKI PEDAEATVVL VGCVPFLEQP AAAFVRLNEA
VLLESVLEVP VPVRFLFVML GPSHTSTDYH ELGRSIATLM SDKLFHEAAY QADDRQDLLS
AISEFLDGSI VIPPSEVEGR DLLRSVAAFQ RELLRKRRER EQTKVEMTTR GGYTAPGKEL
SLELGGSETT PEDDPLLRTG SVFGGLVRDV RRRYPHYPSD LRDALHSQCV AAVLFIYFAA
LSPAITFGGL LGEKTEGLMG VSELIVSTAV LGVLFSLLGA QPLLVVGFSG PLLVFEEAFF
KFCRAQDLEY LTGRVWVGLW LVVFVLALVA AEGSFLVRYI SPFTQEIFAF LISLIFIYET
FYKLYKVFTE HPLLPFYPPE GALEGSLDAG LEPNGSALPP TEGPPSPRNQ PNTALLSLIL
MLGTFFIAFF LRKFRNSRFL GGKARRIIGD FGIPISILVM VLVDYSITDT YTQKLTVPTG
LSVTSPDKRS WFIPPLGSAR PFPPWMMVAA AVPALLVLIL IFMETQITAL IVSQKARRLL
KGSGFHLDLL LIGSLGGLCG LFGLPWLTAA TVRSVTHVNA LTVMRTAIAP GDKPQIQEVR
EQRVTGVLIA SLVGLSIVMG AVLRRIPLAV LFGIFLYMGV TSLSGIQLSQ RLLLILMPAK
HHPEQPYVTK VKTWRMHLFT CIQLGCIALL WVVKSTAASL AFPFLLLLTV PLRHCLLPRL
FQDRELQALD SEDAEPNFDE DGQDEYNELH MPV
//
