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Database: UniProt
Entry: A0A1V4JQX6_PATFA
LinkDB: A0A1V4JQX6_PATFA
Original site: A0A1V4JQX6_PATFA 
ID   A0A1V4JQX6_PATFA        Unreviewed;       947 AA.
AC   A0A1V4JQX6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A1 {ECO:0000313|EMBL:OPJ74616.1};
GN   ORFNames=AV530_001447 {ECO:0000313|EMBL:OPJ74616.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ74616.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ74616.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ74616.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ74616.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ74616.1}.
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DR   EMBL; LSYS01006700; OPJ74616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4JQX6; -.
DR   STRING; 372326.A0A1V4JQX6; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002977; Anion_exchange_1.
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:SF12; BAND 3 ANION TRANSPORT PROTEIN; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01187; ANIONEXHNGR1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE   3: Inferred from homology;
KW   Anion exchange {ECO:0000256|ARBA:ARBA00022681};
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:UP000190648};
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        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        478..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        529..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        561..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        607..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        695..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        737..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        822..846
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        867..886
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        892..910
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          120..364
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          415..593
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   DOMAIN          602..874
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  105511 MW;  50579E7608BE1159 CRC64;
     MDQQSTVPSL DGPPRQQRAE PGQGRPGATP GEAYEERMRR SLDPEGFEDP GIKGSHLSLG
     EMSTPSVTDV DLEAAGSRRS AYPRATHEGY VELHELVMDS NKELCWMEAG HWLKLEEDFK
     ETGYWGQPHL SFLTYRSLLE IRRALAKGAV LFDVAATSLA AIAHVLIDQM IYEGQIKPHD
     REDILRTLLL QHKHPSEAEA VGPLRPAQLQ RSGTAGAETE QPLLREQQPL EMRGLVGAGQ
     GVSGAARPQL PEKVPEDAEA TLVLVGCAAF LEQPTLAFVR LKAAVTLDAV LDVPLPVRFL
     LVVLGPDTPH ISYHEIGRAV ATMMSERVFR RDAYLAEGRQ DLLRGVDDFL EASIVLPPTE
     TPSEQQLRSL VPLQHELLRR RYQPPEKAPG EGFLKDLGLE EPAPEDDDPL RRTGRPFGGL
     VRDICRRYPK YLSDIKDALN PQCLAAVIFI YFAALSPAVT FGGLLSEKTK GMMGVSELLI
     STCVQCVLFS LLSAQPLLVV GFSGPLLVFE EAFYSFCSDN DMEYIVGRVW IGFWLILLVL
     VVVAVEGSFL VRYLSRYTQE IFSFLISLIF IFETFSKLVT IFRDHPLKRY YDVQPTVQPK
     VPEPNTALLS LVLMGGTFFL AFFLRKFKNS AFLPGKVRRL IGDFGVPISI FIMALVDFFI
     KDTYTQKLNV PRGLEVTNAS ARGWFINPMG LNAPFPIWMM FACVVPAVLV FILIFLETQI
     TTLIVSKPER KLVKGSGFHL DLLLIVAMGG LAALFGMPWL SATTVRTITH ANALTVMSKA
     TAAGEKSQIL EVKEQRISGL LVAMLIGVSI LMEPILKYIP LAVLFGIFLY MGVTSLFGIQ
     LFDRILLLLM PPKYHPSEPY VTRVKTWRMH LFTFTQIVVL VLLWVVKSTP ASLALPFLLI
     LTVPLRRFLL PKIFRDIELK CLDADDAVVT FEEAEGTDVY NEVQMPS
//
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