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Database: UniProt
Entry: A0A0Q3TQV5_AMAAE
LinkDB: A0A0Q3TQV5_AMAAE
Original site: A0A0Q3TQV5_AMAAE 
ID   A0A0Q3TQV5_AMAAE        Unreviewed;      1155 AA.
AC   A0A0Q3TQV5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   ORFNames=AAES_68587 {ECO:0000313|EMBL:KQK82942.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK82942.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK82942.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK82942.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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: Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004554}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034693}. 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:KQK82942.1}.
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DR   EMBL; LMAW01001669; KQK82942.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3TQV5; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016328; C:lateral 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; 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:SF14; ANION EXCHANGE PROTEIN 2; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; 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:UP000051836};
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        662..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        704..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        747..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        845..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        905..924
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        944..965
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1005..1024
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1030..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          300..573
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          633..873
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   DOMAIN          874..1082
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1155 AA;  129136 MW;  0F6ED284FFB9378F CRC64;
     MTHSQVSSEI HHIVSSAFQS PEQEALGXGS PVFGEEEEEK DLNKALGVER FEEILCDAHP
     RNAEEAGRSY GEEDFEYHRQ SSHHIHHPLS THLPPDTRRK KGVPKKFFLQ EDEVTEHRAE
     DPVAPPVLPG SPPNPRESTS PKEAQAGSPS AEEGGAVEGA AASAXAGSPG RPVPKSQPGH
     RSYNLHERRR IGSMTGAEQD RYQKMPTDES EAQTLASADL DYMKSHRFED VPGVRRHLVR
     KSAKAQVVHV SKDHKEPMTR HRKQDRQPHE VFVELNELVV DKNQELQWKE TARWIKFEED
     VEEETDRWGK PHVASLSFRS LLELRKTLSH GAVLLDLDQK TLPGVAHQVV EQMVITDQIR
     AEDRANVLRA LLLKHSHPSD EKDFSFPRNI SAGSLGSLLV HHHSTNHVAE GSEPAVTDPL
     IAGHAVEHDT RVDVEREREV LTPTPPAGIT RSKSKHELKL LEKIPDNAEA TVVLVGCVEF
     LDQPTMAFVR LQEAVELDSV LEVPVPVRFL FVLLGPSSTH MDYHEIGRSI STLMSDKQFH
     EAAYLADDRH DLLNAINEFL DCSVVLPPSE VQGEELLRSV AHFQREMLKK REEQERRLLL
     EPKSPEEKAL LKLKVVEGDG EEEDDDPLRR TGRPFGGLIR DVQRRYPKYL SDFRDALDPQ
     CIAAVIFIYF AALSPAITFG GLLGEKTQDL IGVSELIIST SLQGVIFCLL GAQPLLIIGF
     SGPLLVFEEA FFTFCXSNDL EYLVGRVWIG FWLILIVLVM VAFEGSFLVR FVSRFTQEIF
     AFLISLIFIY ETFSKLAKIF QEHPLHGCVQ ANVSEPEAWR NSSTXPANGT ASRAAAKVTG
     QPNTALLSLV LMASTFFIAF FLRKFKNSRF FPGRKLSVPS GFSVTAPDKR GWVINPLGEK
     SDFPVWMMVA SGLPAILVFI LIFMETQITT LIISKKERML QKGSGFHLDL LLIVAMGGFF
     ALFGLPWLAA ATVRSVTHAN ALTVMSKAVA PGDKPKIQEV KEQRVTGLLV AVLVGLSIVI
     GDLLRQIPLA VLFGIFLYMG ITSLNGIQFY ERLQLLLMPP KHHPDVTYVK KVRTLRMHLF
     TGLQLACLAV LWAVMSTVAS LAFPFILILT VPLRMCLLSR IFTDREMKCL DADEAEPILD
     EREGVDEYNE MPMPV
//
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