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Database: UniProt
Entry: A0A3Q1JRB9_ANATE
LinkDB: A0A3Q1JRB9_ANATE
Original site: A0A3Q1JRB9_ANATE 
ID   A0A3Q1JRB9_ANATE        Unreviewed;       920 AA.
AC   A0A3Q1JRB9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000033548.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000033548.2}
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}.
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DR   AlphaFoldDB; A0A3Q1JRB9; -.
DR   STRING; 64144.ENSATEP00000033548; -.
DR   Ensembl; ENSATET00000034037.2; ENSATEP00000033548.2; ENSATEG00000023071.2.
DR   GeneTree; ENSGT00940000157423; -.
DR   InParanoid; A0A3Q1JRB9; -.
DR   Proteomes; UP000265040; Unplaced.
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   GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR   GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
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:SF12; BAND 3 ANION TRANSPORT PROTEIN; 1.
DR   Pfam; PF07565; Band_3_cyto; 2.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR00165; ANIONEXCHNGR.
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   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:UP000265040};
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        395..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        439..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        481..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        513..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        585..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        618..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        675..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        715..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        771..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        797..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        841..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        867..883
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          109..182
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          208..315
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          368..849
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  103100 MW;  CD378CC150C1952C CRC64;
     MENNFTFEQD SDMSYEDNDT AFPSPLRLTP PDQANNYDLE GGREEEDEEN ERPLEAIVIP
     SNSDAYLNQN TNATTRGDAQ AYVELNELQV GVWQETGRWV GFEENFNPTA GTWSPSHVSY
     LTFKSLIQLR KLMSTAAVIL DMNAGSLSSV AEKIADELTS KNAILANEHE ELLRALLMKR
     SQSMGAVVTA GGHIHMQTYS VPKKRDNSDN IEASVVLSGI LDSLHKPAVA FVRLKDSVVM
     DSVLESSVPI RFFFVMVGPS QSGINYSECG RAMGALMADW VFSLEVFLAQ TERDVTNAIA
     DFMDCSIVIP PTEIQETSML QPIIEFQKKL LHDRLRPSDT RLAFGDRVKV EAIPPELKED
     PLARTGYPFG GMVKDIKRRY RHYFSDYIDG LNPQVLSAVI FIYFAALSPA ITFGGLLADK
     TQKMMGVSEL MVSTSVQGII FCLIAAQPVL VIGFSGPLLV FEEAFFLFCK SQGIEYIVGR
     TWVGMWLIVI VVIIVAVEGS FLVRYISRFT QEIFSILISL IFIYETFNKL FMIFKTHPLI
     LNYEHLNDSL DNPFHPIYKE HIELHPDGNM TVHEIEHERP YPNTALLSMC LMFGCFFIAY
     FLRQFKNGHF LPGPIRRLIG DFGVPIAIFF MIAVDISIED AYTQKLLVPK GVEVSNPKAR
     GWIINPMGEK KPFPGWMMGA CCVPALLVFI LIFLESQITT LIVSKPERKM VKGSGFHLDL
     LILVTMGGIA SIFGVPWLSA ATVRSVTHAN ALTVMTKGPK PEIEKVVEQR ISGMLVALMV
     GVSIYMEPIL KMIPMTALFG IFLYMGITSL SGIQMWDRIL LLITPKKYYP SDAYANRVRP
     LRMHLFTLIQ IVCLAVLWVV KMSAFSLALP FVLILTIPLR MLMTGRVFSN LEMKCLDADD
     AKVSLEEEPG EDVYNESPLP
//
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