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Database: UniProt
Entry: A0A3B5AF27_9TELE
LinkDB: A0A3B5AF27_9TELE
Original site: A0A3B5AF27_9TELE 
ID   A0A3B5AF27_9TELE        Unreviewed;      1295 AA.
AC   A0A3B5AF27;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000016484.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000016484.1}
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: 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}.
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DR   STRING; 144197.ENSSPAP00000016484; -.
DR   Ensembl; ENSSPAT00000016745.1; ENSSPAP00000016484.1; ENSSPAG00000012358.1.
DR   GeneTree; ENSGT00940000158259; -.
DR   Proteomes; UP000261400; Unplaced.
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; 1.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; 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   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        731..753
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        765..796
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        816..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        848..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        914..931
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        951..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1002..1023
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1044..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1126..1146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1176..1194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1200..1217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          370..645
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          702..1182
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..138
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1295 AA;  145202 MW;  8A2AADCF002A4D3B CRC64;
     MSNPSAPNQI TDAVASVIHG PEAPASSLHG TPRPEEEDDG DLNKALGVQR FQQILSPAAV
     VPEEQHHTYH EEDIEYHRHS SHHIHRPLSK LPSEGRRKKS SKKRKKDKDH KSSHASSSGA
     IEEGEDEEDE EEEGTEPSSA ASEPEKVKSD VEFFVSDEDH AAKRGKESPH SARELDIIPQ
     SGVGTDTEDA SSTDKPETAS PTAQSAPPEH PPLARVSSAS RSYDLQERRR TGNMTGTEQA
     KYQRIPTDES EAQTLASADL DGIKSHRFED VPGMRRHLVR KSTKGQVVHI GKDHKEPTTR
     SRKQDRTPHE PLPVVLYRSA SRPEGFLLDM DSGQMAGYQK VFVELNELTM DKNQEMQWKE
     TARWIKFEED VEEETDRWGK PHVASLSFRS LLELRKTISH GAVLLDLDQK TLPGIAHQVV
     EQMIISDQIK AEDRANVLRA LLLKHSHPSD EKEHTSHFPR NISAASLGSL ISHHHNANHN
     HQPEPSVTDP LMGAVHSMMD ADTRIDMEKN EVQQKEPSLG PGMHRSKSKH ELKLLEKIPE
     NAEATVVLVG SVDFLEQPTM AFVRLQEAVE LESVLEVPVP VRFLFVLLGP PTTSMDYHQI
     GRSISTLMSD KQFHEAAYLA DDRQDLLNAI NSFLDCSIVL PPSEMGDDEL LRSVARFQRE
     MLRKREEQGV KLSAKEPKSF EEKEALLTPL KKSDDPLQRT GRPFGGLIRD VRRRYPKYLS
     DFKDALNSQC MAAVIFIYFA ALSPAITFGG LLGEKTEGLI GVSELIVSTA VQGVVFCLLG
     AQPLLVVGFS GPLLVFEEAF YSFCKSNDIE YLTGRVWIGF WLIIIVIVTV AFEGSFLVRF
     VSRFTQEIFS FLISLIFICE TFFKLVKIFK DHPLQRCSLV NDTNDGAFTE NITVMLSNST
     LPVTVKVQGE PNTALLSLVL MAGTFFIAFY LRKFKNSAFF PGRFRRVIGD FGVPIAILIM
     VLVDYGIQDT FTQKLSVPSG FSVTTPQKRG WFISPLGTDK PFPIWMMFAC CLPALLVFIL
     IFMETQITTL IVSKKERMLV KGSGFHLDLL LIVVLGGSSA LFGLPWMAAA TVRSVTHVNA
     LTVMSKAVAP GDKPRIQEVK EQRVTGLLVA ILVGMSIVIG DLLRQIPLAV LFGIFLYMGV
     MSLNGIQLTE RMMLLLMPPK YHPDHTYVRK VRTLRMHLFT CIQVVCLAVL WAVMSTQASL
     AFPFVLILTV PVKMFVLRRI FSVREMACVS LTSGGRSRHS SLSKKRRVLM KEVFKFWCFV
     ISRFTDYDNS ARKEKRHVHT CIKFNYICGF TLMLC
//
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