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Database: UniProt
Entry: A0A3B3VT55_9TELE
LinkDB: A0A3B3VT55_9TELE
Original site: A0A3B3VT55_9TELE 
ID   A0A3B3VT55_9TELE        Unreviewed;      1212 AA.
AC   A0A3B3VT55;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000028052.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000028052.1}
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   RefSeq; XP_014908808.1; XM_015053322.1.
DR   AlphaFoldDB; A0A3B3VT55; -.
DR   STRING; 48699.ENSPLAP00000028052; -.
DR   Ensembl; ENSPLAT00000030009.1; ENSPLAP00000028052.1; ENSPLAG00000017110.1.
DR   GeneID; 106960297; -.
DR   CTD; 6508; -.
DR   GeneTree; ENSGT00940000159765; -.
DR   OrthoDB; 1013180at2759; -.
DR   Proteomes; UP000261500; 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   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:SF15; ANION EXCHANGE PROTEIN 3; 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   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   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        707..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        741..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        792..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        824..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        873..890
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        910..927
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        961..982
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1003..1026
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1089..1108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1140..1169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          352..618
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          679..854
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   DOMAIN          867..1141
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..105
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1212 AA;  136552 MW;  DAA7466A50DA1161 CRC64;
     MATGGHDVLA NLQQVKVEDQ DAAEEEEESW EKALSVERFR DVIGDSASCS AERMGRLYTE
     KDFEYHRHTF LHTHHPLSTH LPTPQRKRPH GADRRHRKKR KKKKTSLPPS DVTPTIQEVD
     EEEAESDADG RLATATPTEF PDIQPQFSFG SQEDLEEPLR LAAVHVENEE RSRKTALTLI
     KEAANNDRTE EKDGGQAASQ SASEAVSPAP SRGWLRRKAV HHRLMATQRS NYDLRERLCI
     GSMTAMEAAV YQQVPTDEAE AQMLVSADLD DMKSHRFEDN PGVRRHLVKK SSRCQMSRSS
     MSSTPLSSLK KKKRAADKKT HELFVELNEL IVDKDQEMRW KERARWIKFE EDVEEETDRW
     GKPHVASLSF RSLLELRRTI THGAVLLDLE QNTLPGIAHL VVETMIISDQ IRAEDRPGVL
     RALLLKHSHP SDLKHRFHRH QSSGSLHGSF NHNHVQETSL PLVAEENDDK GPVYDPKQDV
     FVSLFKSLHP VPPEHHPAAA RSLKLLAKIP KDAEAVIVLV GSVEFLEQPA MAFVRLSEAV
     LLESVLEVPV PVRFLFVLLG PSQSNVDYHE IGRSFATLMS EKNFHEVAYF ADDRQDLLNG
     INEFLDCSIV IPPSDVEGKD LLKTVADFQK QLLRKRRERE GKKLQTAYGV EQDSKAEASP
     EEEEEAEQEV DPLKRSGVPF GGLIHDMRRR YPQYVSDLRD ALDTQCVAAV IFIYFAALSP
     TITFGGLLGE KTEGLMGVTE LIVSTATLGV IFSLLAGQPL LIIGFSGPLL VFEEAFYKFC
     QAHDFEYLTG RVWIGFWLIF IVLVIVAAEG SFLVRYISPF TQEIFAFLIS LIFIYETFSK
     LIKVFKEHPL MTVYPSDSTV DVDSPVLNQP NTALLSLVLM IGTFFVAFFL RKFRNSRFLG
     GKARRIIGDF GIPISILLSV LVDISIPDTY TQKLNVPSGF SVTSPDKRGW LISPFGDKQP
     FPTWMMGASI VPALLVFILI FMETQITSLI VSKKERRLMK GSGFHLDLLL IVVLGAVCPL
     FGLPWLTAAT VRSVTHVNAL TVMSKATAPG EKPVIQEVKE QRLTGLLVAV LVGMSIVMTD
     VLRHIPLAVL FGIFLYMGVT SLTGIQLYER ITLMVTPAKH HPDHIYVTKV RTWRMNMFTV
     IQLACIVALW VVKSTVASLA FPFILIMTVP LRRLVLSRIF EERELQALDC DEDSPNFDED
     GRDEYNEIHM LV
//
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