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
//