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Database: UniProt
Entry: A0A2Y9MEW9_DELLE
LinkDB: A0A2Y9MEW9_DELLE
Original site: A0A2Y9MEW9_DELLE 
ID   A0A2Y9MEW9_DELLE        Unreviewed;       961 AA.
AC   A0A2Y9MEW9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A1 {ECO:0000313|RefSeq:XP_022420809.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022420809.1};
RN   [1] {ECO:0000313|RefSeq:XP_022420809.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022420809.1};
RG   RefSeq;
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   RefSeq; XP_022420809.1; XM_022565101.2.
DR   AlphaFoldDB; A0A2Y9MEW9; -.
DR   Proteomes; UP000248483; 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; IPR002977; Anion_exchange_1.
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; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01187; ANIONEXHNGR1.
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:UP000248483};
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        454..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        498..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        540..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        572..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        614..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        653..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        708..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        750..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        810..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        836..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        880..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        906..928
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          127..374
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          426..606
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   DOMAIN          615..887
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
SQ   SEQUENCE   961 AA;  106968 MW;  AB2ABCCD146CC895 CRC64;
     MFLELVIPGD GQKRKPGTCS VGYAGGSDHC RQLNNQDSAM GDSQENEDKL EEFLEQKEYE
     DLGFPTLQVE EAEAQLTEPT ATDYHTASRR PPDVLEVVVE LRELVMDEKN QELQWMETAR
     WVQLEENLGK GGIWGRPHLS YLTFWSLLEL QKAFAKGTVL LDLPEKSLAG VASQLLDRFI
     FEGQIQPQDR ENLFRVLLLK HSHARDVEAL GSVKPAVLTR SGDPSQPLLP QHPSLETEVF
     CEQGEGSAEG HSSSGMLGKS PQDREATLVL VGCARFLERP VLGFVRLKEP METEQKPQEP
     EGPAVPVRFL IVLLGPEAPN IDYTQLGRAA ATLMSERVFR TDAYLAQNKE MLVHSLEGFL
     DCSLVLPPTD APPEDALLSL VPVQKELLKR RYLPSSAKPE PSFLKGLDLN GGLEDTQDDP
     LQRTGRLFGG LVRDIRRRYP RYLSDITDAL NPQVLSAIIF IYFAALSPAI TFGGLLGEKT
     HNLMGVSELL ISTAAQGILF SLLGAQPLLV VGFSGPLLVF EEAFFSFCKS NGLEYIVGRV
     WIGFWLILLV VLVVAFEGSF LVRFISRYTQ EIFSFLISLI FIYETFSKLV TIFQDHPLLE
     NYDHNVTRIP KPQAPLPNTA LLSLVLMAGT FLFAMMLRKF KNSSYFPGKL RRVIGDFGVP
     ISILIMVMVD ALIQDTYTQK LSVPKGLTVS NTSARGWLIH PLGLYKPFPI WMMFASALPA
     LLVFILIFLE SQITTLIISK PERKVAKGSG FHLDLLLVMG MGGVATLFGM PWLSATTVRS
     VTHANALTVT GKASTPGTAA QIQEVKEQRI SGLLVSVLVG LSILMGPILS HIPLAVLFGI
     FLYMGVTSLS GIQLFDRILL LFKPRKYHPD VPYAKRVRTW RMHLFTGTQI ICLVVLWVVR
     SIKTISLALP FILILTVPLR HFLLPLIFQN LELQCLDADN AKPNFDEENG QDEYDEVAMP
     V
//
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