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Database: UniProt
Entry: A0A1S3LUX8_SALSA
LinkDB: A0A1S3LUX8_SALSA
Original site: A0A1S3LUX8_SALSA 
ID   A0A1S3LUX8_SALSA        Unreviewed;      1099 AA.
AC   A0A1S3LUX8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=LOC106568665 {ECO:0000313|RefSeq:XP_013994656.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013994656.1};
RN   [1] {ECO:0000313|RefSeq:XP_013994656.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013994656.1};
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: 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362035}.
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DR   RefSeq; XP_013994656.1; XM_014139181.1.
DR   AlphaFoldDB; A0A1S3LUX8; -.
DR   OrthoDB; 1013180at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa14.
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; 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:UP000087266};
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        759..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        793..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        844..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        876..894
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        934..952
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        972..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1023..1043
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          400..674
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          731..1052
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..99
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..126
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  122382 MW;  8AC280CC12E0AE53 CRC64;
     MSNPKDASDT NAMATATSAP PALSRRSEDD DEEQDLNKTL GVQLFQQILH PPARGPPEKH
     RAYNEEDFEY HRHSSHHIHH PLSKLPPERR KKKSKKKEAG WRRGSGPGGA PNIEEDEEEE
     ADESYSQNDG EGGQTTTPTP DTDTDTHNED VQFFVSEDDP ASVTPAPMHS KAGSATLPRR
     LTIVPETALG TNLPEDATPT DEPVDSVLAP NKGRNGLSSS PSRESHNPST RGSTPPSSSV
     SSSSSRIPPP GSRSYDLQER RRLGNMTGGQ QERHQRQATD DSEAQMLGSA DLDGIKSHRF
     EDVPAVHRHL VRKSNKGQVV HISKDHKEPS APCSKLDRTP HEPVLEYRST SRSDRMVRLE
     FVGRMARHQK VFVELNELVM DKNQELQWRE TARWIKFEED VEEETDRWGK PHVASLSFRS
     LLELRKTISH GAVLLDLNQH TLPGIAHQVV EQMIISDQIK VEDRANVLRA LLLKHSHPSD
     EKEHSSFTHN ISAASLASLM VNHHSSSNHI GQAEPSVTDT VMGGGEAACI LPDTRIDMEK
     SEKDNPPKLG MHRSKSKHEL KLLEKIPENA EATVVLVGTV AFLEQPSMAF VRLQEAVLLE
     SVLEVPVPVR FLFLLMGPPI ANIDYHQIGR SISTLMSDKH FHEAAYLADE RQDLLNAINS
     FLDCSIVLPP SEVGGEELLR SVARFQREML HKREEQQGKK LKVKEPKSPK DKALQASFKP
     GDDPLRRSGH LFGGLISDAA RRYPKYASDF RDALNPQCMA AIIFIYFAAL SPAVTFGGLL
     GEKTGGLIGV SELIIATAMQ GVIFSLLGAQ PLLVVGFSGP LLVFEEAFYS FCNANHIEYL
     TGRVWIGFWL VLIVVIIVAF EGSFMVRFVS RFTQEIFSFL ISLIFIYETF SKLGKIFQEH
     PLQRCYLVND TWTSSSCNNT VVGVPGKVVG EPNTALLTLV LMSGTFFIAF YLRKFKNSAF
     FPGKLRRMIG DFGVPIAILI MVLVDYSIKD TYTQKLSVPT GFSVTSPEKR RWLIPPLGSD
     GQFPVWMMAT SILPALLVFI LIFMETQITT FVHCDRRSPA SDPHRCALWD LPLHGRHVPQ
     RYPAHRAHAA AFDASQVSS
//
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