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Database: UniProt
Entry: A0A3P8NMQ7_ASTCA
LinkDB: A0A3P8NMQ7_ASTCA
Original site: A0A3P8NMQ7_ASTCA 
ID   A0A3P8NMQ7_ASTCA        Unreviewed;      1253 AA.
AC   A0A3P8NMQ7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000006096.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000006096.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000006096.1}
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   AlphaFoldDB; A0A3P8NMQ7; -.
DR   STRING; 8154.ENSACLP00000006096; -.
DR   Ensembl; ENSACLT00000006236.1; ENSACLP00000006096.1; ENSACLG00000004023.1.
DR   GeneTree; ENSGT00940000158259; -.
DR   OMA; RYQRMPT; -.
DR   Proteomes; UP000265100; Chromosome 9.
DR   Bgee; ENSACLG00000004023; Expressed in ovary and 8 other cell types or tissues.
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; 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.
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..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        773..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..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        912..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        946..966
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1001..1022
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1043..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1125..1145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1175..1193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1199..1216
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..1181
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1253 AA;  140256 MW;  602C0BFD758CA379 CRC64;
     MSNPDAPSQV TDAVASVIHG PEAPAASSLH GSPRPEEEDD GDLNKALGVQ RFQQILTPAA
     AVPDKEHHIY HDEDIEYHRH SSHHIHRPLS KLPSDVRRRK GSKKRKKDKD HKSSHPLCSV
     PIEEGEDEEE EEEEGTELNS VLSERSESER TKDVEFFVSE DDHVSKSVKE SPHSVRKLDI
     VPQSGVGGEH EDATSTDKLP SSEPSSPTAQ SVPAEHTPLT RVSSASRSYD LTERRRTGNM
     TGAEQAKYQR IPTDESEAQT LASADLDGIK SHRFEDVPGM RRHLVRKSTK NQVVHIGKDH
     KEPTTRSRKQ DRTPHEPVVL YRSASWTEGV HRCGQMARQK VFVELNELTM DKNQELQWKE
     TARWIKFEED VEEETDRWGK PHVASLSFRS LLELRRTISH GAVLLDLDQK TLPGIAHQVV
     EQMIISDQIK AEDRANVLRA LLLKHSHPSD EKEHSSHFPR NISAASLGSL IAHHHSVNHT
     NQTEPSVTDP LMGTVRVTGD TDTHIDMEKN EVQQREPSIG PGMHRSKSKH ELKLLEKIPE
     NAEATVVLVG SVDFLEQPTM AFVRLQEAVE LESVLEVPVP VRFLFVLLGP ATTSMDYHQI
     GRSISTLMSD KQFHEAAYLA DDRQDLLNAI NSFLDCSIVL PPSEVGGDEL LRSVARFQRE
     MLRKREELEV KLMAKEPKSL EEKEALLKPS KKSDDPLERT GRPFGGLIRD VQRRYPKYVS
     DFKDALNSQC MAAVIFIYFA ALSPAITFGG LLGEKTNGLI GVSELIVSTS VQGVVFCLLG
     AQPLLVVGFS GPLLVFEEAF YSFCTSNNIE YLTGRVWIGF WLIIIVVTMV AFEGSFLVRF
     VSRFTQEIFS FLISLIFICE TFIKLVRIFK EHPLKSCSLN GTDADDLAEN ITLMMKNSSQ
     PSTVKVSGEP NTALLSLVLM AGTFFIAFYL RKFKNSAFFP GRIRRIIGDF GVPIAILIMV
     LVDYSIEDTF TQKLSVPSGF SVTNSDKRGW FISPLGSNGE FPIWMMFACC LPALLVFILI
     FMETQITTLI VSKKERMLVK GSGFHLDLLL IVVLGGTSAL FGLPWMAAAT VRSVTHVNAL
     TVMSKAVAPG DKPRIQEVKE QRVTGLLVAI LVGLSIVIGD LLCQIPLAVL FGIFLYMGVM
     SLNGIQLTER MMLLLMPPKY HPDHTYVRKV RTLRMHLFTC IQLVCLAVLW AIMSTAASLA
     FPFVLILTVP VKMFVLRRVF TVKEMACLDA DDAEPKFDER ECHDEYSEMQ MPV
//
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