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
//