ID A0A3P9Q9I9_POERE Unreviewed; 1159 AA.
AC A0A3P9Q9I9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000030755.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000030755.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000030755.1};
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 AlphaFoldDB; A0A3P9Q9I9; -.
DR STRING; 8081.ENSPREP00000030755; -.
DR Ensembl; ENSPRET00000031105.1; ENSPREP00000030755.1; ENSPREG00000020828.1.
DR GeneTree; ENSGT00940000159765; -.
DR OMA; HKLWRPP; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000020828; Expressed in head and 1 other cell type or tissue.
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 Reference proteome {ECO:0000313|Proteomes:UP000242638};
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 654..676
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 688..719
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 739..764
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 771..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 820..837
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 857..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 908..929
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 950..973
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1036..1055
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1087..1116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 299..565
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 626..801
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT DOMAIN 815..1088
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 19..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 130543 MW; FF4004E39CDB6B9C CRC64;
MGRLYTEKDF EHHRHAFLHT HHPLSTHLPA SQRKRPHGAD RRHRKKRKRK KTSLPPSDVT
PTIQEVDEEE AEPDADLATA TPTEFPDIRP QFSFGSQEDL EEPLRLAAVH VENEERSASR
KTALTLIKEA AKNDGTEERD GGRAASRSAS EAVNPAPSRG WLRRKAVHHR LMAAQRSNYD
LRERLCIGSM TAMETAVYQQ VPTDEAEAQM LVSADLDDMK SHRFEDNPGV RRHLVKKSSR
CQMSRSSMSS TPLSSLKKKK RAADKKTHEL FVELNELIVD KDQEMRWKER ARWIKFEEDV
EEETDRWGKP HVASLSFRSL LELRRTITHG AVLLDLEQNT LPGIAHLVVE TMIISDQIRA
EDRPGVLRAL LLKHSHPSDL KHRFHRHQSS GSLHGSFNHN HLQETSLPLV AEENDDKGPV
YDPKQDVFVS LFKSLHPVPP EHHPAAARSL KLLAKIPKDA EAVIVLVGSV EFLEQPAMAF
VRLSEAVVLE SVLEIPVPVR FLFVLLGPSQ SNVDYHEIGR SFATLMSEKN FHEVAYFADD
RQDLLNGINE FLDCSIVIPP SDVEGKDLLK TVADFQKQLL RKRREREGKK LPSAYGAEQD
SKAEASPEEE EEAEQEVDPL KRSGVPFGGL IHDMRRRYPQ YVSDLRDALD TQCVAAVIFI
YFAALSPTIT FGGLLGEKTE GLMGVTELIV STATLGVIFS LLAGQPLLII GFSGPLLVFE
EAFYKFCQAH DFEYLTGRVW IGFWLIFIVL VIVAAEGSFL VRYISPFTQE IFAFLISLIF
IYETFSKLIK VFKEHPLMTV YPSDSTVDVD GPVLNQPNTA LLSLVLMIGT FFVAFFLRKF
RNSRFLGGKA RRIIGDFGIP ISILLSVLVD ISIPDTYTQK LNVPSGFSVT SPDKRGWLIS
PFGDKQPFPT WMMGASVVPA LLVFILIFME TQITSLIVSK KERRLMKGSG FHLDLLLIVV
LGAVCPLFGL PWLTAATVRS VTHVNALTVM SKATAPGEKP VIQEVKEQRL TGLLVAVLVG
MSIVMTDVLR HIPLAVLFGI FLYMGVTSLT GIQLYERITL MVTPAKHHPD HIYVTKVRTW
RMNMFTAIQL ACIVALWVVK STVASLAFPF ILIMTVPLRR LVLSRIFEER ELQALDCDED
SPNFDEDGRD EYNEIHMLV
//
