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Database: UniProt
Entry: A0A3P9PZD9_POERE
LinkDB: A0A3P9PZD9_POERE
Original site: A0A3P9PZD9_POERE 
ID   A0A3P9PZD9_POERE        Unreviewed;      1224 AA.
AC   A0A3P9PZD9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A7 {ECO:0000313|Ensembl:ENSPREP00000027134.1};
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:ENSPREP00000027134.1, 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:ENSPREP00000027134.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000027134.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; A0A3P9PZD9; -.
DR   Ensembl; ENSPRET00000027423.1; ENSPREP00000027134.1; ENSPREG00000018341.1.
DR   GeneTree; ENSGT00940000157045; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000018341; Expressed in head.
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; 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:SF105; SODIUM BICARBONATE COTRANSPORTER 3; 1.
DR   Pfam; PF07565; Band_3_cyto; 2.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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        592..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        621..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        679..702
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        709..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        808..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        846..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        894..913
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        934..958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        994..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1020..1039
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1078..1102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          145..258
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          369..514
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          563..1072
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          57..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1127..1165
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        57..72
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1224 AA;  137290 MW;  F1FA6DCFACEF4422 CRC64;
     MDESREQMNP LLSRGLDEEA LVDHGKTSFT TLSNYETEDL ESHRAVYVGV HVPFGRGSKR
     RHRHRERRHH RKKKDRDCEE EKEDGRESPS YDTPSQRVQF ILGTEDDDLE HIPHDLFTEL
     DELSFRDGGA TEWRETARWL KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCILNGTVML
     DMRANSIEEI ADMVIDSMVA SGQLKEDLRA KVREAMLKKH HHQNERKLSN RIPLVRSIAD
     IGEGLSSSRL SLHKPGLASS VSSLSQRRES RVSVLLSHLL PSSSSNTGLS PGPSPHSTPQ
     NTPLSFRRSH LSPSQTRCTG PGPQGIPEVV VSPPEDDEPA NSAEEDAVSP QLTRRTSSAS
     QNHELLPLEG PMVSPHSLPN NLDGNKAMER RPSKVGVDMN FMKKIPPGAE ASNVLVGEVD
     FLEKPIIAFV RLSPAVLITG LTEVPVPTRF LFLLLGPHGK GPQYHEIGRS MATLMTDEIF
     HDVAYKAKDR TDLLSGIDEF LDQVTVLPPG EWDPTIRIEP PKNVPSQMKR KRPSHPNGNA
     PPAGELEKED DHHAGPELQR TGRIFGGLIL DVKRKAPFYW SDIKDSLNLQ CLASILFLYC
     ACMSPVITFG GLLGEATKGS ISAIESLFGA SLTGVAYSLF AGQPLTILGS TGPVLVFEKI
     LFKFCKDYGL SYLSLRTSIG LWTAFLCILL VATDASSLVC YITRFTEEAF AALICIIFIY
     EALEKLFHLG EYYPVNMHNN LDNLTFYSCQ CSPPANASDQ LLQHWNRTGY NSSDSIPWSN
     LNVSMCKLLD GEFVGPACGH HGPYIPDVLF WSIILFFTTF FLSSFLKQFK TERYFPTKVR
     STISDFAVFL TIMIMVLVDY LMGIPSPKLH VPDRFEPTSK HRGWLMDPLG ENPWWTLLVA
     AVPALLCTIL IFMDQQITAV IINRKEHKLK KGCGYHLDLL IVAIMLGVCS IMGLPWFVAA
     TVLSISHVNS LKVESGCSAP GEQPKFLGIR EQRVTGFMIF TMMGCSVFMT SVLKFIPMPV
     LYGVFLYMGV SSLKGIQFFD RIRLFGMPAK HQPDLIYLRY VPLWKVHVFT LVQLTCLVLL
     WVIKASAAAV VFPMMVLALV FIRKLLDLLF TKRELSWLDD LMPESKKKTE DDKKKKAQEK
     LHCLLKEEES QLEEEEEEER KMKVHFEGSN RLNIPVNSIS GRSYRIGVVT ESLQWKNSQE
     KVACVRVDVS PDSPGEGSTA ETFL
//
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