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Database: UniProt
Entry: A0A091IPI2_EGRGA
LinkDB: A0A091IPI2_EGRGA
Original site: A0A091IPI2_EGRGA 
ID   A0A091IPI2_EGRGA        Unreviewed;      1039 AA.
AC   A0A091IPI2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
DE   Flags: Fragment;
GN   ORFNames=Z169_13097 {ECO:0000313|EMBL:KFP10609.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP10609.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP10609.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP10609.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK500822; KFP10609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091IPI2; -.
DR   STRING; 188379.A0A091IPI2; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
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; IPR013769; Band3_cytoplasmic_dom.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF37; ELECTRONEUTRAL SODIUM BICARBONATE EXCHANGER 1; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE   3: Inferred from homology;
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:UP000053119};
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        455..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        489..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        532..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        568..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        670..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        708..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        756..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        796..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        856..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        882..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        952..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          125..382
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          426..934
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          40..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1009
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP10609.1"
FT   NON_TER         1039
FT                   /evidence="ECO:0000313|EMBL:KFP10609.1"
SQ   SEQUENCE   1039 AA;  118007 MW;  6A30055FEF2974AD CRC64;
     RHDEEAVIDQ GRTSNVVNIH YEKEELEGHR TLYVGVRMPL VRQSHRHHRP HSQKHRKRER
     EKDSAPAEQG YHYTPSQRVQ FILGTEEDEQ HVPHDLFTEL DEICVKEGED AEWKETARWL
     KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCIINGTMLL DICANSIEEI ADMILGQQEQ
     SAEFDERMRA KVREVLLKKH HHQNEKKRNN LLPIVRSFAD ASKKQADLHL LDKPAQTLTP
     HPSPTTAEAK NGVNHETNAM DLSKAELHFM KKIPTGAEAS NVLVGQLDFL HQPIVAFVRL
     TPAVLLSGMT EVPIPTRFLF VLLGPEGKAH QYHEIGRSMA TIMTDEVFHD VAYKAKNRAD
     LVAGIDEFLD QVTVLPPGEW DPSIRIEPPK TVPSQEKRKM PGALDDSSSH SKPEKHSGPE
     LERTGRLFGG LILDVKRKAP WFWSDFRDGL SLQCLASFLF LYCACMSPVI TFGGLLGEAT
     NGHISAMESL LGASMTGVVY SLFAGQPLTI LGSTGPVLVF EKILYKFCKE YALSYLSLRV
     CIGLWTAFFC IVLVATDASC LVCYITRFTE EAFASLICII FIYEALEKLS HLRETYPVHM
     HSKLDFLTIY YCKCEAPAHP SNETLRFWES HKINVSGLAW ENLTVTECRY LHGEFQGPAC
     GRNGPYTPNV LFWCCILFFS TFVLSSLLKK FKTSRYFPTR VRSTVSDFAV FLTIVVMVLI
     DFMIGIPSPK LHVPHMFKPT RDDRGWFISP IGPNPWWTVL AALIPALLCT ILIFMDQQIT
     AVIVNRKEHR LKKGCGYHLD LFMVAVMLGV CSVMGLPWFV AATVLSITHV NSLKVESNCS
     APGEQPKFLG IREQRVTGLM IFVLMGCSVF FTSVLKFIPM PVLYGVFLYM GVSSLRGIQF
     FDRLKLFWMP AKHQPDFIYL RHVPLRKVHF FTLIQLICLV LLWAIKVSRA AIIFPMMVLA
     LVFVRKVMDF CFSKRELSFL DDLMPESKKK KLDDAKNEAK EEELKLGKTS TSDTPKQNSD
     RADPSEINIS DEMPKTTVW
//
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