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Database: UniProt
Entry: A0A087VAG1_BALRE
LinkDB: A0A087VAG1_BALRE
Original site: A0A087VAG1_BALRE 
ID   A0A087VAG1_BALRE        Unreviewed;      1054 AA.
AC   A0A087VAG1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
DE   Flags: Fragment;
GN   ORFNames=N312_05794 {ECO:0000313|EMBL:KFO09603.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO09603.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO09603.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO09603.1};
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; KL485974; KFO09603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087VAG1; -.
DR   Proteomes; UP000053309; 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:UP000053309};
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..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        533..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        928..945
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          232..256
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          1014..1054
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        238..256
FT                   /note="Polar 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        1029..1043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO09603.1"
FT   NON_TER         1054
FT                   /evidence="ECO:0000313|EMBL:KFO09603.1"
SQ   SEQUENCE   1054 AA;  119465 MW;  E96835CE1A6FB659 CRC64;
     RHDEEAVIDQ GRTSNVVNIH YEKEELEGHR TLYVGVRMPL VRQSHRHHRP HSQKHRKRER
     EKDSVPTEQG YHYTPSQRVQ FILGTEEDEQ HVPHDLFTEL DEICAKEGED AEWKETARWL
     KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCIINGTVLL DICANSIEEI ADMILGQQEQ
     STEFDEHVRA KVREVLLKKH HHQNEKKRNN LLPIVRSFAD VSKKQSDLHL LDKPAQTLTP
     HPSPTTAEAK NGVNHESNAT DLSKAELHFM KKIPTGAEAS NVLVGELDFL RQPIVAFVRL
     TPAVLLSGMT EVPIPTRFLF VLLGPEGKAH QYHEIGRSMA TIMTDEVFHD VAYKAKNRAD
     LVAGIDEFLD QVTVLPPGEW DPSIRIEPPK NVPSQEKRKM PGALDDSAAH SKPEKHSGPE
     LERTGRLFGG LILDVKRKAP WFWSDFRDGL SLQCLASFLF LYCACMSPVI TFGGLLGEAT
     NGHISAMESL LGASMTGVVY SLFAGQPLTI LGSTGPVLVF EKILYKFCKE YTLSYLSLRA
     CIGLWTAFFC IVLVATDASC LVCYITRFTE EAFASLICII FIYEALEKLS HLRETYPVHM
     HSKLDFLTVY YCKCEAPSHP SNKTLRFWES NKINVSGITW ENLTVTECRY LHGEFHGPAC
     GRNGPYAPNV LFWCCILFFS TFVLSSLLKK FKTSRYFPTR VRSTISDFAV FLTIVIMVLI
     DFLIGIPSPK LHVPHMFKPT RDDRGWFINP IGPNPWWTVL AALIPALLCT ILIFMDQQIT
     AVIVNRKEHR LKKGCGYHLD LFMVAVMLGV CSVMGLPWFV AATVLSITHV NSLKVESGCS
     APGEQPKFLG IREQRVTGLM IFVLMGCSVF FTSVLKFIPM PVLYGVFLYM GVSSLRGIQF
     FDRLKLFGMP AKHQPDFIYL RHVPLRKVHF FTMIQLICLV LLWAIKVSRA AIIFPMMVLA
     LVFVRKVMDF CFSKRELSFL DDLMPESKKK KLDDAKNEAK EEEESQKMME AAAANSVQLK
     LGKTSDLDIP KQSSDRTDPS EINISDEMSK TTVW
//
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