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Database: UniProt
Entry: A0A093GVD9_STRCA
LinkDB: A0A093GVD9_STRCA
Original site: A0A093GVD9_STRCA 
ID   A0A093GVD9_STRCA        Unreviewed;      1046 AA.
AC   A0A093GVD9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
DE   Flags: Fragment;
GN   ORFNames=N308_10446 {ECO:0000313|EMBL:KFV74263.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV74263.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV74263.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV74263.1};
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; KL205766; KFV74263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093GVD9; -.
DR   STRING; 441894.ENSSCUP00000004961; -.
DR   Proteomes; UP000053584; 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:UP000053584};
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..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        542..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        572..591
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        671..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        711..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        762..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        800..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        862..881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        887..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        957..974
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..940
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          42..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..62
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1013
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1030
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV74263.1"
FT   NON_TER         1046
FT                   /evidence="ECO:0000313|EMBL:KFV74263.1"
SQ   SEQUENCE   1046 AA;  118218 MW;  C0401243C34B0734 CRC64;
     RPDEEAVVDQ GGTSNVVNIH YEKEELEGHR TLYVGVRMPL VRQSHRHHRP HSQKHRKRER
     AKGYARAGQG YHDTPSQRVQ FILGAEEDEQ HVPHDLFTEL DEICVKEGEH AEWKETARWL
     KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCIINGTVLL DICANSIEEI ADMILDQQEQ
     SNEFDERMRV KVREALLKKH HHQNEKKRNN LLPIVRSFAD VNKKQTDLHL LDKPAQTLTP
     HPPPTTVEAK NGTSHETSPM DLSKAELHFM KKIPTGAEAS NVLVGELDFL RRPIVAFARL
     TPAVLLSGMT EVPIPTRFLF VLLGPEGKAH QYHEIGRSMA TLMTDEVFHD VAYKAKDRAD
     LVAGIDEFLD QVTVLPPGEW DPSIRIEPPK NVPSQKKRKM PGALDDGACH SEPEKHSGPE
     LQRTGRLFGG LMLDVKRKAP WFWSDFRDAL SLQCLASFLF LYCACMSPVI TFGGLLGEAT
     DGHISAMESL LGASMTGVVY SLFAGQPLTI LGSTGPVLVF EKILYKFCKD YALSYLSLRT
     CIGLWTSFLC VVLVATDASC LVCYITRFTE EAFAALICII FIYEALEKLI WLGEAYPIHM
     GSELDLLTVY YCKCEAPAHP TNETLRFWES NKINPSLITW ENLTVSECRR LHGEFHGLAC
     GHDGPYTPNV LFWSCILFFS TFILSGSLKM FKTSHYFPTR VGFSPQVRST ISDFAVFLTI
     VTMVIIDYLI GIPSPKLHVP SMFQPTRDDR GWLINPIGPN PWWTVLAAFI PALLCTILIF
     MDQQITAVIV NRKEHKLKKG CGYHLDLLMV AVMLGVCSMM GLPWFVAATV LSITHVNSLK
     LESGCSAPGE QPRFLGIREQ RVTGLMIFVL MGCSVFLTGV LKFIPMPVLY GVFLYMGVSS
     LRGIQFFDRL KLFGMPKKHQ PDFIYLRHVP LRKVHLFTLI QLTCLVLLWI IKASPAAIVF
     PMMVLALVFV RKVMDFCFSK RELSWLDDLM PESKKKKLDD AENEAKEEEL NLGKTSYSDV
     SNQDNSDRVD PSDINISDEM PKTTVW
//
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