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Database: UniProt
Entry: A0A093IRU7_FULGA
LinkDB: A0A093IRU7_FULGA
Original site: A0A093IRU7_FULGA 
ID   A0A093IRU7_FULGA        Unreviewed;      1039 AA.
AC   A0A093IRU7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 44.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
DE   Flags: Fragment;
GN   ORFNames=N327_07402 {ECO:0000313|EMBL:KFW04388.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW04388.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFW04388.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW04388.1};
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; KK597904; KFW04388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093IRU7; -.
DR   Proteomes; UP000053806; 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:UP000053806};
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..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..254
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        238..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1028
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW04388.1"
FT   NON_TER         1039
FT                   /evidence="ECO:0000313|EMBL:KFW04388.1"
SQ   SEQUENCE   1039 AA;  118033 MW;  F13235B0E80E4BB6 CRC64;
     RHDEEAVIDQ GRTSNVVNIH YEKEELEGHR TLYVGVRMPL VRQSHRHHRP HSQKHRKRER
     EKDSALTEQG YHYTPSQRVQ FILGTEEDEQ HVPHDLFTEL DEICVKDGED AEWKETARWL
     KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCIINGTVLL DICANSIEEI ADMILSQQEQ
     SPEFDERMQA KVREVLLKKH HHQNEKKRNN LLPIVRSFAD GSKKQSDPHL LDKPAQTLTP
     HPSPTTAEAK NGVNHETSAM DLSKAELHFM KKIPTGAEAS NVLVGELDFL HQPIVAFVRL
     TPAVLLSGMT EVPIPTRFLF VLLGPEGKAH QYHEIGRSMA TIMTDEVFHD VAYKAKNRAD
     LVAGIDEFLD QVTVLPPGEW DPSIRIEPPK NVPSQEKRKM PGALDDSTSH SKPEKHSGPE
     LEQTGRLFGG LILDVKRKAP WFWSDFRDGL SLQCLASFLF LYCACMSPVI TFGGLLGEAT
     SGHISAMESL LGASMTGVVY SLFAGQPLTI LGSTGPVLVF EKILYKFCQD YTLSYLSLRA
     CIGLWTTFFC IVLVATDASC LVCYITRFTE EAFASLICII FIYEALEKLS HLRETYPVHM
     HSKLDFLTIY YCKCEAPTHP SNETLRFWES NKINVSGITW ENLTVTECRY LHGEFQGPAC
     GHNGPYTPNV LFWCCILFFS TFVLSSLLKK FKTSRYFPTR VRSTISDFAV FLTIVIMVLI
     DFMIGIPSPK LHVPHMFKPT RDDRGWFINP IGPNPWWTVL AALIPALLCT ILIFMDQQIT
     AVIVNRKEHR LKKGCGYHLD LLMVAVMLGV CSVMGLPWFV AATVLSITHV NSLKVESNCS
     APGEHPKFLG IREQRVTGLM IFVLMGCSVF FTSVLKFIPM PVLYGVFLYM GVSSLRGIQF
     FDRLKLFWMP AKHQPDFIYL RHVPLRKVHF FTLIQLLCLV LLWGIKASRA AIIFPMMVLA
     LVFVRKVMDF CFSKRELSFL DDLMPESKKK KLDDAKNEAK EEELKLGKTS DLDIPKQNSD
     RADPSEINIS DEMSKTTVW
//
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