ID G1NFB9_MELGA Unreviewed; 726 AA.
AC G1NFB9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000011690.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000011690.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000011690.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00034408};
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; G1NFB9; -.
DR Ensembl; ENSMGAT00000012570.3; ENSMGAP00000011690.3; ENSMGAG00000011177.3.
DR GeneTree; ENSGT00940000159765; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; G1NFB9; -.
DR TreeFam; TF313630; -.
DR Proteomes; UP000001645; Chromosome 7.
DR Bgee; ENSMGAG00000011177; Expressed in brain and 18 other cell types or tissues.
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; IPR001717; Anion_exchange.
DR InterPro; IPR018241; Anion_exchange_CS.
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 InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF15; ANION EXCHANGE PROTEIN 3; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PE 3: Inferred from homology;
KW Anion exchange {ECO:0000256|ARBA:ARBA00022681};
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
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:UP000001645};
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 211..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 245..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 296..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 328..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 386..404
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 424..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 475..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 517..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 577..596
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 603..622
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 655..683
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 1..98
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT REGION 132..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 81731 MW; 963C253337E1A783 CRC64;
YEKTGRKLIM SVLKKEHAFL EQPTMAFVRL NEAVFLESVL EVPIPVRFIF VLLGPSQANM
DYHEIGRSIS TLMSDKHFHE AAYMADDRQD LLNAINEFLD CSIVIPPSEV EGKDLLKSIA
TFQKLLLRKR KEREQKSMKE GDGGPEFPRS SPALHAPPEL CEVKAEEEEE EAEDDPLKRT
GIFFGGLVRD IKRRYPKYLS DIRDALHSQC LAAVLFIYFA ALSPAITFGG LLGEKTEGLM
GVSELIISTS VLGILFSLLG AQPLLVIGFS GPLLVFEEAF YKFCQTQDIE YLTGRVWIGL
WLIVFIFIIV AAEGSFLVRY ISPFTQEIFA FLISLIFIYE TFYKLYKVFA EHPLLKFYPP
NVQSGLNASM LSADAMSLGI RMQPNTALLS LILMLGTFFI AFFMRKFKNS RFLGGKARRI
IGDFGIPISI LVMVLVDYTI TDTYTQKLNV PSGLSVTSPH KRGWFIHPMG SNGTFPLWMM
FASAIPALLV FILIFMETQI TTLIVSKKER KLLKGSGFHL DLLLIGTMGG LCALFGLPWL
TAATVRSVTH VNALTVMSKA IAPGEKPKIE EVKEQRVTGV LIAALVGLSI VMGNMLRQIP
LAVLFGIFLY MGVTSLTGIQ LYERLLLIFM PSKHHPDHIY VVKVKTWRMN LFTCIQLACI
VLLWVVKSTV ASLAFPFVLI MTVPLRRFVL PRFFHDRELK ALDSEDAEPN FDEDGRDEYN
ELHMPV
//
