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Database: UniProt
Entry: A0A232F6S7_9HYME
LinkDB: A0A232F6S7_9HYME
Original site: A0A232F6S7_9HYME 
ID   A0A232F6S7_9HYME        Unreviewed;      1046 AA.
AC   A0A232F6S7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-NOV-2023, entry version 23.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   ORFNames=TSAR_005653 {ECO:0000313|EMBL:OXU26541.1};
OS   Trichomalopsis sarcophagae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC   Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX   NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU26541.1, ECO:0000313|Proteomes:UP000215335};
RN   [1] {ECO:0000313|EMBL:OXU26541.1, ECO:0000313|Proteomes:UP000215335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alberta {ECO:0000313|EMBL:OXU26541.1,
RC   ECO:0000313|Proteomes:UP000215335};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXU26541.1};
RX   PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA   Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT   "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL   Curr. Biol. 27:2007-2013(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXU26541.1}.
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DR   EMBL; NNAY01000781; OXU26541.1; -; Genomic_DNA.
DR   STRING; 543379.A0A232F6S7; -.
DR   Proteomes; UP000215335; Unassembled WGS sequence.
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; 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   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF47; ANION EXCHANGE PROTEIN; 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.
PE   3: Inferred from homology;
KW   Anion exchange {ECO:0000256|ARBA:ARBA00022681};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362035}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}.
FT   DOMAIN          116..393
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          460..978
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          35..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..434
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  117571 MW;  1163015B23FDFA93 CRC64;
     MAQTLWCRSA GRRRHVRGSG SRSTXQPDEA KTLQELDIDD LESHRSDDPR GMRRHKAAHP
     TVQIGRRKEG GIPHETFKKM YDHSPHEVFV QLDELHGVGE EREWRETARW IKYEEDVEEG
     ADRWGRPHVA SLSFHSLLNL RRCLETGVVL LDLEEKDLPG LAYRVVEQMV IEELILPEDR
     PVVMRALLLR HRHVHEHDRG FRFGAKRNYA SYTSLQSIWF DDEDATREGA ENNNLNDSKP
     KIVASNQALD SNNHTVVDMK EELTFTSSNE DMKKGHNDHI LKRIPSGAEA TVVLVGAVDF
     LDQPTIAFVR LAEGILMPAI TEVTIPVRFM FTLLGPRNSD LDYHEIGRSI STLMSNTSFH
     MIAYKANERR ELLSAINEFL DDSIVLPPGD WERQALLPFG ELKAKSEAIR KRKAKAIEEK
     KKKQQQQIQS ENAAAKKALL AGEDEKKPPD DSDPLRRTRR PFGGLINDIK RRYPYYLSDF
     TDGLSSSCLA AAIFMYFAAL CTAITFGGLL SDKTHNVIGI SETLVSCCCT GIIMALFATQ
     PLVIIGTTGP LLLFDESLYN FCMANNLDFL TMRLYVGAWM AIIALAIACV EGSVLVRLFT
     RFTEEIFTGL ISILYIVETF IKLVNYFKRN PLLPAYCFAS DTSNDNNQTV YQDILHQSPV
     NNTEISRLME ASQTAVSSVL GISNNRTDFA LYQDSPFIPA HDKVGLLINQ PNTALMCTIL
     CLGTFLGAYY LRIFRNSHYL GRSARRAFGD FGVPISIITF VLIDYLAGVK TEKLLVPEGL
     SPTLPGRSWL VSPTKGDVPL WMALACCVPA LLVYILVFME TQISELIIDK KERKLRKGNG
     YHMDIVVVCL MNFGCGLIGA PWCCAASVRS LTHVNAVTVM SRTHAPGDKP HIVEVKEQRV
     SSLLVAILVG VSVLMAPLLR RVPMSVLLGV FLYMGISSTN GVQLFDRVKL FFMPVKHHGT
     ANYVRRVQTY KMHIFTLVQI TCLAVLWTVK STKAALALPF FLILMIPLRA QMTHFFSTAE
     LRALDSKNPD NEEDEPDFYE EAPLPG
//
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