ID A0A158RB74_THECL Unreviewed; 983 AA.
AC A0A158RB74;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN ORFNames=TCLT_LOCUS3730 {ECO:0000313|EMBL:VDN00724.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000374101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000374101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN00724.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UYYF01004265; VDN00724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158RB74; -.
DR STRING; 103827.A0A158RB74; -.
DR WBParaSite; TCLT_0000374101-mRNA-1; TCLT_0000374101-mRNA-1; TCLT_0000374101.
DR OMA; FWVAVWI; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; 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; 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:SF36; ANION EXCHANGE PROTEIN; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
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:UP000276776};
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 443..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 470..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 526..544
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 556..574
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 644..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 682..699
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 719..746
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 766..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 828..847
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 923..941
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 113..361
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 411..906
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
SQ SEQUENCE 983 AA; 111242 MW; 90CC797C25BB8FFF CRC64;
MAKRRSTTSQ PDIRIRSDSQ SSLLRRRSIT EVYPKPSLFG GQDLLLDPLY SIQPLQVGNH
PENNPIHNVR EVLEGHEKEV PLIYTEMLHL EKDGKKSKQW KQVARWIKYE QTVEGDGTRF
SKPHVTLLSV ISIIQLKNCL RKGVILLDIE ANSFEEVTDQ LCAAWMERGM LESESSTCIK
DLLRSPKYHL IGNSMRSSTE IRKAITTFAT DRLEWNSDVN HVINKRLSEG ENEGEQEESM
YDVSLREMKK LAEGTEGAAI MSAIFSGLDR PICAFLRLEK AKVFYPEMPN IPVPLRFVFV
LISPHDHYTN ETRAIGRTMG ALFSDEIFRK VAHCSLEPYT IADALEEFFV QVVAIPPGNC
STETRWEPNT DSDQVARSVG MLYASYDDPF DEEPELEHKK EMHNDIVRTG RCFGGLCDDI
KRKAPFFVSD FSDFFRGRWS QSFAAFIFLF FANITSIITF GAVMERALHH QMAAIENIIC
GGISGVIFAL FSGQPLNILS ATGPTLVFET ILFDFCLANG WEFLPFRFWV AVWIGVVLLI
LVATDMSALV GLITRFTEEA FAALISIVFI IQSFEKLVEI SHDAPIITDP KSVFDSPCVC
YLNESVALGF NSTMQQKLMD IDAEDCIKRG GEAFGLQCHF KPDVYMLSIL LTFGTFALAY
GLNIFRRTPF LTFTIRNSIS DFGVFIAIVV MTAVSKFIGL DLPVLHIPLN FRPTTDRPWL
INFLSVDWYV ALFAALPAVF YAILIIMDQQ ITAVIINRKD NKLRKGYGYH LDLLVIAVLV
VICGSLGLPF YVAATVLSVM HVDSLRLQSD TSAPGEKAQF LGVREQRLTA IIAHLLIGFS
VFITPVIKLV PLPVLIGIFL YMGVVSMLGL QFIQRIAMLF MPIKYQPDYV WLRLVRMKRV
HLFTCIQILS IVGLFAVKYM PSFSMMFPLM LVLMVLIRMF CLEKIFSKQE LIALDDPVPS
FHSVVSAKQQ YNRGIFFLNS ILF
//
