ID T1G3A7_HELRO Unreviewed; 927 AA.
AC T1G3A7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=20215555 {ECO:0000313|EnsemblMetazoa:HelroP78329};
GN ORFNames=HELRODRAFT_78329 {ECO:0000313|EMBL:ESO05115.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP78329, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO05115.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP78329}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362035}.
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DR EMBL; AMQM01004077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB096411; ESO05115.1; -; Genomic_DNA.
DR RefSeq; XP_009017048.1; XM_009018800.1.
DR AlphaFoldDB; T1G3A7; -.
DR STRING; 6412.T1G3A7; -.
DR EnsemblMetazoa; HelroT78329; HelroP78329; HelroG78329.
DR GeneID; 20215555; -.
DR KEGG; hro:HELRODRAFT_78329; -.
DR CTD; 20215555; -.
DR eggNOG; KOG1172; Eukaryota.
DR HOGENOM; CLU_002289_5_1_1; -.
DR InParanoid; T1G3A7; -.
DR OMA; WWTILAS; -.
DR OrthoDB; 1013180at2759; -.
DR Proteomes; UP000015101; 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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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:SF36; ANION EXCHANGE PROTEIN; 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:UP000015101};
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 361..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 415..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 579..597
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 609..633
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 665..684
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 705..729
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 765..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 791..810
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 51..289
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 332..843
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 112..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 105832 MW; 890C9A49D42334B8 CRC64;
MKFKWEPLIT ASLLHNNHCL FTQMDVLCHF RDDTFAWKEA ARWLKYEEKV EIGGRWSKPH
VTTTSLHAIL QLREAITSGR CMLDMQLNVP CPNLTGLNLF KTDSIRKLRH ILTQPHKHKN
RKGERKRKIN NNNNNNNNNN KNNNNINKEN NDANDINNAN KTTNKKLSLP NRKLMKKIPN
KTETASILIG QVDFLNEPII ALFRLKSTNV VEELCEVALP TRFVALAIGP FKKMTIGECN
EIGRAMAALF NDKVFCEVAY NAYTAHDILT GIDEYLDDLT VLPPSIWDPC ARLEPPVNTK
TKVLMMMEEV LNDDVIDESL IRTGRIKNPE YRLFGGLVAD VKRRFRYFLS DIRDGLHVQC
IASIIFLYFA CITPIVTFGG LMGRKTDNYM GTMETLTSAA VCGCFYALFS GQPLTIIGAT
GPLLVFESIL YHLCKENRID FLSFRCWIGL WSFVYLLIIV AFDLSSYVRY ITRFTEESFA
VLISLIFIVE AFSKIFEIWH THPVLLRREA IYTNTGTSLQ LDPSENDVNL SRDDVDMSRD
LLYGNDEGCL TKDDCQSANW TTLGAVCDND NYVSAVPDVF LLSFLLFFGT FSIAFTLRTF
RNSPFFPSLI RNLLGDFAVF LSIVAMTVVD YFFGLDTPKL EVPNEFKPTL PDRGWLVNPL
KINHWWLILV ATFPGLLATI LISLDQQITA VIINRKEHKL KKGHGYHLDL FVLAILIAIC
SFLGLPWFVA ATVRAITHVK SLIRESEVKI PGERPQMLGV REQRVTGFLI HLFIGFSTLL
TSVLRLVPMP VLYGVFLYMG ITSLGDVQFV ERVLLLFMPI KHQPDCIYLR HVKTRNVHSF
TLIQIGCSVL MWSIKSIQAT SIGFPLVLIA LIVTRKVMDL LFSQRDLYWL DNLLPDNKRR
KSEDLKKHLD AIDLQVILII NQTNNFE
//
