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Database: UniProt
Entry: A0A2A3EHC5_APICC
LinkDB: A0A2A3EHC5_APICC
Original site: A0A2A3EHC5_APICC 
ID   A0A2A3EHC5_APICC        Unreviewed;      1116 AA.
AC   A0A2A3EHC5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   ORFNames=APICC_05420 {ECO:0000313|EMBL:PBC30692.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC30692.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC30692.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC30692.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KZ288255; PBC30692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EHC5; -.
DR   STRING; 94128.A0A2A3EHC5; -.
DR   Proteomes; UP000242457; 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   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:UP000242457};
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        574..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        616..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        659..684
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        691..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        779..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        817..833
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        866..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        908..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        968..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        994..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1040..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1064..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          224..483
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          545..1046
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  125227 MW;  A30145EC997D513C CRC64;
     MDNGLSPTSM QNADDETTEE MENVVSSESE APISERAASG FSDSPTVGSP RVQFEKIKEE
     EVHHSFKKDE VPSVGASANH DEDRKCRRHQ KHEHKRHHHK SRKYSLQEDP QWRKRSGAGL
     PDGPGVLARR VSVQPEEAST LQELDIDDLE SHRSDDPRGM RRHKAAHSTV QIGRKKEGGI
     PHDTFKKMYD HSPHEVFVQL DELYGVGEER EWRETARWIK YEEDVEEGAD RWGRPHVASL
     SFHSLLNLRR CLETGVVLLD LEEKDLPGLV YRVVEQMVIE ELILPEDRPV VMRALLLRHR
     HVHDHDRGFR FGGKRNYASY TSLQNLNDAK PKIVSSNLAL DSNHTVVDMK EELTYTSSNE
     DLKKSHNDYI LKRIPAGAEA TVVLVGAVDF LDQPTIAFVR LAEGVFIPSI TEVTIPVRFM
     FTLLGPRNAD LDYHEIGRSI ATLMANTSFH KVAYKANERR ELLSAINEFL DDSIVLPPGD
     WERQALLPFS ELKAKSEAIR KRKAKALEEK SKPVQSEAAV KKALLAGEEE KKAADDDDPL
     RRTKRPFGGL INDIKRRYPF YLSDFTDGLS SSCLAAAIFM YFAALCTAIT FGGLMSDKTH
     NVIGISETLV SGSWTGVVMA LFSTQPLVII GTTGPLLLFD ESLYNFCLAN ELEFLTVRVY
     VGAWMGIIAL AIACVEGSVL VRLFTRFTEE IFTGLISILY IVETFIKLYN YFVKNPLLDE
     YSFIPETNRT FYQEQPLNVT EIDVVSPKTG ETIGIPLSKP QTLIPAHNAA GILINQPNTA
     LMCTILCLGT FLGAYYLRIF RNSHYLGRSA RRAFGDFGVP ISIVVFALID YLAKVKTEKL
     LVPEGLTPTQ PGRNWIVSPA GVHKPIPLWM AMACIVPALL VYILVFMETQ ISELIIDKKE
     RKLRKGNGYH MDIVVVCLMN VGCGLMGAPW CCAASVRSLT HVSAVTVMSR THAPGDKPHI
     VEVKEQRVSA LLVAVLIGVS VLMAPLLRRV PMSVLLGVFL YMGISSTNGV QLFDRVKLFF
     MPVKHHGTAN YVRRVQTYKM HIFTLIQILC LAILWIVKST RAALALPFFL ILMIPLRGQM
     NHFFTAAELR ALDSKGSEHE STEDEPDFYE EAPLPG
//
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