ID A0A2K5YKA2_MANLE Unreviewed; 1223 AA.
AC A0A2K5YKA2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A2 {ECO:0000313|Ensembl:ENSMLEP00000015993.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000015993.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000015993.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. 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}.
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DR RefSeq; XP_011839736.1; XM_011984346.1.
DR AlphaFoldDB; A0A2K5YKA2; -.
DR Ensembl; ENSMLET00000039459.1; ENSMLEP00000015993.1; ENSMLEG00000032141.1.
DR GeneID; 105542704; -.
DR CTD; 6522; -.
DR GeneTree; ENSGT00940000158259; -.
DR OrthoDB; 1013180at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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:0022853; F:active monoatomic ion transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:UniProt.
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 GO; GO:0098660; P:inorganic ion transmembrane transport; IEA:UniProt.
DR Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR InterPro; IPR001717; Anion_exchange.
DR InterPro; IPR002978; Anion_exchange_2.
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 NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF14; ANION EXCHANGE PROTEIN 2; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01188; ANIONEXHNGR2.
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.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
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 691..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 733..756
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 776..801
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 808..826
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 883..900
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 973..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1013..1037
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1073..1092
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1098..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 334..601
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 662..1151
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 135040 MW; B0FFCD47D2DF37DE CRC64;
MTQPEPESLG PGTPGFPEQE EDELHRTLGV ERFEEILHEA GSRGGEEPGR SYGEEDFEYH
RQSSHHIHHP LSTHLPPDAR RRKTPQGPGR KPRRRPGASA TGETPTIEEG EEDEDEASEA
EGARAVTQPS PASTPSSVQF FLQEDDSADR KAERTSPSSP APLPHQEATP QASKGAQAGT
KVEEAVVVAS GTAGGDDGGA SGRPLPKAQP GHRSYNLQER RRIGSMTGAE QALLPRVPTD
ESEAQTLATA DLDLMKSHRF EDVPGVRRHL VRKNAKGSTQ SGREGREPGP TPRARPRAPH
KPHEVFVELN ELLLDKNQEP QWRETARWIK FEEDVEEETE RWGKPHVASL SFRSLLELRR
TLAHGAVLLD LDQQTLPGVA HQVVEQMVIS DQIKAEDRAN VLRALLLKHS HPSDEKDFSF
PRNISAGSLG SLLGHHHGQG AESDPHVTEP LIGGVPETRL EVERERELPP PAPPAGITRS
KSKHELKLLE KIPENAEATV VLVGCVEFLS RPTMAFVRLR EAVELDAVLE VPVPVRFLFL
LLGPSSANMD YHEIGRSIST LMSDKQFHEA AYLADERDDL LTAINAFLDC SVVLPPSEVQ
GEELLRSVAH FQRQMLKKRE EQGRLLPTGA GLEPKSAQDK ALLQMVEAAG AAEDDPLRRT
GRPFGGLIRD VRRRYPHYLS DFRDALDPQC LAAVIFIYFA ALSPAITFGG LLGEKTQDLI
GVSELIMSTA LQGVVFCLLG AQPLLVIGFS GPLLVFEEAF FSFCSSNHLE YLVGRVWIGF
WLVLLALLMV ALEGSFLVRF VSRFTQEIFA FLISLIFIYE TFYKLVKIFQ EHPLHGCSAS
NSSEVDGGEN MTWAGARPTL GPGNRSLAGQ SGQGKPQGQP NTALLSLVLM AGTFFIAFFL
RKFKNSRFFP GRIRRVIGDF GVPIAILIMV LVDYSIEDTY TQKLSVPSGF SVTAPEKRGW
VINPLGEKSP FPVWMMVASL LPAILVFILI FMETQITTLI ISKKERMLQK GSGFHLDLLL
IVAMGGICAL FGLPWLAAAT VRSVTHANAL TVMSKAVAPG DKPKIQEVKE QRVTGLLVAL
LVGLSIVIGD LLRQIPLAVL FGIFLYMGVT SLNGIQFYER LHLLLMPPKH HPDVTYVKKV
RTLRMHLFTA LQLLCLALLW AVMSTAASLA FPFILILTVP LRMVVLTRIF TEREMKCLDA
NEAEPVFDER EGVDEYNEMP MPV
//
