ID A0A226NP93_CALSU Unreviewed; 1371 AA.
AC A0A226NP93;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN ORFNames=ASZ78_011358 {ECO:0000313|EMBL:OXB69238.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB69238.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB69238.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB69238.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB69238.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) 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}.
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:OXB69238.1}.
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DR EMBL; MCFN01000003; OXB69238.1; -; Genomic_DNA.
DR STRING; 9009.A0A226NP93; -.
DR Proteomes; UP000198323; 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; 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:SF15; ANION EXCHANGE PROTEIN 3; 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.
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 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:UP000198323};
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 856..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 890..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 941..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 973..991
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1032..1049
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1069..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1120..1141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1162..1185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1222..1241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1248..1267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1300..1328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 467..731
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 828..1300
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 154534 MW; 80ADE906B8BFD913 CRC64;
MAAGESLPVG DAFIDLQQGR DRAEKASPGA EDDEDLDKTL SIERFGDLIS KSASSDLEKQ
RRSYSERDFE FHRQTSHHIH HPLSTHLPSA LKFQKRPPRA SRRKKRRRKK KKTSVPPSEV
TPTIQEVDEE GGEEEEEEEE EEEEEGESEA EETQEKEVFA ESEGEARGKN SSPKLEPPSK
PKARLGHPCL SWAWRLGKAF TIGSDEDESG STLAPAQFHV EEECGILSST SRFTDLLQDK
GPTSPRSLPG PRERLSQGWE KRKPWGQVAS GQRVTYDLKE RMCIGSMTTL ESAAYQRVPT
DEAEAQMLVS ADLDGMKSED NMSILQEGEE AARELEVSSS PEVAVSARVR NSLSYEDFDE
FAFNFEDYDL WEAIRNHLGY PGGEPTCHRF EDNPGVRRHL MKKPSRSQVT RASKKLASTP
SVKKKKKKKK LDRKPHEVFV ELNELVVDKN QEMHWRETAR WIKFEEDVEE DTARWGKPHV
ASLSFRSLLE LRKTIAHGAV LLDLEQTTLP GIAHLMVETM IISDQIRAED RANVMRALLL
KHSHPNDEKE GFFPRNHSSS SMNSIVGNHH HNHTTDTCVP LMGEERIEMA DPKAHETECK
EKNVHVHNSE GHRKYLKLME KIPEDAEATV VLVGCVQFLE QPTMAFVRLN EAVFLESVLE
VPIPVRFIFV LLGPSQANMD YHEIGRSIST LMSDKLFHEA AYMADDRQDL LNAINEFLDC
SIVIPPSEVE GKDLLKSIAT FQKLMLRKRK EREQKSMKEG DVQEAKGLST YIWAKEFVPS
ALYAPVGPPL QSLAEGPALH APPELCEVKA EEEEEEAEDD PLKRTGIFFG GLVRDIKRRY
PKYLSDIRDA LHSQCLAAVL FIYFAALSPA ITFGGLLGEK TEGLMGVSEL IISTSVLGIL
FSLLGAQPLL VIGFSGPLLV FEEAFYKFCQ TQGIEYLTGR VWIGLWLIVF IFIIVAAEGS
FLVRYISPFT QEIFAFLISL IFIYETFYKL YKVFAEHPLL KFYPPDVQSS LNSSMLSADA
VSLGIRMQPN TALLSLILML GTFFIAFFMR KFKNSRFLGG KARRIIGDFG IPISILVMVL
VDYTITDTYT QKLNVPSGLS VTSPHKRGWF IHPMGSSGTF PLWMMFASAI PALLVFILIF
METQITTLIV SKKERKLLKG SGFHLDLLLI GTMGGLCALF GLPWLTAATV RSVTHVNALT
VMSKAIAPGE KPKIEEVKEQ RVTGVLIAAL VGLSIVMGNM LRQIPLAVLF GIFLYMGVTS
LTGIQLYERL LLIFMPSKHH PDHIYVVKVK TWRMNLFTCI QLACIVLLWV VKSTVASLAF
PFVLIMTVPL RRFVLPRFFH DRELKALDSE DAEPNFDEDG RDEYNELHMP V
//