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Database: UniProt
Entry: A0A226NP93_CALSU
LinkDB: A0A226NP93_CALSU
Original site: A0A226NP93_CALSU 
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
//
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