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Database: UniProt
Entry: A0A3Q3CXT0_HAPBU
LinkDB: A0A3Q3CXT0_HAPBU
Original site: A0A3Q3CXT0_HAPBU 
ID   A0A3Q3CXT0_HAPBU        Unreviewed;      1253 AA.
AC   A0A3Q3CXT0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A7 {ECO:0000313|Ensembl:ENSHBUP00000033153.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033153.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000033153.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_014190766.1; XM_014335280.1.
DR   AlphaFoldDB; A0A3Q3CXT0; -.
DR   Ensembl; ENSHBUT00000026717.1; ENSHBUP00000033153.1; ENSHBUG00000019916.1.
DR   GeneID; 102290413; -.
DR   GeneTree; ENSGT00940000157045; -.
DR   OrthoDB; 1013180at2759; -.
DR   Proteomes; UP000264840; Unplaced.
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; 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:SF105; SODIUM BICARBONATE COTRANSPORTER 3; 1.
DR   Pfam; PF07565; Band_3_cyto; 2.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
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:UP000264840};
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        606..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        693..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        723..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        821..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        859..877
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        907..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        947..971
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1007..1026
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1033..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1084..1115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          142..280
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          378..528
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          577..1085
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..69
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1253 AA;  139802 MW;  A6CC10882470C503 CRC64;
     MDEQNEGEHV LTGLDEEAIV DHGKTSFATL SNHEKDDFES HRAVYVGVHV PLGRESKRRH
     RHRGHKQRKK KNRDSEEGKE DGRDSPTYDT PSQRVQFILG TEDDDLEHVP HDLFTEMDEL
     SFRDGTATEW RETARWLKFE EDVEDGGERW SKPYVATLSL HSLFELRSCI LNGTVLLDMR
     ASSIEEIADM VIDSMVASGQ LKEDLRDKVR EAMLKKHHHQ NERKLSNRIP LVRSIADIGK
     KHSDPLLLEK NGEGLSSSRL SLHKPGTASS VSNLSQRRES RVSVLLNHLL PSSSSNTGLF
     PGPSPFTTPQ ALRRSQSPSH RQGVVLGPQG IPEVVVSPPE DEDPPEEEAV SPQLSRRASS
     ASQSVELLPL EGPLVSQNSV PNNLDSNKAM DRRPSKVGVS RESSSVDFSK VDMNFMKKIP
     PGAEASNVLV GEVDFLEKPI IAFVRLSPAV LITGLTEVPV PTRFLFLLLG PHGKGPQYHE
     IGRSMATLMT DEIFHDVAYK AKDRTDLLSG IDEFLDQVTV LPPGEWDPTI RIEPPKNVPS
     QIKRKIPLQP NGSAPPAGEL EKEEDHHAGP ELQRTGRIFG GLVLDVKRKA PFYWSDIRDA
     LSLQCLASVL FLYCACMSPV ITFGGLLGEA TKGNISAIES LFGASLTGVA YSLFAGQPLT
     ILGSTGPVLV FEKILFKFCK DYSLSYLSLR TSIGLWTAFL CILLVATDAS SLVCYITRFT
     EEAFAALICV IFIYEALEKL FHLGELYPVN MHNSLDNLTL YSCQCSPPAN ATDEVMQKWN
     QSGYSPDSIE WSSLSVSTCK LLHGDFVGPA CGHHGPYIPD VLFWSVILFF TTFFLSSFLK
     QFKTERYFPT RVRSTISDFA VFITIMIMVL VDYLMGIPSP KLNVPDRFEP TSKNRGWLMD
     PLGENPWWTL LVAVLPAMLC TILIFMDQQI TAVIINRKEH KLKKGCGYHL DLLLVAIMLG
     VCSIMGLPWF VAATVLSISH VNSLKVESGC SAPGEQPKFL GIREQRVTGF MIFVLMGCSV
     FMTSVLKFIP MPVLYGVFLY MGVSSLKGIQ FFDRIKLFGM PAKHQPDLIY LRYVPLWKVH
     IFTLIQLSCL VLLWVIKVSA AAVVFPMMVL ALVFIRKLLD FFFTKRELSW LDDLMPESKK
     KTEDDKKKKA REKLDEESGL EEEEEMGIKD TYEDSNRLKI PVKELSGSSD TDPLVVNISD
     EMAKTAVWKA VNSSAESCVQ PVKLSGSQEK VACVRVDVSP DTPGRDSTTE TFL
//
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