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Database: UniProt
Entry: A0A3Q0GIZ6_ALLSI
LinkDB: A0A3Q0GIZ6_ALLSI
Original site: A0A3Q0GIZ6_ALLSI 
ID   A0A3Q0GIZ6_ALLSI        Unreviewed;      1090 AA.
AC   A0A3Q0GIZ6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-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|RefSeq:XP_025058158.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025058158.1};
RN   [1] {ECO:0000313|RefSeq:XP_025058158.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: 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_025058158.1; XM_025202373.1.
DR   AlphaFoldDB; A0A3Q0GIZ6; -.
DR   Proteomes; UP000189705; Unplaced.
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: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; IPR003024; Na/HCO3_transpt.
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; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
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:UP000189705};
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        484..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        513..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        571..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        601..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        699..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        737..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        785..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        825..849
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        885..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        911..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        969..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          141..407
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          455..963
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1017..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..71
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  122308 MW;  1BDD63386DBE3B93 CRC64;
     MERTHSGKKL LPGHDEEAVV DMGKTSSTVN TNFEKEELES HRAVYIGLHV PFGKSGRRRH
     RHRGHRHHRR KKDKETDQDD GRESPSYDTP SQRVQFILGT EDDDEEHIPH DLFTEMDELC
     FRDGGECEWK ETARWLKFEE DVEDGGDRWS KPYVATLSLH SLFELRSCIL NGTVMLDMRA
     NTLDEIADMV LDNMIASGQL DESRRENVRE ALLKRHHHQN EKKFSSRIPL VRSFADIGKK
     HSDPHLLDRN GLLASPQSAP GNLDIGKNVD VKGNGTGGSR ENSTVDFSKV DMNFMRKIPT
     GAEASNVLVG EVDFLERPII AFVRLAPAVL LSGLTEVPVA TRFLFLLLGP AGKGPQYHEI
     GRSIATLMTD DVFHDVAYKA KDRNDLLSGI DEFLDQVTVL PPGEWDPSIR IEPPKSVPSQ
     EKRKLPKFPN GSTPTGETLK EEGHHAGPEL QRTGRLFGGL MLDIKRKTTF FLSDFKDALS
     LQCLASILFL YCACMSPVIT FGGLLGEATQ GRISAIESLF GASLTGIAYS LFAGQPLTIL
     GSTGPVLVFE KILFKFCKDY GLSYLSLRTS IGLWTSFFCI LLVATDASSL VCYITRFTEE
     AFAALICIIF IYEALEKLFH LGEVYAFNMH NDLDKLTSYS CVCSEPQNPS NDTLQLWAKS
     NKSVDTITWS NLTVLECKAF KGAFLGSACG HQGPYIPDVL FWSVILFFTT FFLSSFLKQF
     KTKRYFPTKV RSTISDFAVF LTIMIMVLID YLVGVPSPKL LVPEKFEPTS KDRGWFIDPL
     GNNPWWTLLV AAVPALLCTI LIFMDQQITA VIINRKEHKL KKGCGYHLDL LVVGVMLGIC
     SLMGLPWFVA ATVLSISHVN SLKVESECSA PGEQPKFLGI REQRVTGLMI FVLMGLSVFM
     TSVLKFIPMP VLYGVFLYMG VSSLKGIQFF DRIKLFGMPA KHQPDLIYLR YVPLWKVHIF
     TVVQLTCLIL LWVIKASAAA VVFPMMVLAL VFIRKLMDLC FTKRELSWLD DLMPESKKKK
     EDDKKKKEKE EAEQMLHAGD SESMHLPYGG GNILTIPVKP MKYSPEKPES VQINMEGSSG
     MKYVDAETSL
//
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