ID A0A452GF79_9SAUR Unreviewed; 929 AA.
AC A0A452GF79;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000000190.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000000190.1}
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: 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 AlphaFoldDB; A0A452GF79; -.
DR STRING; 38772.ENSGAGP00000000190; -.
DR Ensembl; ENSGAGT00000000219.1; ENSGAGP00000000190.1; ENSGAGG00000000163.1.
DR Proteomes; UP000291020; 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; 2.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF12; BAND 3 ANION TRANSPORT PROTEIN; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 2.
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 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:UP000291020};
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 430..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 472..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 515..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 547..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 588..605
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 677..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 719..742
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 800..821
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 851..868
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 874..892
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 104..349
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 402..578
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT DOMAIN 582..856
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 105008 MW; 026E66445B984A20 CRC64;
MSKKAVVDPG QEDYEAEIGR RLDEEGYRDS ELKQSEMSLD EQSRSSSLDQ IQEASGRAGA
AHPSTSSQGT HEAYVELHEL VMDRNNELRW MEAGHWIKLE EDFEEAGHWG RPHLSYLTFH
SLLEVHKAFT KGTILLDLPE KFLAGITNQL IDRMISEGQL KSQDKETIRR TLLLQHSHPD
GSESLGTLSP GQLERKDTKD EVTSEPLMQE YHQIEMQTFT GTEQEGPQRQ AFRKPLLDKI
AEDAEATLVL VGRATFLDHP TLAFVRLKEA VELDLVLQVP VPVRFLFMVL GPDSPHISYH
EIGRAVSTMM AERGFRRDAY LAEGRQDLIK GLEEFLDCSI VLPPCEIQDE RLLRSLVPMQ
KELLRKRYLP DKKKPETRTL KDLEKDHEEE EDDDPLRRTG WPFGGLVRDI KRRYPKYLSD
IKDALNAQCL AAVIFIYFAA LSPAITFGGL LGEKTSNLIG VPELLISTAA QGIIFCLLGA
QPLLVVGFSG PLLVFEEAFF KFCENYGMEY IVGRVWIGFW LILLVLLVVA FEGSFLVRYI
SRYTQEIFSI LISLIFIYET FAKLITIFKK HPLRKTYGST DEPKPNTALL SLVLMAGTFF
IAFFLRKFKN SAFFPGKLRR VIGDFGVPIS IFIMALADFF IKDTTDTQKL SVPKGLEVSN
TTARGWFIHP LGKNRDFPIW MMFGAALPAL LVFILIFLES QITTLIVSKP ERKLVKGSGF
HLDLLLIVGM GGIAALFGMP WLSATTVRTI SHANALTVMV KTTTPGEKAQ VQEVKEQRIS
GLLVSILVGL SILMEPVLKL IPLAVLFGIF LYMGVTSLNG IQLYDRILLL LMPPKYHPEE
PYVKRVKTWR MHIFTLTQIV CLATLWAVKS TPASLALPFV LILTVPLRRF LLPKIFSDIE
LKCLDAEDAN VTFDETEGRD VYHEVQMPI
//
