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Database: UniProt
Entry: G5AXG3_HETGA
LinkDB: G5AXG3_HETGA
Original site: G5AXG3_HETGA 
ID   G5AXG3_HETGA            Unreviewed;      1085 AA.
AC   G5AXG3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   ORFNames=GW7_02881 {ECO:0000313|EMBL:EHB01724.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB01724.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB01724.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
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   EMBL; JH167395; EHB01724.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5AXG3; -.
DR   STRING; 10181.G5AXG3; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   InParanoid; G5AXG3; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
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:SF20; ELECTROGENIC SODIUM BICARBONATE COTRANSPORTER 4; 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:UP000006813};
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        450..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        484..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        535..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        568..591
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        671..690
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        702..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        757..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        795..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        857..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        882..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        952..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          76..343
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          421..935
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          157..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1015
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1085 AA;  120914 MW;  CCCE3E52B38EFCE9 CRC64;
     MKVKEKVGVG KLDSAKYRRR CLDGGSPAAE QLQDILGEED EAPNPTLFTE MDTLQHDGDQ
     MEWKESARWI KFEEKVEEGG ERWSKPHVST LSLHSLFELR TCLQTGTVLL DLDRGSLPQI
     IDDVIEKQIE DGLLRPELRE RVSYVLLRKH RHQTKKPIHR SLVDIGKSVS STTSRSPARS
     PAAGPSLRRS TEDLRIRQSA NYGHLCHAQS RSMNDISHNP NTDQRKNKFM KKIPKDSEAS
     NVLVGEVDFL DQPFIAFVRL IQSAMLGGVT EVPVPTRFLF ILLGPSGRAK SYNEIGRAIA
     TLMVDDLFSD VAYKARNRDD LIAGIDEFLD EVIVLPPGEW DPNIRIEPPK KVPSADKRKS
     VFSPAELGQM NGTVGGGGVS AGGGGNGSGA GGSGASGTSG GDDAEMPAAH EIGEELIWTG
     RFFGGLCLDV KRKLPWFLSD FCDGFHIQSI SAILFIYLGC ITNAITFGGL LGDATDNYQG
     VMESFLGTAM AGSLFCLFSG QPLIILSSTG PILIFEKLLF DFSKGNGLDY MEFRLWIGLH
     SAIQCLILVA TDASFIIKYI TRFTEEGFST LISFIFIYDA IKKMIGAFRY YPINMDFKPD
     SITTYKCECI APDPVNTTVF NASAPLAPNT NNSLYNSLNL TALDWSLLSK KECLSYGGHL
     LGNSCQFIPD LALMSFILFF GTYSMTLTLK KFKFSRYFPT KVRALVADFS IIFSILLFCG
     IDACFGLETP KLHVPNVIKP TRPDRGWFVA PFGKNPWWVY LASILPALLV TILIFMDQQI
     TAVIVNRKEN KLKKAAGYHL DLFWVGILMA LCSFTGLPWY VAATVISIAH IDSLKMETET
     SAPGEQPQFL GVREQRVTGI IVFILTGISV FLAPILKYIP MPVLYGVFLY MGVASLNGIQ
     FWERCKLFLM PAKHQPDHAF LRHVPLRRIH LFTLVQILCL AVLWILKSTV AAIIFPVMIL
     GLIFVRRLLD FIFSQHDLAW IDNILPEKEK KETDKKKRKG AHEDSDEEEK DLPVGVTHSD
     SSFTGSELDR SITLHFKISC PASPAFSYSR NPVFMVPQVK IEMESDYDFT DVDEYVREAD
     GETTL
//
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