ID H3CTY4_TETNG Unreviewed; 1199 AA.
AC H3CTY4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000011718.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000011718.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; H3CTY4; -.
DR STRING; 99883.ENSTNIP00000011718; -.
DR Ensembl; ENSTNIT00000011906.1; ENSTNIP00000011718.1; ENSTNIG00000008866.1.
DR GeneTree; ENSGT00940000159765; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; H3CTY4; -.
DR OMA; KSINTHK; -.
DR TreeFam; TF313630; -.
DR Proteomes; UP000007303; 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; 2.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 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:UP000007303};
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 690..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 724..755
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 775..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 807..825
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 860..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 898..915
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 949..970
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 991..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1077..1096
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1128..1155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 381..599
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 662..838
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT DOMAIN 855..1128
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 67..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 135672 MW; DC250B5758B35F3A CRC64;
KEDEENLEKA LSVERFGDII SDSASPSGDR MGRNYTEKDF EYHRHTFHHT HHPLSTHLPL
PQRLRKRVHS MDRWRKKKRK KKKTSLPPSD VTPTIHEVDE EEEAQSDTDG QGVSATPTET
PDIQPQFSLG SQEDLEEPPP LTTFHVENEH LLTKKAASMQ IQAETHNGKI PLLGQNEEDD
GEETACSSVP QQSDPSASNT THSCFRKRAV HHRLAGTQRS NYDLRERICI GSMTALEMAV
YQQVPTDEAE AQMLASADLD DMKSHRFEDN PGVRRPSGCQ ISRASNSSTP LSSLKKKKRA
ADKKTHELFV ELNGNRWCLT KYMNDQWRKC VAFSIHLKHH IKKVERGFFG FFCSSSKKEY
FGVLRFLCDN PKPKQSLLAS RSVVLVKIIG CDIVKPEQIS NITKHLITKH SHPSDLKHRF
HRLQSSTSLH GSFNHNHVQD TNLPLVTEEH DAVSVMWLHY WSPYVPKSLH PLPPEGHPAA
ARSMKLLAKI PKDAEAVIVL VGCVEFLQQP AMAFVRLNEA VLLESVLEVP VPVRFLFVLL
GPSQSNVDYH EIGRSFSTLM SDKSFHEVAY FADNRQDLLN GINEFLDYSI VIPPSDIEGK
DLLKTVVEFQ KQMLRKRKER ELKKNHSFTA YGACKHILEI SPCEEEEEGD EEVDPLKRSG
IIFGGLIHDI RRRYPHYVSD LKDALDTQCI AAVIFIYFAA LSPTITFGGL LGEKTEGMMG
VTELIVSTAT LGVIFSLLAG QPLLIIGFSG PLLVFEEAYF KFCQAYNYEY LTGRVWIGFW
LIFIVLVIVA AEGSFLVRYI SPFTQEIFAF LISLIFIYET FSKLIKVFKE HPLMSVYPND
TTMAYGFHDD HLALLNQPNT ALLSLVLMIG TFFLAFFLRK LRNSRFLGGK ARRIIGDFGI
PISILVFVMI DYSVPDTYTQ KLNVPAGFSV TSPDKRNWFI SPFGDKQPFP TWMMGASVVP
ALLVFILIFM ETQITSLIVS KKERRLVKGS GFHLDLLLIV ILGAICPLFG LPWLTAATVR
SVTHVNALTV MSKATAPGEK LKIQEVKEQR LTGLLVAVLV GMSVVMTRVL RLIPLAVLFG
IFLYMGVTSL TGIQLYERIT LMVTPAKHHP DRIYVTKVKT WRMNMFTLAQ LGCIVALWVV
KSTTASLAFP FILIMTPLRR LILSRIFEER ELQALDCDED SPNFDEDGRD EYNEIHMLV
//
