ID A0A3B4X2D9_SERLL Unreviewed; 753 AA.
AC A0A3B4X2D9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chloride anion exchanger {ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Solute carrier family 26 member 3 {ECO:0000256|RuleBase:RU362052};
GN Name=SLC26A3 {ECO:0000313|Ensembl:ENSSLDP00000010381.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000010381.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000010381.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mediates chloride-bicarbonate exchange with a chloride
CC bicarbonate stoichiometry of 2:1 in the intestinal epithelia. Plays a
CC role in the chloride and bicarbonate homeostasis during sperm
CC epididymal maturation and capacitation.
CC {ECO:0000256|RuleBase:RU362052}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|RuleBase:RU362052}.
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DR AlphaFoldDB; A0A3B4X2D9; -.
DR STRING; 1841481.ENSSLDP00000010381; -.
DR Ensembl; ENSSLDT00000010757.1; ENSSLDP00000010381.1; ENSSLDG00000008256.1.
DR GeneTree; ENSGT01070000253775; -.
DR OrthoDB; 1067648at2759; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0098661; P:inorganic anion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR00815; sulP; 1.
DR PANTHER; PTHR11814:SF19; CHLORIDE ANION EXCHANGER; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|RuleBase:RU362052};
KW Chloride {ECO:0000256|RuleBase:RU362052};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}; Transport {ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 73..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 166..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 366..383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 461..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 516..709
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 734..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83647 MW; A94E06D134047A81 CRC64;
MMRPGAKQYV VARPLYSEET FAEKHEKVYR QRKTMLNHIK QYFTCDAKRA KNAALSLLPV
IGWMKIYRVK EWLLSDIVSG LSTGLVAVLQ GLAYCLLASL PPWYGLFSAF FPVIMYFFLG
TSRHISVGPF PVLCLMIGSV VTRLVPDEGP PVNITGFEGL TRDEQRVLVA SSVTFLAGIM
QLAMGVFQVG FVVMYLSDTL VSGFTTAAAI HILVSQLKFV LGLQVPGISG PLSIIYTLEI
IINKITSTNV CDVVISLVIM VVVFIVKELN DRFKSKLPVP IPIEVIMTVI ACGVSYAFDF
KTKYGIDVVG HIPKGYEPPM APNLHIFQDT AVEAFPMAIV GFAVAFSVAK VYSVKHDYTI
DGNQELIAFG VSNIFGASFK SFAASTALSR SAVQESTGGK TQIAGLLSAI IVMIVTLAIG
FLLEPLPKSV LGAVVIVNLK GMLMQFRDVP YLWRRDKPDC IVWLGTCIAA ILLGLDLGLA
AGLGVELLSV VLRAQFPRCS VLANIKGTDI YKDRKDYIDI YEQEGVKIFR IPSPIFFANI
DFFRSKLVEA VGFNPLRVLR KRNKALRMIR KLLKKGDLQW TCNGLLNTSC RPIKESEDES
NMEELDLPTD FKDLPTRIDW NADLPGNISV PRVEVHSLIL DFAAVSFLDI SALKGLKTSL
KELIRVEVEV YIVACDPYIL EKLHHCCFFD DEVQPSMFFL TLHDAMLHIL EKHPESTEKK
SNCEKIITTV TVHHPGGSLR STDRNVPDRE TRF
//