ID A0A2I3S6V3_PANTR Unreviewed; 735 AA.
AC A0A2I3S6V3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:ENSPTRP00000072721.1,
GN ECO:0000313|VGNC:VGNC:8759};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000072721.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000072721.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000072721.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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|ARBA:ARBA00008692, ECO:0000256|RuleBase:RU362052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACZ04028340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC190236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3S6V3; -.
DR Ensembl; ENSPTRT00000077141.1; ENSPTRP00000072721.1; ENSPTRG00000022537.5.
DR VGNC; VGNC:8759; SLC26A3.
DR GeneTree; ENSGT01070000253775; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000022537; Expressed in skeletal muscle tissue and 1 other cell type or tissue.
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:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
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; PS01130; SLC26A; 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 Reference proteome {ECO:0000313|Proteomes:UP000002277};
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 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 104..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 206..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 373..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 410..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 468..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 510..688
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 735 AA; 81337 MW; 1F70272DFB0A2A61 CRC64;
MIEPFGNQYI VARPVYSTNA FEENHKKTER HHKTFLDHLK VCCSCSPQKA KRIVLSLFPI
ASWLPAYRLK EWLLSDIVSG ISTGIVAVLQ GLAFALLVDI PPVYGLYASF FPAIIYLFLG
TSKHISVGPF PILSMMVGLA VSGAVSKAVP DRNATTLGLS NNSNNSSLLD DKRVTVAASV
TVLSGIIQLA FGILRIGFVV IYLSESLISG FTTAAAVHVL VSQLKFIFQL TVPSHNDPLS
IFKVLVSVFS QIEKTNIADL VTALIVLLVV SIVKEINQRF KDKLPVPIPI EFIMTVIAAG
VSYGCDFKNR FKVAVVGDMN PGFQPPITPD VQAFQNTIGD CFGIAMVAFA VAFSVASVYS
LKYDYPLDGN QELIALGLGN IVCGVFRGFA GSTALSRSAV QESTGGKTQI AGLIGAIIVL
IVLLAIGFLL APLQKSVLAA LALGNLKGML MQFAEIGRLW RKDKYDCLIW IMTFIFTIVL
GLGLGLAASV AFQLLTIEKK CHWLREQCPS PIYFANIGFF RQKLIDAVGF SPLRILRKRN
KALRKIRKLQ KQGLLQVTPK GFICTVDTIK DSDEELDNNQ IEVLDQPINT TDLPFQIDWN
DDLPLNIEVP KISLHSLILD FSAVSFLDVS SMRGLKSILQ EFIRIKVDVY IVGTDDDFIE
KLNRYEFFDG EVKNSIFFLT IHDAVLHILM KKDYSTSKFN PSQEKDGKID FTINTNGGLR
NRVYEVRFFN RFIFT
//