S26A3_RAT
ID S26A3_RAT Reviewed; 757 AA.
AC Q924C9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Chloride anion exchanger;
DE AltName: Full=Down-regulated in adenoma;
DE Short=Protein DRA;
DE AltName: Full=Solute carrier family 26 member 3;
GN Name=Slc26a3; Synonyms=Dra;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RA Ye H.J., Binder H.J., Rajendran V.M.;
RT "Molecular cloning and characterization of down-regulated in adenoma (DRA)
RT mRNA from rat colon.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chloride/bicarbonate exchanger. Mediates the efficient
CC absorption of chloride ions in the colon, participating in fluid
CC homeostasis. Plays a role in the chloride and bicarbonate homeostasis
CC during sperm epididymal maturation and capacitation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDZK1, CFTR, SLC26A6 and SLC9A3R1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Localized in sperm membranes.
CC Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm
CC tail (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylation is required for efficient cell surface expression,
CC and protection from proteolytic degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AF337809; AAK83221.1; -; mRNA.
DR RefSeq; NP_446207.1; NM_053755.2.
DR AlphaFoldDB; Q924C9; -.
DR SMR; Q924C9; -.
DR STRING; 10116.ENSRNOP00000009473; -.
DR GlyGen; Q924C9; 1 site.
DR iPTMnet; Q924C9; -.
DR PhosphoSitePlus; Q924C9; -.
DR PaxDb; Q924C9; -.
DR Ensembl; ENSRNOT00000009473; ENSRNOP00000009473; ENSRNOG00000006878.
DR GeneID; 114629; -.
DR KEGG; rno:114629; -.
DR UCSC; RGD:620623; rat.
DR CTD; 1811; -.
DR RGD; 620623; Slc26a3.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q924C9; -.
DR OMA; KKRDRHH; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q924C9; -.
DR TreeFam; TF313784; -.
DR Reactome; R-RNO-427601; Multifunctional anion exchangers.
DR PRO; PR:Q924C9; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000006878; Expressed in duodenum and 10 other tissues.
DR Genevisible; Q924C9; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; ISO:RGD.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
DR GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR030321; SLC26A3.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF19; PTHR11814:SF19; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 2: Evidence at transcript level;
KW Antiport; Cell membrane; Chloride; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..757
FT /note="Chloride anion exchanger"
FT /id="PRO_0000080163"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..176
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..250
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..335
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..404
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..757
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 518..713
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 757 AA; 83369 MW; 195D867306ED8ECF CRC64;
MIEAIGNQYV VARPVYSTKA FGEEFKKTYG HHKTFLDHLK GCCSCSSQKA KKIALSLFPI
ASWLPAYKIK EWLLSDIVSG ISTGLVAVLQ GLAFALLVNI PPAYGLYAAF FPVITYFFLG
TSRHISVGPF PVLSMMVGVV VTRVASGSDT SPALSSSSAE NDSMIEEKVM VAASVTVLSG
IIQLLLGVLQ IGFVVIYLSE SLISGFTTAA AIHVLVSQLK FMLQLTVPAH SDPFSIFKVL
ESVFSQIQKT NIADLVTSVI ILVVVFVVKE INQRYRSKLP VPIPIELIMT VIATGISYGC
NFEQRFGVAV VGNMSLGFQP PITPSVEVFQ DTIGDCFGIA IVGFAVAFSV ASVYSLKYDY
PIDGNQELIA LGVSNIFTGA FKGFAGSTAL SRSGVQESTG GKTQVAGLLS AVIVLIVIVA
IGFLLQPLQK SVLAALALGN LKGMLMQFAE IGRLWKKDKY DCLIWIMTFI FAIVLGLGLG
LAASVAFQLL TIVFRTQFPK CSTLANVGRS NIYKNKKNYA DVYEPEGVKI FRCPSPIYFA
NIGFFKQKLI DAVGFNPLRI LRKRNKALKK IRKLQKQGLI QVTPKGFICT SDGFKDSDEE
LDNNQIEELD QPINTTDLPF EIDWNADLPL NITIPKISLH SLILDFSAVS FLDISSMRGL
RTILQEFIRI KVDVYIVGTD DDFIDKLARC EFFDDEVTDS IFFLTIHDAI LHIWMKKDYS
TSKFNSSQEK ERKFDFTINT NGGLRNRECQ VPVETKF
