S26A3_MOUSE
ID S26A3_MOUSE Reviewed; 757 AA.
AC Q9WVC8; B2RTD9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=10428871; DOI=10.1074/jbc.274.32.22855;
RA Melvin J.E., Park K., Richardson L., Schultheis P.J., Shull G.E.;
RT "Mouse down-regulated in adenoma (DRA) is an intestinal Cl(-)/HCO(3)(-)
RT exchanger and is up-regulated in colon of mice lacking the NHE3 Na(+)/H(+)
RT exchanger.";
RL J. Biol. Chem. 274:22855-22861(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH CFTR; SLC26A6 AND SLC9A3R1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21976599; DOI=10.1095/biolreprod.111.094037;
RA Chavez J.C., Hernandez-Gonzalez E.O., Wertheimer E., Visconti P.E.,
RA Darszon A., Trevino C.L.;
RT "Participation of the Cl-/HCO(3)- exchangers SLC26A3 and SLC26A6, the
RT Cl- channel CFTR, and the regulatory factor SLC9A3R1 in mouse sperm
RT capacitation.";
RL Biol. Reprod. 86:1-14(2012).
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.
CC {ECO:0000269|PubMed:10428871, ECO:0000269|PubMed:21976599}.
CC -!- SUBUNIT: Interacts with PDZK1 (By similarity). Interacts with CFTR,
CC SLC26A6 and SLC9A3R1. {ECO:0000250, ECO:0000269|PubMed:21976599}.
CC -!- INTERACTION:
CC Q9WVC8; P26361: Cftr; NbExp=3; IntAct=EBI-6895537, EBI-6115317;
CC Q9WVC8; Q8CIW6: Slc26a6; NbExp=2; IntAct=EBI-6895537, EBI-6895517;
CC Q9WVC8; P70441: Slc9a3r1; NbExp=2; IntAct=EBI-6895537, EBI-1184085;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:21976599};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21976599}.
CC Note=Localized in sperm membranes. Midpiece of sperm tail. Colocalizes
CC with CFTR at the midpiece of sperm tail.
CC -!- TISSUE SPECIFICITY: Expressed in spermatogenic cells.
CC {ECO:0000269|PubMed:21976599}.
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; AF136751; AAD42784.1; -; mRNA.
DR EMBL; BC139271; AAI39272.1; -; mRNA.
DR EMBL; BC139273; AAI39274.1; -; mRNA.
DR CCDS; CCDS25863.1; -.
DR RefSeq; NP_067328.1; NM_021353.3.
DR RefSeq; XP_017170439.1; XM_017314950.1.
DR PDB; 5DOW; X-ray; 1.70 A; B/D/F/H=563-583.
DR PDBsum; 5DOW; -.
DR AlphaFoldDB; Q9WVC8; -.
DR SMR; Q9WVC8; -.
DR IntAct; Q9WVC8; 3.
DR STRING; 10090.ENSMUSP00000001254; -.
DR BindingDB; Q9WVC8; -.
DR ChEMBL; CHEMBL4523503; -.
DR TCDB; 2.A.53.2.3; the sulfate permease (sulp) family.
DR GlyGen; Q9WVC8; 2 sites.
DR MaxQB; Q9WVC8; -.
DR PaxDb; Q9WVC8; -.
DR PRIDE; Q9WVC8; -.
DR ProteomicsDB; 256672; -.
DR Antibodypedia; 31383; 82 antibodies from 26 providers.
DR DNASU; 13487; -.
DR Ensembl; ENSMUST00000001254; ENSMUSP00000001254; ENSMUSG00000001225.
DR GeneID; 13487; -.
DR KEGG; mmu:13487; -.
DR UCSC; uc007nhj.2; mouse.
DR CTD; 1811; -.
DR MGI; MGI:107181; Slc26a3.
DR VEuPathDB; HostDB:ENSMUSG00000001225; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q9WVC8; -.
DR OMA; KKRDRHH; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q9WVC8; -.
DR TreeFam; TF313784; -.
DR Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR BioGRID-ORCS; 13487; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Slc26a3; mouse.
DR PRO; PR:Q9WVC8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WVC8; protein.
DR Bgee; ENSMUSG00000001225; Expressed in left colon and 46 other tissues.
DR ExpressionAtlas; Q9WVC8; baseline and differential.
DR Genevisible; Q9WVC8; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA:MGI.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IMP: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; IDA:UniProtKB.
DR GO; GO:0051454; P:intracellular pH elevation; IMP:UniProtKB.
DR GO; GO:0060081; P:membrane hyperpolarization; IMP:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IMP: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 1: Evidence at protein level;
KW 3D-structure; 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_0000080162"
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 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 566..576
FT /evidence="ECO:0007829|PDB:5DOW"
FT HELIX 579..582
FT /evidence="ECO:0007829|PDB:5DOW"
SQ SEQUENCE 757 AA; 83590 MW; 32B1AC648BE74A07 CRC64;
MIEAIGNQYV VARPVYSTKT FGEEFKKTHR HHKTFLDHLK GCCSCSSQKA KKIALSLFPI
ASWLPAYKIK EWLLSDIVSG ISTGLVAVLQ GLAFALLVNI PPAYGLYAAF FPVITYFFLG
TSRHISVGPF PVLSMMVGVV VTRVVSDPNA SSELSSSSTE NDSFIEEKVM VAASVTVLSG
IIQLLLGVLQ VGFVVIYLSE SLISGFTTAA AIHVLVSQLK FMLQLPVPAY SDPFSIFKVL
ESVFTQIQKT NIADLVTSVI ILVVVFVFKE INQRYRSKLP VPIPIELIMT VIATGVSYGC
NFEDRFGVAV VGNMSLGFQP PITPSVEVFQ DTIGDSFGIA IVGFAVAFSV ASVYSLKYDY
PIDGNQELIA LGVSNIFTGA FKGFAGSTAL SRSGVQESTG GKTQVAGLLS AVIVLIVIVA
IGFLLQPLQK SVLAALALGN LKGMLMQFAE IGRLWKKDKY DCLIWIMTFI FAIVLGLGLG
LAASVAFQLL TIVFRTQFPK CSTLANVGRS NIYKNKKNYA EVYEPEGVKI FRCPSPIYFA
NIGFFKQKLI DAVGFSPLRI LRKRNKALKK IRKLQKRGLI QMTPKGFICT SDGFKDSDEE
LDNNQIEELD QPINTTDLPF DIDWNGDLPL NITIPKISLH SLILDFSAVS FLDVSSMRGL
RTILQEFIRI KVDVYIVGTD DDFIDKLARC EFFDDEVTDS IFFLTIHDAI LHILMKKDYS
TSKFNSSQEK ERKFDFTINT NGGLRNRECQ VPVETKF
