S26A1_RAT
ID S26A1_RAT Reviewed; 703 AA.
AC P45380;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Sulfate anion transporter 1;
DE Short=SAT-1;
DE AltName: Full=Canalicular sulfate transporter;
DE AltName: Full=Solute carrier family 26 member 1;
DE AltName: Full=Sulfate/carbonate antiporter;
GN Name=Slc26a1; Synonyms=Sat1;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8300633; DOI=10.1016/s0021-9258(17)42040-0;
RA Bissig M., Hagenbuch B., Stieger B., Koller T., Meier P.J.;
RT "Functional expression cloning of the canalicular sulfate transport system
RT of rat hepatocytes.";
RL J. Biol. Chem. 269:3017-3021(1994).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-586 AND SER-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27210743; DOI=10.1016/j.ajhg.2016.03.026;
RA Gee H.Y., Jun I., Braun D.A., Lawson J.A., Halbritter J., Shril S.,
RA Nelson C.P., Tan W., Stein D., Wassner A.J., Ferguson M.A., Gucev Z.,
RA Sayer J.A., Milosevic D., Baum M., Tasic V., Lee M.G., Hildebrandt F.;
RT "Mutations in SLC26A1 Cause Nephrolithiasis.";
RL Am. J. Hum. Genet. 98:1228-1234(2016).
CC -!- FUNCTION: Mediates sulfate transport with high affinity
CC (PubMed:8300633). Mediates oxalate transport (PubMed:8300633). Mediates
CC bicarbonate transport (By similarity). Does not accept succinate as
CC cosubstrate (PubMed:8300633). {ECO:0000250|UniProtKB:P58735,
CC ECO:0000269|PubMed:8300633}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:27210743}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney cortex and medulla, ileum and
CC colon (at protein level) (PubMed:27210743). Expressed in liver and
CC kidney (PubMed:8300633). Less abundant in muscle and brain
CC (PubMed:8300633). {ECO:0000269|PubMed:27210743,
CC ECO:0000269|PubMed:8300633}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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; L23413; AAA17545.1; -; mRNA.
DR PIR; A49994; A49994.
DR AlphaFoldDB; P45380; -.
DR SMR; P45380; -.
DR STRING; 10116.ENSRNOP00000000047; -.
DR TCDB; 2.A.53.2.2; the sulfate permease (sulp) family.
DR GlyGen; P45380; 3 sites.
DR iPTMnet; P45380; -.
DR PaxDb; P45380; -.
DR PRIDE; P45380; -.
DR UCSC; RGD:620136; rat.
DR RGD; 620136; Slc26a1.
DR eggNOG; KOG0236; Eukaryota.
DR InParanoid; P45380; -.
DR PhylomeDB; P45380; -.
DR Reactome; R-RNO-174362; Transport and synthesis of PAPS.
DR Reactome; R-RNO-427601; Multifunctional anion exchangers.
DR PRO; PR:P45380; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; ISS:UniProtKB.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:RGD.
DR GO; GO:0006821; P:chloride transport; ISO:RGD.
DR GO; GO:0019532; P:oxalate transport; ISO:RGD.
DR GO; GO:0008272; P:sulfate transport; IDA:RGD.
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; IPR030331; SLC26A1.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF31; PTHR11814:SF31; 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 Anion exchange; Antiport; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..703
FT /note="Sulfate anion transporter 1"
FT /id="PRO_0000080157"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 531..689
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 703 AA; 75447 MW; A90D839D70BD2738 CRC64;
MDASPEPPQK GGTLVLVRRQ PPVSQGLLET LKARLKKSCT CSMPCAQALV QGLFPVIRWL
PQYRLKEYLA GDVMSGLVIG IILVPQAIAY SLLAGLQPIY SLYTSFFANL IYFLMGTSRH
VNVGIFSLLC LMVGQVVDRE LQLAGFDPSQ DSLGPGNNDS TLNNTATLTV GLQDCGRDCH
AIRIATALTL MAGLYQVLMG ILRLGFVSTY LSQPLLDGFA MGASVTILTS QAKHLLGVRI
PRHQGLGMVI HTWLSLLQNV GQANLCDVVT SAVCLAVLLT AKELSDRYRH YLKVPVPTEL
LVIVVATIAS HFGQLHTRFG SSVAGNIPTG FVAPQIPDPK IMWSVALDAM SLALVGSAFS
ISLAEMFARS HGYSVSANQE LLAVGCCNVL PAFFHCFATS AALSKTLVKI ATGCQTQLSS
VVSAAVVLLV LLVLAPLFHD LQRCVLACII VVSLRGALRK VKDLPQLWRL SPADALVWVA
TAATCVLVSI EAGLLAGVFF SLLSLAGRTQ RPRAALLARI GDSTFYEDAA EFEGLLPPPE
VRVFRFTGPL YYANKDFFLR SLYSLTGLDA GYSATRKDRG TEVGVSNRSL VDRKDLGSVS
SGDGLVVPLA FGFHTVVIDC APLLFLDVAG MATLKDLRKN YRALDITLLL ACCSPSVRDT
LRKGGFLGED QGTAEELLFP SVHSAVETAC ARREELMAAD SAL
