S26A1_HUMAN
ID S26A1_HUMAN Reviewed; 701 AA.
AC Q9H2B4; A8K9N2; Q7Z5R3; Q96BK0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Sulfate anion transporter 1;
DE Short=SAT-1;
DE AltName: Full=Solute carrier family 26 member 1;
GN Name=SLC26A1; Synonyms=SAT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=11087667; DOI=10.1006/geno.2000.6355;
RA Lohi H., Kujala M., Kerkelae E., Saarialho-Kere U., Kestilae M., Kere J.;
RT "Mapping of five new putative anion transporter genes in human and
RT characterization of SLC26A6, a candidate gene for pancreatic anion
RT exchanger.";
RL Genomics 70:102-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=12713736; DOI=10.1089/104454903321515913;
RA Regeer R.R., Lee A., Markovich D.;
RT "Characterization of the human sulfate anion transporter (hsat-1) protein
RT and gene (SAT1; SLC26A1).";
RL DNA Cell Biol. 22:107-117(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-556.
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-556.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INVOLVEMENT IN CAON, AND VARIANTS CAON THR-56; MET-185 AND LEU-358.
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:12713736). Mediates oxalate transport (PubMed:12713736).
CC Mediates bicarbonate transport (By similarity). Does not accept
CC succinate as cosubstrate (By similarity).
CC {ECO:0000250|UniProtKB:P45380, ECO:0000250|UniProtKB:P58735,
CC ECO:0000269|PubMed:12713736}.
CC -!- INTERACTION:
CC Q9H2B4-2; Q92876: KLK6; NbExp=3; IntAct=EBI-12908340, EBI-2432309;
CC Q9H2B4-2; Q96JF0-2: ST6GAL2; NbExp=3; IntAct=EBI-12908340, EBI-12908338;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P58735};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P45380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2B4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2B4-2; Sequence=VSP_043671, VSP_043672;
CC -!- TISSUE SPECIFICITY: Expressed most abundantly in the kidney and liver,
CC with lower levels in the pancreas, testis, brain, small intestine,
CC colon, and lung. {ECO:0000269|PubMed:12713736}.
CC -!- DISEASE: Nephrolithiasis, calcium oxalate (CAON) [MIM:167030]: A form
CC of nephrolithiasis, a condition in which urinary supersaturation leads
CC to stone formation in the urinary system. Patients manifest acute renal
CC colic with severe pain originating in the flank. Patients with small,
CC non-obstructing stones or those with staghorn calculi may be
CC asymptomatic. The majority of renal calculi contain calcium. CAON is
CC characterized by calcium oxalate kidney stones.
CC {ECO:0000269|PubMed:27210743}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AF297659; AAG22075.1; -; mRNA.
DR EMBL; AY124771; AAM94171.1; -; mRNA.
DR EMBL; AK292747; BAF85436.1; -; mRNA.
DR EMBL; AC019103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82628.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82629.1; -; Genomic_DNA.
DR EMBL; BC015517; AAH15517.1; -; mRNA.
DR CCDS; CCDS33933.1; -. [Q9H2B4-2]
DR CCDS; CCDS33934.1; -. [Q9H2B4-1]
DR RefSeq; NP_071325.2; NM_022042.3. [Q9H2B4-1]
DR RefSeq; NP_602297.1; NM_134425.2. [Q9H2B4-2]
DR RefSeq; NP_998778.1; NM_213613.3. [Q9H2B4-1]
DR AlphaFoldDB; Q9H2B4; -.
DR SMR; Q9H2B4; -.
DR BioGRID; 116071; 6.
DR IntAct; Q9H2B4; 2.
DR STRING; 9606.ENSP00000354721; -.
DR TCDB; 2.A.53.2.16; the sulfate permease (sulp) family.
DR GlyGen; Q9H2B4; 2 sites.
DR iPTMnet; Q9H2B4; -.
DR PhosphoSitePlus; Q9H2B4; -.
DR BioMuta; SLC26A1; -.
DR DMDM; 209572674; -.
DR jPOST; Q9H2B4; -.
DR MassIVE; Q9H2B4; -.
DR MaxQB; Q9H2B4; -.
DR PaxDb; Q9H2B4; -.
DR PeptideAtlas; Q9H2B4; -.
DR PRIDE; Q9H2B4; -.
DR ProteomicsDB; 80523; -. [Q9H2B4-1]
DR ProteomicsDB; 80524; -. [Q9H2B4-2]
DR Antibodypedia; 8230; 106 antibodies from 27 providers.
DR CPTC; Q9H2B4; 3 antibodies.
DR DNASU; 10861; -.
DR Ensembl; ENST00000361661.6; ENSP00000354721.2; ENSG00000145217.14. [Q9H2B4-1]
DR Ensembl; ENST00000398516.3; ENSP00000381528.2; ENSG00000145217.14. [Q9H2B4-1]
DR Ensembl; ENST00000398520.6; ENSP00000381532.2; ENSG00000145217.14. [Q9H2B4-2]
DR Ensembl; ENST00000622731.4; ENSP00000483506.1; ENSG00000145217.14. [Q9H2B4-2]
DR GeneID; 10861; -.
DR KEGG; hsa:10861; -.
DR MANE-Select; ENST00000398516.3; ENSP00000381528.2; NM_022042.4; NP_071325.2.
DR UCSC; uc003gbx.5; human. [Q9H2B4-1]
DR CTD; 10861; -.
DR DisGeNET; 10861; -.
DR GeneCards; SLC26A1; -.
DR HGNC; HGNC:10993; SLC26A1.
DR HPA; ENSG00000145217; Tissue enhanced (liver).
DR MalaCards; SLC26A1; -.
DR MIM; 167030; phenotype.
DR MIM; 610130; gene.
DR neXtProt; NX_Q9H2B4; -.
DR OpenTargets; ENSG00000145217; -.
DR PharmGKB; PA400; -.
DR VEuPathDB; HostDB:ENSG00000145217; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244925; -.
DR HOGENOM; CLU_1234655_0_0_1; -.
DR InParanoid; Q9H2B4; -.
DR OMA; EMFARNH; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q9H2B4; -.
DR TreeFam; TF313784; -.
DR PathwayCommons; Q9H2B4; -.
DR Reactome; R-HSA-174362; Transport and synthesis of PAPS.
DR Reactome; R-HSA-427601; Multifunctional anion exchangers.
DR SignaLink; Q9H2B4; -.
DR BioGRID-ORCS; 10861; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; SLC26A1; human.
DR GenomeRNAi; 10861; -.
DR Pharos; Q9H2B4; Tbio.
DR PRO; PR:Q9H2B4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H2B4; protein.
DR Bgee; ENSG00000145217; Expressed in right adrenal gland cortex and 91 other tissues.
DR Genevisible; Q9H2B4; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; ISS:UniProtKB.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0019532; P:oxalate transport; ISS:UniProtKB.
DR GO; GO:0008272; P:sulfate transport; 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; 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 Alternative splicing; Anion exchange; Antiport; Cell membrane;
KW Disease variant; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..701
FT /note="Sulfate anion transporter 1"
FT /id="PRO_0000080155"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 527..687
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VAR_SEQ 193..224
FT /note="VLMGVLRLGFVSAYLSQPLLDGFAMGASVTIL -> TSWGRNSFQQHPWQLT
FT QRSDSQELLEEEERSC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043671"
FT VAR_SEQ 225..701
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043672"
FT VARIANT 56
FT /note="A -> T (in CAON; unknown pathological significance;
FT dbSNP:rs142573758)"
FT /evidence="ECO:0000269|PubMed:27210743"
FT /id="VAR_077134"
FT VARIANT 185
FT /note="T -> M (in CAON; dbSNP:rs139024319)"
FT /evidence="ECO:0000269|PubMed:27210743"
FT /id="VAR_077135"
FT VARIANT 358
FT /note="S -> L (in CAON; dbSNP:rs148832260)"
FT /evidence="ECO:0000269|PubMed:27210743"
FT /id="VAR_077136"
FT VARIANT 556
FT /note="Q -> R (in dbSNP:rs3796622)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_046727"
FT CONFLICT 459..460
FT /note="DL -> GF (in Ref. 1; AAG22075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 75016 MW; A37E9E3D232043AD CRC64;
MDESPEPLQQ GRGPVPVRRQ RPAPRGLREM LKARLWCSCS CSVLCVRALV QDLLPATRWL
RQYRPREYLA GDVMSGLVIG IILVPQAIAY SLLAGLQPIY SLYTSFFANL IYFLMGTSRH
VSVGIFSLLC LMVGQVVDRE LQLAGFDPSQ DGLQPGANSS TLNGSAAMLD CGRDCYAIRV
ATALTLMTGL YQVLMGVLRL GFVSAYLSQP LLDGFAMGAS VTILTSQLKH LLGVRIPRHQ
GPGMVVLTWL SLLRGAGQAN VCDVVTSTVC LAVLLAAKEL SDRYRHRLRV PLPTELLVIV
VATLVSHFGQ LHKRFGSSVA GDIPTGFMPP QVPEPRLMQR VALDAVALAL VAAAFSISLA
EMFARSHGYS VRANQELLAV GCCNVLPAFL HCFATSAALA KSLVKTATGC RTQLSSVVSA
TVVLLVLLAL APLFHDLQRS VLACVIVVSL RGALRKVWDL PRLWRMSPAD ALVWAGTAAT
CMLVSTEAGL LAGVILSLLS LAGRTQRPRT ALLARIGDTA FYEDATEFEG LVPEPGVRVF
RFGGPLYYAN KDFFLQSLYS LTGLDAGCMA ARRKEGGSET GVGEGGPAQG EDLGPVSTRA
ALVPAAAGFH TVVIDCAPLL FLDAAGVSTL QDLRRDYGAL GISLLLACCS PPVRDILSRG
GFLGEGPGDT AEEEQLFLSV HDAVQTARAR HRELEATDAH L
