S26A2_MOUSE
ID S26A2_MOUSE Reviewed; 739 AA.
AC Q62273; Q543D6; Q8R2L9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Sulfate transporter;
DE AltName: Full=Diastrophic dysplasia protein homolog;
DE AltName: Full=ST-OB;
DE AltName: Full=Solute carrier family 26 member 2;
GN Name=Slc26a2; Synonyms=Dtd, Dtdst;
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].
RX PubMed=9370300; DOI=10.1016/s0378-1119(97)00336-3;
RA Kobayashi T., Sugimoto T., Saijoh K., Fukase M., Chihara K.;
RT "Cloning of mouse diastrophic dysplasia sulfate transporter gene induced
RT during osteoblast differentiation by bone morphogenetic protein-2.";
RL Gene 198:341-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Sulfate transporter. May play a role in endochondral bone
CC formation. {ECO:0000250|UniProtKB:P50443}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50443};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Distributed mainly in the thymus, testis and
CC osteoblastic cells.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; D42049; BAA07650.1; -; mRNA.
DR EMBL; AK052942; BAC35214.1; -; mRNA.
DR EMBL; AK163974; BAE37562.1; -; mRNA.
DR EMBL; CH466528; EDL09779.1; -; Genomic_DNA.
DR EMBL; BC028345; AAH28345.1; -; mRNA.
DR CCDS; CCDS29282.1; -.
DR RefSeq; NP_031911.1; NM_007885.2.
DR AlphaFoldDB; Q62273; -.
DR SMR; Q62273; -.
DR STRING; 10090.ENSMUSP00000119447; -.
DR GlyGen; Q62273; 2 sites.
DR iPTMnet; Q62273; -.
DR PhosphoSitePlus; Q62273; -.
DR SwissPalm; Q62273; -.
DR EPD; Q62273; -.
DR MaxQB; Q62273; -.
DR PaxDb; Q62273; -.
DR PeptideAtlas; Q62273; -.
DR PRIDE; Q62273; -.
DR ProteomicsDB; 260769; -.
DR Antibodypedia; 27892; 150 antibodies from 24 providers.
DR DNASU; 13521; -.
DR Ensembl; ENSMUST00000146409; ENSMUSP00000119447; ENSMUSG00000034320.
DR GeneID; 13521; -.
DR KEGG; mmu:13521; -.
DR UCSC; uc008fbu.1; mouse.
DR CTD; 1836; -.
DR MGI; MGI:892977; Slc26a2.
DR VEuPathDB; HostDB:ENSMUSG00000034320; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244925; -.
DR InParanoid; Q62273; -.
DR OMA; ALYWIPK; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q62273; -.
DR TreeFam; TF313784; -.
DR Reactome; R-MMU-174362; Transport and synthesis of PAPS.
DR Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR BioGRID-ORCS; 13521; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Nqo1; mouse.
DR PRO; PR:Q62273; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q62273; protein.
DR Bgee; ENSMUSG00000034320; Expressed in left colon and 263 other tissues.
DR ExpressionAtlas; Q62273; baseline and differential.
DR Genevisible; Q62273; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; ISO:MGI.
DR GO; GO:1902358; P:sulfate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0008272; P:sulfate transport; ISO:MGI.
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; IPR030280; SLC26A2.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF16; PTHR11814:SF16; 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 Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..739
FT /note="Sulfate transporter"
FT /id="PRO_0000080159"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 568..719
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50443"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 31
FT /note="T -> A (in Ref. 4; AAH28345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81604 MW; EEDB1DA6278EC6BD CRC64;
MSSENKEQHD LSPRDLPEEA FGFPSELPLE TQRRSGTDLR QSETGHGRRA FRRIHMELRE
KPDTDIKQFV IRELQKSCQC SAAKVRDGAF DFFPVLRWLP KYDLKKNILG DVMSGLIVGI
LLVPQSIAYS LLAGQEPIYG LYTSFFASII YFLFGTSRHI SVGIFGILCL MIGEVVDREL
HKACPDTDAT SSSIAVFSSG CVVVNHTLDG LCDKSCYAIK IGSTVTFMAG VYQVAMGFFQ
VGFVSVYLSD ALLSGFVTGA SFTILTSQAK YLLGLSLPRS HGVGSVITTW IHIFRNIRNT
NICDLITSLL CLLVLVPSKE LNEHFKDKLK APIPVELIVV VAATLASHFG KLNGNYNSSI
AGHIPTGFMP PKAPDWSLIP NVAVDAIAIS IIGFAITVSL SEMFAKKHGY TVKANQEMYA
IGFCNIIPSF FHCITTSAAL AKTLVKESTG CQTQLSAIVT ALVLLLVLLV IAPLFYSLQK
CVLGVITIVN LRGALLKFRD LPKMWRLSRM DTVIWFVTML SSALLSTEIG LLVGVCFSMF
CVILRTQKPK NSLLGLEEES ETFESISTYK NLRSKSGIKV FRFIAPLYYI NKECFKSALY
KKALNPVLVK AAWKKAAKRK LKEEMVTFRG DPDEVSMQLS HDPLEVHTIV IDCSAIQFLD
TAGIHTLKEV RRDYEAVGIQ VLLAQCNPSV RDSLARGEYC KKEEETLLFY SLSEAVAFAE
DSQNQKGVCV VNGLSLSGD
