S2611_MOUSE
ID S2611_MOUSE Reviewed; 593 AA.
AC Q80ZD3; B2RQF3; Q8BTP1; Q8BWL3; Q8CHW8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sodium-independent sulfate anion transporter;
DE AltName: Full=Solute carrier family 26 member 11;
GN Name=Slc26a11 {ECO:0000312|MGI:MGI:2444589};
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] {ECO:0000305, ECO:0000312|EMBL:AAO49173.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO49173.1};
RA Mount D.B.;
RT "Characterization of Mus musculus Slc26a11, a putative anion exchanger.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC40782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC34882.1}, and
RC NOD {ECO:0000312|EMBL:BAC40782.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAC40782.1}, and
RC Embryonic heart {ECO:0000312|EMBL:BAC34882.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH38604.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH38604.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAI32494.1}, and
RC Salivary gland {ECO:0000312|EMBL:AAH38604.1};
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).
CC -!- FUNCTION: Exhibits sodium-independent sulfate anion transporter
CC activity that may cooperate with SLC26A2 to mediate DIDS-sensitive
CC sulfate uptake into high endothelial venules endothelial cells (HEVEC).
CC {ECO:0000250|UniProtKB:Q86WA9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86WA9};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WA9}. Lysosome
CC membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q86WA9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072,
CC ECO:0000269|Ref.1};
CC IsoId=Q80ZD3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q80ZD3-2; Sequence=VSP_052687, VSP_052688;
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38604.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF345196; AAO49173.1; -; mRNA.
DR EMBL; AK052202; BAC34882.1; -; mRNA.
DR EMBL; AK089182; BAC40782.1; -; mRNA.
DR EMBL; BC038604; AAH38604.1; ALT_INIT; mRNA.
DR EMBL; BC132493; AAI32494.1; -; mRNA.
DR EMBL; BC137897; AAI37898.1; -; mRNA.
DR CCDS; CCDS25717.1; -. [Q80ZD3-1]
DR RefSeq; NP_848858.2; NM_178743.3. [Q80ZD3-1]
DR RefSeq; XP_006533484.1; XM_006533421.2. [Q80ZD3-2]
DR AlphaFoldDB; Q80ZD3; -.
DR SMR; Q80ZD3; -.
DR STRING; 10090.ENSMUSP00000050999; -.
DR iPTMnet; Q80ZD3; -.
DR PhosphoSitePlus; Q80ZD3; -.
DR SwissPalm; Q80ZD3; -.
DR EPD; Q80ZD3; -.
DR MaxQB; Q80ZD3; -.
DR PaxDb; Q80ZD3; -.
DR PeptideAtlas; Q80ZD3; -.
DR PRIDE; Q80ZD3; -.
DR ProteomicsDB; 256869; -. [Q80ZD3-1]
DR ProteomicsDB; 256870; -. [Q80ZD3-2]
DR Antibodypedia; 32732; 35 antibodies from 10 providers.
DR DNASU; 268512; -.
DR Ensembl; ENSMUST00000050880; ENSMUSP00000050999; ENSMUSG00000039908. [Q80ZD3-1]
DR GeneID; 268512; -.
DR KEGG; mmu:268512; -.
DR UCSC; uc007mqm.1; mouse. [Q80ZD3-1]
DR UCSC; uc007mqn.1; mouse. [Q80ZD3-2]
DR CTD; 284129; -.
DR MGI; MGI:2444589; Slc26a11.
DR VEuPathDB; HostDB:ENSMUSG00000039908; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244925; -.
DR HOGENOM; CLU_003182_12_2_1; -.
DR InParanoid; Q80ZD3; -.
DR OMA; VTNKFPI; -.
DR OrthoDB; 289441at2759; -.
DR PhylomeDB; Q80ZD3; -.
DR TreeFam; TF323537; -.
DR Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR BioGRID-ORCS; 268512; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Slc26a11; mouse.
DR PRO; PR:Q80ZD3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80ZD3; protein.
DR Bgee; ENSMUSG00000039908; Expressed in granulocyte and 190 other tissues.
DR Genevisible; Q80ZD3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008509; F:anion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter 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: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; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Anion exchange; Cell membrane; Ion transport;
KW Lysosome; Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..593
FT /note="Sodium-independent sulfate anion transporter"
FT /id="PRO_0000320687"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 453..566
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 564..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..8
FT /note="MAPDTCCC -> MHAPTPVC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052687"
FT VAR_SEQ 9..180
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052688"
FT CONFLICT 37
FT /note="A -> S (in Ref. 3; AAH38604)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="M -> V (in Ref. 1; AAO49173)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="A -> T (in Ref. 1; AAO49173)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="T -> A (in Ref. 1; AAO49173)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="E -> G (in Ref. 2; BAC40782)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 64109 MW; B073D040EAA77DDE CRC64;
MAPDTCCCSA TALRRRLPVL AWVPDYSLQW LRLDFIAGLS VGLTVIPQAL AYAEVAGLPP
QYGLYSAFMG CFVYFFLGTS RDVTLGPTAI MSLLVSFYTF REPAYAVLLA FLSGCIQLAM
GLLHLGFLLD FISCPVIKGF TSAASITIGF GQIKNLLGLQ KIPRQFFLQV YHTFLHIGET
RVGDAVLGLA SMLLLLVLKC MREHMPPPHP EMPLAVKFSR GLVWTVTTAR NALVVSSAAL
IAYAFEVTGS HPFVLTGKIA EGLPPVRIPP FSVTRDNKTI SFSEMVQDMG AGLAVVPLMG
LLESIAVAKS FASQNNYRID ANQELLAIGL TNVLGSLVSS YPVTGSFGRT AVNAQTGVCT
PAGGLVTGAL VLLSLNYLTS LFSYIPKSAL AAVIITAVTP LFDVKIFRSL WRVQRLDLLP
LCVTFLLSFW EIQYGILAGS LVSLLILLHS VARPKTQVSE GQIFVLQPAS GLYFPAIDAL
REAITNRALE ASPPRSAVLE CTHISSVDYT VIVGLGELLE DFQKKGVALA FVGLQVPVLR
TLLAADLKGF RYFTTLEEAE KFLQQEPGTE PNSIHEDAVP EQRSSLLKSP SGP
