S26A9_MOUSE
ID S26A9_MOUSE Reviewed; 790 AA.
AC Q8BU91; Q8BVC3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Solute carrier family 26 member 9;
DE AltName: Full=Anion transporter/exchanger protein 9;
GN Name=Slc26a9;
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].
RC STRAIN=C57BL/6J;
RA Mount D.B.;
RT "Cloning of mouse SLC26A9, a new member of the sulphate transporter gene
RT family of anion transporters/exchangers.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Lung;
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 FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=15800055; DOI=10.1152/ajpcell.00030.2005;
RA Xu J., Henriksnas J., Barone S., Witte D., Shull G.E., Forte J.G., Holm L.,
RA Soleimani M.;
RT "SLC26A9 is expressed in gastric surface epithelial cells, mediates
RT Cl-/HCO3- exchange, and is inhibited by NH4+.";
RL Am. J. Physiol. 289:C493-C505(2005).
RN [4]
RP FUNCTION.
RX PubMed=17120765;
RA Romero M.F., Chang M.H., Plata C., Zandi-Nejad K., Mercado A., Broumand V.,
RA Sussman C.R., Mount D.B.;
RT "Physiology of electrogenic SLC26 paralogues.";
RL Novartis Found. Symp. 273:126-138(2006).
RN [5] {ECO:0007744|PDB:6RTC, ECO:0007744|PDB:6RTF}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.96 ANGSTROMS) OF 1-557 AND 661-744,
RP FUNCTION, MUTAGENESIS OF GLN-88; PHE-128; ARG-205; LYS-270; LYS-358;
RP SER-392 AND LYS-443, TOPOLOGY, AND TRANSMEMBRANE DOMAINS.
RX PubMed=31339488; DOI=10.7554/elife.46986;
RA Walter J.D., Sawicka M., Dutzler R.;
RT "Cryo-EM structures and functional characterization of murine Slc26a9
RT reveal mechanism of uncoupled chloride transport.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: DIDS- and thiosulfate- sensitive anion exchanger mediating
CC chloride, sulfate and oxalate transport (PubMed:15800055,
CC PubMed:17120765). Mediates chloride/bicarbonate exchange or chloride-
CC independent bicarbonate extrusion thus assuring bicarbonate secretion
CC (PubMed:15800055, PubMed:17120765). May prefer chloride anions and
CC mediate uncoupled chloride anion transport in an alternate-access
CC mechanism where a saturable binding site is alternately exposed to
CC either one or the other side of the membrane (PubMed:31339488).
CC {ECO:0000269|PubMed:15800055, ECO:0000269|PubMed:17120765,
CC ECO:0000269|PubMed:31339488}.
CC -!- ACTIVITY REGULATION: Inhibited by ammonium and thiosulfate.
CC {ECO:0000269|PubMed:15800055}.
CC -!- SUBUNIT: May form homodimers (in vitro). {ECO:0000269|PubMed:31339488}.
CC -!- INTERACTION:
CC Q8BU91; Q8BU91: Slc26a9; NbExp=2; IntAct=EBI-27096086, EBI-27096086;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31339488};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in stomach and trachea. Abundantly
CC expressed in the apical domain of the surface epithelial cells and the
CC deep cells in the gastric gland. Also expressed in heart, brain, lung
CC and liver. {ECO:0000269|PubMed:15800055}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AY034145; AAK54448.1; -; mRNA.
DR EMBL; AK078966; BAC37482.1; -; mRNA.
DR EMBL; AK086815; BAC39749.1; -; mRNA.
DR CCDS; CCDS15273.1; -.
DR RefSeq; NP_796217.2; NM_177243.4.
DR RefSeq; XP_006529763.1; XM_006529700.2.
DR PDB; 6RTC; EM; 3.96 A; A/B=1-557, A/B=661-744.
DR PDB; 6RTF; EM; 7.77 A; A/B=1-557, A/B=661-744.
DR PDBsum; 6RTC; -.
DR PDBsum; 6RTF; -.
DR AlphaFoldDB; Q8BU91; -.
DR SMR; Q8BU91; -.
DR STRING; 10090.ENSMUSP00000036916; -.
DR TCDB; 2.A.53.2.10; the sulfate permease (sulp) family.
DR PhosphoSitePlus; Q8BU91; -.
DR PaxDb; Q8BU91; -.
DR PRIDE; Q8BU91; -.
DR ProteomicsDB; 253378; -.
DR DNASU; 320718; -.
DR GeneID; 320718; -.
DR KEGG; mmu:320718; -.
DR UCSC; uc007cns.1; mouse.
DR CTD; 115019; -.
DR MGI; MGI:2444594; Slc26a9.
DR eggNOG; KOG0236; Eukaryota.
DR InParanoid; Q8BU91; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q8BU91; -.
DR TreeFam; TF313784; -.
DR Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR BioGRID-ORCS; 320718; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8BU91; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BU91; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; IDA:MGI.
DR GO; GO:0006821; P:chloride transport; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0006885; P:regulation of pH; IDA:MGI.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR030306; SLC26A9.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF17; PTHR11814:SF17; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..790
FT /note="Solute carrier family 26 member 9"
FT /id="PRO_0000324493"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 71..96
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 97..100
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 101..109
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 110..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 130..142
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 143..162
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 163..191
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 192..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 225..237
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT INTRAMEM 238..246
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 247..254
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 276..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 287..299
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 300..334
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 335..358
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 359..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 366..379
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 380..390
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 391..400
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 401..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 406..419
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 420..431
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 432..457
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 458..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 462..476
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 477..479
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TRANSMEM 480..498
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31339488"
FT TOPO_DOM 499..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31339488"
FT DOMAIN 519..737
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MUTAGEN 88
FT /note="Q->A,E: Alters chloride anion transport behavior."
FT /evidence="ECO:0000269|PubMed:31339488"
FT MUTAGEN 128
FT /note="F->A: Alters chloride anion transport behavior."
FT /evidence="ECO:0000269|PubMed:31339488"
FT MUTAGEN 205
FT /note="R->E: Has very little effect on anion transport."
FT /evidence="ECO:0000269|PubMed:31339488"
FT MUTAGEN 270
FT /note="K->E: Impairs outward anion transport properties."
FT /evidence="ECO:0000269|PubMed:31339488"
FT MUTAGEN 358
FT /note="K->E: Has very little effect on anion transport."
FT /evidence="ECO:0000269|PubMed:31339488"
FT MUTAGEN 392
FT /note="S->A: Alters chloride anion transport behavior."
FT /evidence="ECO:0000269|PubMed:31339488"
FT MUTAGEN 443
FT /note="K->E: Impairs outward anion transport properties."
FT /evidence="ECO:0000269|PubMed:31339488"
FT CONFLICT 332
FT /note="G -> D (in Ref. 1; AAK54448 and 2; BAC37482)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="L -> F (in Ref. 1; AAK54448 and 2; BAC37482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 86852 MW; 4D473330D4D94DCD CRC64;
MNQPRPRYVV DRAAYSLSLF DDEFEKKDRA YPVGEKLRNT FRCSSAKFKA FVFGLLPVLS
WLPKYKIKDY IIPDLLGGLS GGCIQVPQGM AFALLANLPA VNGLYSSFFP LLTYFFLGGI
HQMVPGTFAV ISILVGNICL QLAPESKFQI FNNVTNETYV DTAAMEAERL HVSATLACLT
AVIQMALGFM QFGFVAIYLS ESFIRGFMTA AGLQILISVL KYIFGLTIPS YTGPGSIVFT
FIDICKNLPH TNIASLIFAL VSGVFLVLVK ELNARYMHKI HFPIPTEMIV VVVATAISGS
CKMPKKYHMQ IVGEIRQGFP TPVAPMVSQW KGMVGTAFSL AIVGYVINLA MGRTLASKHG
YDVDSNQEMI ALGCSNFFGS FFKIHVICCA LSVTLAVDGA GGKSQVASLC VSLVVMITML
VLGSYLYPLP KAVLGALIAV NLKNSLKQLT DPYYLWRKSK LDCCVWVVSF LSSFFLSLPY
GVAVGVAFSI LVVIFQTQFR NGSTLAQVMD TDIYVNPKTY NRAQEIAGVK IVTYCSPLYL
ANSEIFRQKV IAKTGMDPQK VLLAKQKYLR KQEKRTAIPT QQRKSLFMKT KTVSLQELQQ
DFESAPSTDP NNNQAPAAEA HISYITFSPD ASTAAACELP ASTRSPQEAS DTLASVPPFV
TFHTLILDMS GVSFVDLMGI KALAKLSSTY EKIGVQIFLV NIHAQVYNDI SHGGVFEDGC
VQRSHVFPSI HDAVLFAQAN AREAPDRNFH GAPGDTEFSL YDSEEEGPSY WDLEQEMFGT
MFHTETLTAL
