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Database: UniProt
Entry: S26A7_MOUSE
LinkDB: S26A7_MOUSE
Original site: S26A7_MOUSE 
ID   S26A7_MOUSE             Reviewed;         656 AA.
AC   Q8R2Z3; A2AJZ4; B1AWS0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Anion exchange transporter;
DE   AltName: Full=Solute carrier family 26 member 7;
GN   Name=Slc26a7 {ECO:0000312|EMBL:AAH26928.1, ECO:0000312|MGI:MGI:2384791};
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:0000312|EMBL:AAO49172.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO49172.1};
RA   Mount D.B.;
RT   "Characterization of Mus musculus Slc26a7, a novel putative anion
RT   exchanger.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:AAO49172.1}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAH26928.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II {ECO:0000312|EMBL:AAH26928.1};
RC   TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH26928.1};
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).
RN   [5] {ECO:0000305}
RP   IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=12736153; DOI=10.1152/ajpgi.00454.2002;
RA   Petrovic S., Ju X., Barone S., Seidler U., Alper S.L., Lohi H., Kere J.,
RA   Soleimani M.;
RT   "Identification of a basolateral Cl-/HCO3- exchanger specific to gastric
RT   parietal cells.";
RL   Am. J. Physiol. 284:G1093-G1103(2003).
RN   [6] {ECO:0000305}
RP   FUNCTION, ACTIVITY REGULATION, AND TRANSPORTER ACTIVITY.
RX   PubMed=15591059; DOI=10.1074/jbc.m409162200;
RA   Kim K.H., Shcheynikov N., Wang Y., Muallem S.;
RT   "SLC26A7 is a Cl- channel regulated by intracellular pH.";
RL   J. Biol. Chem. 280:6463-6470(2005).
RN   [7] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16263805; DOI=10.1152/ajprenal.00197.2004;
RA   Dudas P.L., Mentone S., Greineder C.F., Biemesderfer D., Aronson P.S.;
RT   "Immunolocalization of anion transporter Slc26a7 in mouse kidney.";
RL   Am. J. Physiol. 290:F937-F945(2006).
RN   [8] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16524946; DOI=10.1681/asn.2005111174;
RA   Xu J., Worrell R.T., Li H.C., Barone S.L., Petrovic S., Amlal H.,
RA   Soleimani M.;
RT   "Chloride/bicarbonate exchanger SLC26A7 is localized in endosomes in
RT   medullary collecting duct cells and is targeted to the basolateral membrane
RT   in hypertonicity and potassium depletion.";
RL   J. Am. Soc. Nephrol. 17:956-967(2006).
RN   [9]
RP   FUNCTION, TRANSPORTER ACTIVITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19723628; DOI=10.1074/jbc.m109.044396;
RA   Xu J., Song P., Nakamura S., Miller M., Barone S., Alper S.L., Riederer B.,
RA   Bonhagen J., Arend L.J., Amlal H., Seidler U., Soleimani M.;
RT   "Deletion of the chloride transporter slc26a7 causes distal renal tubular
RT   acidosis and impairs gastric acid secretion.";
RL   J. Biol. Chem. 284:29470-29479(2009).
RN   [10]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND ACTIVITY REGULATION.
RX   PubMed=24810589; DOI=10.1371/journal.pone.0097191;
RA   Kim K.X., Sanneman J.D., Kim H.M., Harbidge D.G., Xu J., Soleimani M.,
RA   Wangemann P., Marcus D.C.;
RT   "Slc26a7 chloride channel activity and localization in mouse Reissner's
RT   membrane epithelium.";
RL   PLoS ONE 9:e97191-e97191(2014).
RN   [11]
RP   FUNCTION, TRANSPORTER ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=30333321; DOI=10.1172/jci.insight.99631;
RA   Cangul H., Liao X.H., Schoenmakers E., Kero J., Barone S., Srichomkwun P.,
RA   Iwayama H., Serra E.G., Saglam H., Eren E., Tarim O., Nicholas A.K.,
RA   Zvetkova I., Anderson C.A., Frankl F.E.K., Boelaert K., Ojaniemi M.,
RA   Jaeaeskelaeinen J., Patyra K., Loef C., Williams E.D., Soleimani M.,
RA   Barrett T., Maher E.R., Chatterjee V.K., Refetoff S., Schoenmakers N.;
RT   "Homozygous loss-of-function mutations in SLC26A7 cause goitrous congenital
RT   hypothyroidism.";
RL   JCI Insight 3:0-0(2018).
RN   [12]
RP   FUNCTION, TRANSPORTER ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=32726161; DOI=10.1152/ajpcell.00027.2020;
RA   Cao X., Soleimani M., Hughes B.A.;
RT   "SLC26A7 constitutes the thiocyanate-selective anion conductance of the
RT   basolateral membrane of the retinal pigment epithelium.";
RL   Am. J. Physiol. 319:C641-C656(2020).
RN   [13]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=35788623; DOI=10.1038/s41598-022-15151-4;
RA   Yamaguchi N., Suzuki A., Yoshida A., Tanaka T., Aoyama K., Oishi H.,
RA   Hara Y., Ogi T., Amano I., Kameo S., Koibuchi N., Shibata Y., Ugawa S.,
RA   Mizuno H., Saitoh S.;
RT   "The iodide transporter Slc26a7 impacts thyroid function more strongly than
RT   Slc26a4 in mice.";
RL   Sci. Rep. 12:11259-11259(2022).
CC   -!- FUNCTION: Acts as an anion channel mediating the transport of chloride,
CC       bromide, iodide, nitrate, sulfate, gluconate, thiocyanate and
CC       bicarbonate ions (PubMed:15591059, PubMed:24810589, PubMed:30333321,
CC       PubMed:32726161, PubMed:35788623). Its permeability towards bicarbonate
CC       is weak and increases when pH is above 7 (PubMed:15591059). Mediates
CC       oxalate transport (By similarity). Mediates thiocyanate transport in
CC       retinal pigment epithelium cells (PubMed:32726161). Mediates iodide
CC       transport in the thyroid gland, playing an important role in the
CC       synthesis of thyroid hormones and the maintenance of thyroid function
CC       (PubMed:30333321, PubMed:35788623). Although it is an anion channel,
CC       according to PubMed:12736153 and PubMed:19723628 it has been shown to
CC       exhibit chloride-bicarbonate exchanger activity.
CC       {ECO:0000250|UniProtKB:Q8TE54, ECO:0000269|PubMed:12736153,
CC       ECO:0000269|PubMed:15591059, ECO:0000269|PubMed:19723628,
CC       ECO:0000269|PubMed:24810589, ECO:0000269|PubMed:30333321,
CC       ECO:0000269|PubMed:32726161, ECO:0000269|PubMed:35788623}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:15591059,
CC         ECO:0000269|PubMed:24810589};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324,
CC         ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:15591059,
CC         ECO:0000269|PubMed:24810589, ECO:0000269|PubMed:30333321,
CC         ECO:0000269|PubMed:35788623};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66326;
CC         Evidence={ECO:0000305|PubMed:35788623};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bromide(in) = bromide(out); Xref=Rhea:RHEA:75383,
CC         ChEBI:CHEBI:15858; Evidence={ECO:0000269|PubMed:15591059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxalate(in) = oxalate(out); Xref=Rhea:RHEA:76199,
CC         ChEBI:CHEBI:30623; Evidence={ECO:0000250|UniProtKB:Q8TE54};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=nitrate(in) = nitrate(out); Xref=Rhea:RHEA:34923,
CC         ChEBI:CHEBI:17632; Evidence={ECO:0000269|PubMed:15591059,
CC         ECO:0000269|PubMed:24810589};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sulfate(in) = sulfate(out); Xref=Rhea:RHEA:34983,
CC         ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:15591059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate(in) = hydrogencarbonate(out);
CC         Xref=Rhea:RHEA:28695, ChEBI:CHEBI:17544;
CC         Evidence={ECO:0000269|PubMed:15591059};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28697;
CC         Evidence={ECO:0000305|PubMed:15591059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate(in) = D-gluconate(out); Xref=Rhea:RHEA:76139,
CC         ChEBI:CHEBI:18391; Evidence={ECO:0000269|PubMed:15591059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=thiocyanate(in) = thiocyanate(out); Xref=Rhea:RHEA:75347,
CC         ChEBI:CHEBI:18022; Evidence={ECO:0000269|PubMed:32726161};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC         hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12736153,
CC         ECO:0000269|PubMed:19723628};
CC   -!- ACTIVITY REGULATION: Regulated by pH. Activity inhibited by all
CC       inhibitors of several anion channels and transporters, including 4,4'-
CC       Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS), diphenylamine-2-
CC       carboxylic acid, glybenclamide and 5-Nitro-2-(3-phenylpropyl-
CC       amino)benzoic acid. {ECO:0000269|PubMed:12736153,
CC       ECO:0000269|PubMed:15591059, ECO:0000269|PubMed:24810589}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805,
CC       ECO:0000269|PubMed:16524946, ECO:0000269|PubMed:19723628,
CC       ECO:0000269|PubMed:24810589, ECO:0000269|PubMed:30333321,
CC       ECO:0000269|PubMed:32726161}; Multi-pass membrane protein
CC       {ECO:0000255}. Recycling endosome membrane
CC       {ECO:0000269|PubMed:16524946}; Multi-pass membrane protein
CC       {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q8TE54};
CC       Multi-pass membrane protein {ECO:0000255}. Lateral cell membrane
CC       {ECO:0000250|UniProtKB:Q8TE54}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Expressed on the basolateral membrane of acid-
CC       secreting gastric parietal cells, distal nephron segments and apical
CC       domains of proximal tubules and in the glomerulus. Expressed in the
CC       cytoplasm in recycling endosomes of kidney outer medullary collecting
CC       duct cells and in acid-secreting gastric parietal cells. Targeted to
CC       the basolateral membrane in hypertonicity and potassium depletion.
CC       {ECO:0000250|UniProtKB:Q8TE54, ECO:0000269|PubMed:12736153,
CC       ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}.
CC   -!- TISSUE SPECIFICITY: Expressed in the Reissner's membrane epithelial
CC       cells in the cochlea (at protein level) (PubMed:24810589). Expressed in
CC       the retinal pigment epithelium (at protein level) (PubMed:32726161).
CC       Abundantly expressed in parietal cells on the glandular portion of the
CC       stomach. Lower levels are observed in the kidney, with expression in
CC       the proximal tubule and thick ascending limb of the loop of Henle. Also
CC       expressed in distal segments of nephron, in extraglomerular mesagial
CC       cells and a subpopulation of intercalated cells of outer medullary
CC       collecting ducts. Expressed in the thyroid gland.
CC       {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805,
CC       ECO:0000269|PubMed:16524946, ECO:0000269|PubMed:24810589,
CC       ECO:0000269|PubMed:30333321, ECO:0000269|PubMed:32726161}.
CC   -!- DISRUPTION PHENOTYPE: Mice develop goitrous congenital hypothyroidism,
CC       with enlarged thyroid gland and severely reduced T4 than T3 in the
CC       serum and thyroid gland (PubMed:30333321, PubMed:35788623). Animals fed
CC       a low iodine diet show more severe growth failure than those fed a
CC       normal diet (PubMed:35788623). Develop distal renal tubular acidosis,
CC       manifested by metabolic acidosis and alkaline urine pH and in the
CC       stomach, stimulated acid secretion is significantly impaired
CC       (PubMed:19723628). Retinal pigment epithelium cells (RPE) from Slc26a7
CC       KO mice have a dramatically smaller whole cell SCN (-) conductance
CC       compared with wild-type RPE cells (PubMed:32726161).
CC       {ECO:0000269|PubMed:19723628, ECO:0000269|PubMed:30333321,
CC       ECO:0000269|PubMed:32726161, ECO:0000269|PubMed:35788623}.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000255}.
CC   -!- CAUTION: Although it is an anion channel, according to PubMed:12736153
CC       and PubMed:19723628 it has been shown to exhibit chloride-bicarbonate
CC       exchanger activity. {ECO:0000269|PubMed:12736153,
CC       ECO:0000269|PubMed:19723628}.
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DR   EMBL; AF345194; AAO49172.1; -; mRNA.
DR   EMBL; AL772236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL772270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466538; EDL05611.1; -; Genomic_DNA.
DR   EMBL; BC026928; AAH26928.1; -; mRNA.
DR   CCDS; CCDS17979.1; -.
DR   RefSeq; NP_666059.2; NM_145947.2.
DR   AlphaFoldDB; Q8R2Z3; -.
DR   SMR; Q8R2Z3; -.
DR   BioGRID; 229021; 12.
DR   STRING; 10090.ENSMUSP00000041789; -.
DR   PhosphoSitePlus; Q8R2Z3; -.
DR   jPOST; Q8R2Z3; -.
DR   PaxDb; 10090-ENSMUSP00000041789; -.
DR   PeptideAtlas; Q8R2Z3; -.
DR   ProteomicsDB; 253375; -.
DR   Antibodypedia; 25657; 71 antibodies from 10 providers.
DR   DNASU; 208890; -.
DR   Ensembl; ENSMUST00000042221.14; ENSMUSP00000041789.8; ENSMUSG00000040569.14.
DR   GeneID; 208890; -.
DR   KEGG; mmu:208890; -.
DR   UCSC; uc008saz.2; mouse.
DR   AGR; MGI:2384791; -.
DR   CTD; 115111; -.
DR   MGI; MGI:2384791; Slc26a7.
DR   VEuPathDB; HostDB:ENSMUSG00000040569; -.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01100000263544; -.
DR   HOGENOM; CLU_003182_9_5_1; -.
DR   InParanoid; Q8R2Z3; -.
DR   OMA; FVDHTVM; -.
DR   OrthoDB; 1067648at2759; -.
DR   PhylomeDB; Q8R2Z3; -.
DR   TreeFam; TF313784; -.
DR   Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR   BioGRID-ORCS; 208890; 3 hits in 78 CRISPR screens.
DR   PRO; PR:Q8R2Z3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8R2Z3; Protein.
DR   Bgee; ENSMUSG00000040569; Expressed in vestibular membrane of cochlear duct and 174 other cell types or tissues.
DR   ExpressionAtlas; Q8R2Z3; baseline and differential.
DR   Genevisible; Q8R2Z3; MM.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IC:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB.
DR   GO; GO:0005253; F:monoatomic anion channel activity; IMP:MGI.
DR   GO; GO:0019531; F:oxalate transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
DR   GO; GO:0006821; P:chloride transport; IDA:MGI.
DR   GO; GO:0001696; P:gastric acid secretion; IDA:UniProtKB.
DR   GO; GO:0035429; P:gluconate transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0015705; P:iodide transport; IDA:UniProtKB.
DR   GO; GO:0006820; P:monoatomic anion transport; IMP:MGI.
DR   GO; GO:0015706; P:nitrate transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0019532; P:oxalate transport; IDA:UniProtKB.
DR   GO; GO:0008272; P:sulfate transport; IDA:UniProtKB.
DR   GO; GO:0006590; P:thyroid hormone generation; IMP:UniProtKB.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
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:SF75; ANION EXCHANGE TRANSPORTER; 1.
DR   PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
KW   Anion exchange; Cell membrane; Endosome; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..656
FT                   /note="Anion exchange transporter"
FT                   /id="PRO_0000320682"
FT   TOPO_DOM        1..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..144
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..343
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        426..448
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        470..656
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          492..641
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   REGION          641..656
FT                   /note="Membrane targeting"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TE54"
FT   CONFLICT        233
FT                   /note="F -> L (in Ref. 1; AAO49172 and 4; AAH26928)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        639
FT                   /note="S -> T (in Ref. 1; AAO49172 and 4; AAH26928)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   656 AA;  71829 MW;  321924A9BE7A1D0A CRC64;
     MTGAKRKKRS VLWGKMHTPH REDIKQWCKR RLPILEWAPQ YNLKENLLPD TVSGIMLAVQ
     QVAQGLSFAM LSSVHPVFGL YGSLFPAIIY AIFGMGRHVA TGTFALTSLI SANAVERLVP
     QSSRNLTTQS NSSVLGLSEF ELQRIGVAAA VSFLGGVIQL VMFVLQLGSA TFLLTEPVIS
     AMTTGAATHV VTSQVKYLLG IKMPYISGPL GFFYIYAYVF ENIKSVQLEA LLFSLLSIIV
     LVLVKELNEQ FKRKIKVVLP VDLVLIIAAS FACYCTNMEN TYGLEVVGHI PNGIPPPRAP
     PMNILSAVLT EAFGVALVGY VASLALAQGS AKKFKYSVDD NQEFLAHGLS NVIPSFLFCI
     PSAAAMGRTA GLYSTGAKTQ VACLISCIFV LIVIYAIGPL LYWLPMCVLA SIIVVGLKGM
     LIQFRDLKKY WNVDKIDWGI WISTYIFTIC FAANVGLLFG VICTIAIVLG RFPRAKTLSI
     TDMKEMELKV KTEMHDETSQ QIKIISINNP LVFLNAKKFS ADLMKIILKE SDSNQPLDDV
     SKCEQNTLLS SLSNGNCNEE ASQPCSSEKC SLVLNCSGLT FFDYTGVSTL VELYLDCKSR
     SVDVFLANCT ASLIKAMTYY GDLDTEKPIF FDSVPAAISI IQSNKNLSKA SDHSEV
//
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