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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//