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 27-MAR-2024, entry version 143. DE RecName: Full=Anion exchange transporter; DE AltName: Full=Solute carrier family 26 member 7; GN Name=Slc26a7 {ECO:0000312|EMBL:AAH26928.1, GN 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; LDWSFIQ; -. 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 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. DR Genevisible; Q8R2Z3; MM. 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 //