ID S6A18_MOUSE Reviewed; 615 AA. AC O88576; O88577; O88578; O88579; O88580; O88581; Q91XG6; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 156. DE RecName: Full=Sodium-dependent neutral amino acid transporter B(0)AT3 {ECO:0000303|PubMed:19478081}; DE AltName: Full=Sodium- and chloride-dependent transporter XTRP2; DE AltName: Full=Solute carrier family 6 member 18; DE AltName: Full=System B(0) neutral amino acid transporter AT3; GN Name=Slc6a18 {ECO:0000312|MGI:MGI:1336892}; GN Synonyms=B0at3 {ECO:0000303|PubMed:19478081}, Xt2 GN {ECO:0000303|PubMed:15121838}, Xtrp2; 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] (ISOFORMS 1; 2; 3; 4; 5 AND 6), AND TISSUE RP SPECIFICITY. RC TISSUE=Kidney; RX PubMed=9932288; RA Nash S.R., Giros B., Kingsmore S.F., Kim K.M., El-Mestikawy S., Dong Q., RA Fumagalli F., Seldin M.F., Caron M.G.; RT "Cloning, gene structure, and genomic localization of an orphan transporter RT from mouse kidney with six alternatively-spliced isoforms."; RL Recept. Channels 6:113-128(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Kidney; 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 [3] RP DISRUPTION PHENOTYPE. RX PubMed=15121838; DOI=10.1128/mcb.24.10.4166-4173.2004; RA Quan H., Athirakul K., Wetsel W.C., Torres G.E., Stevens R., Chen Y.T., RA Coffman T.M., Caron M.G.; RT "Hypertension and impaired glycine handling in mice lacking the orphan RT transporter XT2."; RL Mol. Cell. Biol. 24:4166-4173(2004). RN [4] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH RP CLTRN. RX PubMed=19478081; DOI=10.1074/jbc.m109.011171; RA Singer D., Camargo S.M., Huggel K., Romeo E., Danilczyk U., Kuba K., RA Chesnov S., Caron M.G., Penninger J.M., Verrey F.; RT "Orphan transporter SLC6A18 is renal neutral amino acid transporter RT B0AT3."; RL J. Biol. Chem. 284:19953-19960(2009). RN [5] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=20377526; DOI=10.1042/bj20091667; RA Vanslambrouck J.M., Broeer A., Thavyogarajah T., Holst J., Bailey C.G., RA Broeer S., Rasko J.E.; RT "Renal imino acid and glycine transport system ontogeny and involvement in RT developmental iminoglycinuria."; RL Biochem. J. 428:397-407(2010). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF ASP-21; GLN-25; HIS-50; TYR-72; GLY-78; RP LYS-90; SER-158; LEU-213; ARG-225; ASN-283; ASP-287; SER-296; MET-297; RP ILE-456; GLY-464; LEU-477; GLY-495; ASP-502 AND GLN-568. RX PubMed=26240152; DOI=10.1074/jbc.m115.648519; RA Fairweather S.J., Broeer A., Subramanian N., Tumer E., Cheng Q., RA Schmoll D., O'Mara M.L., Broeer S.; RT "Molecular basis for the interaction of the mammalian amino acid RT transporters B0AT1 and B0AT3 with their ancillary protein collectrin."; RL J. Biol. Chem. 290:24308-24325(2015). CC -!- FUNCTION: Symporter that transports one amino acid molecule together CC with two sodium and one chloride ions in kidneys and plays a role in CC the neutral amino acids reabsorption (PubMed:19478081, PubMed:26240152, CC PubMed:20377526). Preferentially transports neutral amino acids such as CC L-glycine and L-alanine but also other neutral amino acids CC (PubMed:19478081, PubMed:26240152, PubMed:20377526). Required CLTRN for CC cell surface expression and for its amino acid transporter activity CC (PubMed:26240152, PubMed:20377526). The transport mechanism is pH- CC independent (PubMed:19478081). {ECO:0000269|PubMed:19478081, CC ECO:0000269|PubMed:20377526, ECO:0000269|PubMed:26240152}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + L-alanine(out) + 2 Na(+)(out) = chloride(in) + CC L-alanine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71311, ChEBI:CHEBI:17996, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; CC Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526, CC ECO:0000269|PubMed:26240152}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) + CC glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57305; CC Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + L-methionine(out) + 2 Na(+)(out) = CC chloride(in) + L-methionine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71303, CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844; CC Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + L-valine(out) + 2 Na(+)(out) = chloride(in) + CC L-valine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71307, ChEBI:CHEBI:17996, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57762; CC Evidence={ECO:0000269|PubMed:19478081}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + L-isoleucine(out) + 2 Na(+)(out) = CC chloride(in) + L-isoleucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71299, CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045; CC Evidence={ECO:0000269|PubMed:19478081}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + L-serine(out) + 2 Na(+)(out) = chloride(in) + CC L-serine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71315, ChEBI:CHEBI:17996, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; CC Evidence={ECO:0000269|PubMed:19478081}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + L-leucine(out) + 2 Na(+)(out) = chloride(in) + CC L-leucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71279, ChEBI:CHEBI:17996, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57427; CC Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.79 mM for L-alanine (in the presence of CLTRN) CC {ECO:0000269|PubMed:26240152}; CC KM=0.14 mM for L-alanine (in the presence of ACE2) CC {ECO:0000269|PubMed:26240152}; CC KM=0.99 mM for L-glycine (in the presence of CLTRN) CC {ECO:0000269|PubMed:26240152}; CC KM=0.27 mM for L-glycine (in the presence of ACE2) CC {ECO:0000269|PubMed:26240152}; CC KM=0.9 mM for L-alanine (in the presence of CLTRN) CC {ECO:0000269|PubMed:20377526}; CC KM=2.3 mM for L-glycine (in the presence of CLTRN) CC {ECO:0000269|PubMed:20377526}; CC -!- SUBUNIT: Interacts with CLTRN; this interaction regulates the CC trafficking of SLC6A18 to the cell membrane and its activity. CC {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:26240152}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; Multi-pass CC membrane protein {ECO:0000255}. Cell membrane CC {ECO:0000269|PubMed:20377526, ECO:0000269|PubMed:26240152}; Multi-pass CC membrane protein {ECO:0000255}. Note=In kidneys localizes to the apical CC membrane in distal segments of the proximal tubule (PubMed:19478081, CC PubMed:20377526). Cell membrane expression is CLTRN-dependent CC (PubMed:20377526). {ECO:0000269|PubMed:19478081, CC ECO:0000269|PubMed:20377526}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=A12; CC IsoId=O88576-1; Sequence=Displayed; CC Name=2; Synonyms=A11; CC IsoId=O88576-2; Sequence=VSP_050365; CC Name=3; Synonyms=B11; CC IsoId=O88576-3; Sequence=VSP_050364; CC Name=4; Synonyms=A10; CC IsoId=O88576-4; Sequence=VSP_050366, VSP_050367; CC Name=5; Synonyms=B9; CC IsoId=O88576-5; Sequence=VSP_050364, VSP_050366, VSP_050367; CC Name=6; Synonyms=A8; CC IsoId=O88576-6; Sequence=VSP_050363, VSP_050697; CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney. CC {ECO:0000269|PubMed:9932288}. CC -!- DEVELOPMENTAL STAGE: Barely detectable at post natal day 0, reaching CC maximum expression after the third week of life. CC {ECO:0000269|PubMed:20377526}. CC -!- DISRUPTION PHENOTYPE: Animals lacking this protein exhibit no gross CC abnormalities and grow to adulthood, although they do exhibit CC hypertension. The elevated blood pressure appears to be attributable to CC a decreased level of renal glycine. High-affinity renal reabsorption of CC glycine is eliminated and intrarenal glycine concentration is reduced. CC {ECO:0000269|PubMed:15121838}. CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) CC (TC 2.A.22) family. SLC6A18 subfamily. {ECO:0000305}. CC -!- CAUTION: Human SLC6A18 has been shown to be an inactive protein. CC {ECO:0000269|PubMed:26240152}. 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; AF075262; AAC27757.1; -; mRNA. DR EMBL; AF075263; AAC27758.1; -; mRNA. DR EMBL; AF075264; AAC27759.1; -; mRNA. DR EMBL; AF075265; AAC27760.1; -; mRNA. DR EMBL; AF075266; AAC27761.1; -; mRNA. DR EMBL; AF075267; AAC27762.1; -; mRNA. DR EMBL; BC010748; AAH10748.1; -; mRNA. DR CCDS; CCDS36727.1; -. [O88576-1] DR CCDS; CCDS49311.1; -. [O88576-3] DR CCDS; CCDS49312.1; -. [O88576-4] DR CCDS; CCDS88479.1; -. [O88576-5] DR CCDS; CCDS88481.1; -. [O88576-2] DR RefSeq; NP_001035782.1; NM_001040692.3. [O88576-1] DR RefSeq; NP_001129559.1; NM_001136087.2. [O88576-3] DR RefSeq; NP_001162115.1; NM_001168644.1. [O88576-4] DR RefSeq; NP_001162116.1; NM_001168645.1. [O88576-5] DR RefSeq; NP_001162117.1; NM_001168646.1. [O88576-2] DR AlphaFoldDB; O88576; -. DR SMR; O88576; -. DR DIP; DIP-60421N; -. DR IntAct; O88576; 1. DR STRING; 10090.ENSMUSP00000152525; -. DR GlyCosmos; O88576; 1 site, No reported glycans. DR GlyGen; O88576; 3 sites. DR iPTMnet; O88576; -. DR PhosphoSitePlus; O88576; -. DR jPOST; O88576; -. DR PaxDb; 10090-ENSMUSP00000022105; -. DR ProteomicsDB; 260802; -. [O88576-1] DR ProteomicsDB; 260803; -. [O88576-2] DR ProteomicsDB; 260804; -. [O88576-3] DR ProteomicsDB; 260805; -. [O88576-4] DR ProteomicsDB; 260806; -. [O88576-5] DR ProteomicsDB; 260807; -. [O88576-6] DR Antibodypedia; 1938; 96 antibodies from 23 providers. DR DNASU; 22598; -. DR Ensembl; ENSMUST00000109679.4; ENSMUSP00000105301.3; ENSMUSG00000021612.16. [O88576-4] DR Ensembl; ENSMUST00000109680.10; ENSMUSP00000105302.3; ENSMUSG00000021612.16. [O88576-3] DR Ensembl; ENSMUST00000220650.2; ENSMUSP00000152403.2; ENSMUSG00000021612.16. [O88576-5] DR Ensembl; ENSMUST00000222029.2; ENSMUSP00000152525.2; ENSMUSG00000021612.16. [O88576-1] DR Ensembl; ENSMUST00000223026.2; ENSMUSP00000152516.2; ENSMUSG00000021612.16. [O88576-6] DR Ensembl; ENSMUST00000223074.2; ENSMUSP00000152146.2; ENSMUSG00000021612.16. [O88576-2] DR GeneID; 22598; -. DR KEGG; mmu:22598; -. DR UCSC; uc007rds.2; mouse. [O88576-1] DR UCSC; uc007rdt.2; mouse. [O88576-2] DR UCSC; uc007rdu.2; mouse. [O88576-3] DR UCSC; uc007rdv.2; mouse. [O88576-4] DR UCSC; uc007rdw.2; mouse. [O88576-5] DR AGR; MGI:1336892; -. DR CTD; 348932; -. DR MGI; MGI:1336892; Slc6a18. DR VEuPathDB; HostDB:ENSMUSG00000021612; -. DR eggNOG; KOG3659; Eukaryota. DR GeneTree; ENSGT00940000158906; -. DR HOGENOM; CLU_006855_7_2_1; -. DR InParanoid; O88576; -. DR OMA; VLTWVMW; -. DR OrthoDB; 3084493at2759; -. DR PhylomeDB; O88576; -. DR TreeFam; TF343812; -. DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane. DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters. DR BioGRID-ORCS; 22598; 2 hits in 75 CRISPR screens. DR ChiTaRS; Slc6a18; mouse. DR PRO; PR:O88576; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; O88576; Protein. DR Bgee; ENSMUSG00000021612; Expressed in right kidney and 33 other cell types or tissues. DR ExpressionAtlas; O88576; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0031526; C:brush border membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0140931; F:neutral L-amino acid:sodium:chloride symporter activity; IDA:UniProtKB. DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:MGI. DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW. DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB. DR GO; GO:1990297; P:renal amino acid absorption; IMP:UniProtKB. DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central. DR CDD; cd11517; SLC6sbd_B0AT3; 1. DR InterPro; IPR042701; B0AT3_SLC6sbd. DR InterPro; IPR000175; Na/ntran_symport. DR InterPro; IPR002438; Neutral_aa_SLC6. DR InterPro; IPR037272; SNS_sf. DR PANTHER; PTHR11616:SF109; INACTIVE SODIUM-DEPENDENT NEUTRAL AMINO ACID TRANSPORTER B(0)AT3; 1. DR PANTHER; PTHR11616; SODIUM/CHLORIDE DEPENDENT TRANSPORTER; 1. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR PRINTS; PR01206; ORPHTRNSPORT. DR SUPFAM; SSF161070; SNF-like; 1. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. DR Genevisible; O88576; MM. PE 1: Evidence at protein level; KW Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein; KW Membrane; Neurotransmitter transport; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..615 FT /note="Sodium-dependent neutral amino acid transporter FT B(0)AT3" FT /id="PRO_0000214807" FT TOPO_DOM 1..26 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 27..47 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 48..52 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 53..73 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 74..105 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 106..126 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 127..177 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 178..198 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 199..206 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 207..227 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 228..255 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 256..276 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 277..288 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 289..309 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 310..397 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 398..418 FT /note="Helical; Name=8" FT /evidence="ECO:0000255" FT TOPO_DOM 419..441 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 442..462 FT /note="Helical; Name=9" FT /evidence="ECO:0000255" FT TOPO_DOM 463..472 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 473..493 FT /note="Helical; Name=10" FT /evidence="ECO:0000255" FT TOPO_DOM 494..520 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 521..541 FT /note="Helical; Name=11" FT /evidence="ECO:0000255" FT TOPO_DOM 542..570 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 571..591 FT /note="Helical; Name=12" FT /evidence="ECO:0000255" FT TOPO_DOM 592..615 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 167 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 353 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 377..444 FT /note="SASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNMEGVITPL FT LDMGILPKGIPKEVMT -> PTWKQISGARVLGEGCARLTSRVCEASVLP (in FT isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9932288" FT /id="VSP_050364" FT VAR_SEQ 377..422 FT /note="SASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNME -> VL FT LCGLCSSLGCCLPWVCPPCLGTWRVSLHHYWTWGSYPKVYPRRS (in isoform FT 6)" FT /evidence="ECO:0000303|PubMed:9932288" FT /id="VSP_050363" FT VAR_SEQ 423..615 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:9932288" FT /id="VSP_050697" FT VAR_SEQ 445..454 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9932288" FT /id="VSP_050365" FT VAR_SEQ 499..552 FT /note="FCDDIEWMTGRRPGLYWQVTWRVVSPMLLFGIFLSYIVLLIQTPPSYKAWNP FT QY -> NIFPQERRSSTQAGCRSPVCSCPSCPHCGSLELLWLSYCPSTNRGGRLRIWKV FT V (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:9932288" FT /id="VSP_050366" FT VAR_SEQ 553..615 FT /note="Missing (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:9932288" FT /id="VSP_050367" FT MUTAGEN 21 FT /note="D->N: No effect on protein abundance. Increases FT localization to the cell membrane. Increases alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 25 FT /note="Q->D: No effect on protein abundance. Almost FT complete loss of cell surface localization. Decreases FT alanine uptake activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 25 FT /note="Q->V: No effect on protein abundance. Strong FT decrease of cell surface localization. Decreases alanine FT uptake." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 50 FT /note="H->Y: No effect on protein abundance. No effect on FT cell surface localization. Increases alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 72 FT /note="Y->H: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 78 FT /note="G->S: No effect on protein abundance. No effect on FT cell surface expression. Decreases alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 90 FT /note="K->T: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 158 FT /note="S->D: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 213 FT /note="L->W: No effect on protein abundance. No effect on FT cell surface localization. Decreases alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 225 FT /note="R->T: No effect on protein abundance. Strong FT decreases of cell surface localization. Decreases alanine FT uptake." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 283 FT /note="N->D: No effect on protein abundance. Strong FT decreases of cell surface localization. Decreases alanine FT uptake." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 287 FT /note="D->K: No effect on protein abundance. Strong FT decreases of cell surface localization. Decreases alanine FT uptake." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 287 FT /note="D->N: No effect on protein abundance. Strong FT decreases of cell surface localization. Decreases alanine FT uptake activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 296 FT /note="S->R: No effect on protein abundance. Strong FT decreases of cell surface localization. Decreases alanine FT uptake activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 297 FT /note="M->C: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 297 FT /note="M->S: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 456 FT /note="I->T: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 464 FT /note="G->N: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 477 FT /note="L->P: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 495 FT /note="G->R: No effect on protein abundance. Strong FT decreases of cell surface localization. Decreases alanine FT uptake activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 502 FT /note="D->N: Decreases protein abundance. Strong decreases FT of cell surface localization. Strong decreases on alanine FT uptake activity." FT /evidence="ECO:0000269|PubMed:26240152" FT MUTAGEN 568 FT /note="Q->R: No effect on protein abundance. No effect on FT cell surface localization. No effect on alanine uptake FT activity." FT /evidence="ECO:0000269|PubMed:26240152" SQ SEQUENCE 615 AA; 69229 MW; A7925C0397FC63F8 CRC64; MAQASGMDPL VDIEDERPKW DNKLQYLLSC IGFAVGLGNI WRFPYLCQTH GGGAFLIPYF IALVFEGIPL FYIELAIGQR LRRGSIGVWK TISPYLGGVG LGCFSVSFLV SLYYNTVLLW VLWFFLNSFQ HPLPWSTCPL DLNRTGFVQE CQSSGTVSYF WYRQTLNITS DISNTGTIQW KLFLCLVACW STVYLCVIRG IESTGKVIYF TALFPYLVLT IFLIRGLTLP GATEGLIYLF TPNMKTLQNP RVWLDAATQI FFSLSLAFGG HIAFASYNPP RNNCEKDAVI IALVNSMTSL YASIAIFSVM GFKASNDYGR CLDRNILSLI NEFDLPELSI SRDEYPSVLM YLNATQTARV AQLPLKTCHL EDFLDKSASG PGLAFIVFTE AVLHMPGASV WSVLFFGMLF TLGLSSMFGN MEGVITPLLD MGILPKGIPK EVMTGVICFA CFLSAICFTL QSGGYWLEIF DSFAASLNLI IFAFMEVVGV IHIYGMKRFC DDIEWMTGRR PGLYWQVTWR VVSPMLLFGI FLSYIVLLIQ TPPSYKAWNP QYEHFPSREE KFYPGWVQVT CVLLSFLPSL WVPGVALAQL LSQYKQRWKA THLESGLKLQ ESRGC //