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Neutral amino acid transporter A (Alanine/serine/cysteine/threonine transporter 1) (ASCT-1) (SATT) (Solute carrier family 1 member 4)

 SATT_HUMAN              Reviewed;         532 AA.
P43007; B7Z3C0; D6W5F0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 162.
RecName: Full=Neutral amino acid transporter A;
AltName: Full=Alanine/serine/cysteine/threonine transporter 1;
Short=ASCT-1;
AltName: Full=SATT;
AltName: Full=Solute carrier family 1 member 4;
Name=SLC1A4; Synonyms=ASCT1, SATT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain cortex;
PubMed=8101838;
Arriza J.L., Kavanaugh M.P., Fairman W.A., Wu Y.-N., Murdoch G.H.,
North R.A., Amara S.G.;
"Cloning and expression of a human neutral amino acid transporter with
structural similarity to the glutamate transporter gene family.";
J. Biol. Chem. 268:15329-15332(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
PubMed=8340364;
Shafqat S., Tamarappoo B.K., Kilberg M.S., Puranam R.S.,
McNamara J.O., Guadano-Ferraz A., Fremeau R.T. Jr.;
"Cloning and expression of a novel Na(+)-dependent neutral amino acid
transporter structurally related to mammalian Na+/glutamate
cotransporters.";
J. Biol. Chem. 268:15351-15355(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7896285; DOI=10.1006/geno.1994.1577;
Hofmann K., Dueker M., Fink T., Lichter P., Stoffel W.;
"Human neutral amino acid transporter ASCT1: structure of the gene
(SLC1A4) and localization to chromosome 2p13-p15.";
Genomics 24:20-26(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201 AND ASN-206.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
INVOLVEMENT IN SPATCCM, AND VARIANT SPATCCM LYS-256.
PubMed=25930971; DOI=10.1111/cge.12605;
Srour M., Hamdan F.F., Gan-Or Z., Labuda D., Nassif C., Oskoui M.,
Gana-Weisz M., Orr-Urtreger A., Rouleau G.A., Michaud J.L.;
"A homozygous mutation in SLC1A4 in siblings with severe intellectual
disability and microcephaly.";
Clin. Genet. 88:E1-E4(2015).
[17]
INVOLVEMENT IN SPATCCM, AND VARIANT SPATCCM LYS-256.
PubMed=26138499; DOI=10.1111/cge.12637;
Heimer G., Marek-Yagel D., Eyal E., Barel O., Oz Levi D., Hoffmann C.,
Ruzzo E.K., Ganelin-Cohen E., Lancet D., Pras E., Rechavi G.,
Nissenkorn A., Anikster Y., Goldstein D.B., Ben Zeev B.;
"SLC1A4 mutations cause a novel disorder of intellectual disability,
progressive microcephaly, spasticity and thin corpus callosum.";
Clin. Genet. 88:327-335(2015).
[18]
FUNCTION, INVOLVEMENT IN SPATCCM, VARIANTS SPATCCM LYS-256 AND
TRP-457, AND CHARACTERIZATION OF VARIANTS SPATCCM LYS-256 AND TRP-457.
PubMed=26041762; DOI=10.1136/jmedgenet-2015-103104;
Damseh N., Simonin A., Jalas C., Picoraro J.A., Shaag A., Cho M.T.,
Yaacov B., Neidich J., Al-Ashhab M., Juusola J., Bale S.,
Telegrafi A., Retterer K., Pappas J.G., Moran E., Cappell J.,
Anyane Yeboa K., Abu-Libdeh B., Hediger M.A., Chung W.K., Elpeleg O.,
Edvardson S.;
"Mutations in SLC1A4, encoding the brain serine transporter, are
associated with developmental delay, microcephaly and
hypomyelination.";
J. Med. Genet. 52:541-547(2015).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Transporter for alanine, serine, cysteine, and
threonine. Exhibits sodium dependence.
{ECO:0000269|PubMed:26041762}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17081065};
Multi-pass membrane protein {ECO:0000269|PubMed:17081065}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P43007-1; Sequence=Displayed;
Name=2;
IsoId=P43007-2; Sequence=VSP_042880, VSP_042881;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed mostly in brain, muscle, and
pancreas but detected in all tissues examined.
-!- DISEASE: Spastic tetraplegia, thin corpus callosum, and
progressive microcephaly (SPATCCM) [MIM:616657]: A
neurodevelopmental disorder characterized by thin corpus callosum,
severe progressive microcephaly, severe intellectual disability,
seizures, spasticity, and global developmental delay. Most
patients are unable to achieve independent walking or speech.
{ECO:0000269|PubMed:25930971, ECO:0000269|PubMed:26041762,
ECO:0000269|PubMed:26138499}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. SLC1A4 subfamily.
{ECO:0000305}.
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EMBL; L14595; AAA02761.1; -; mRNA.
EMBL; L19444; AAA19438.1; -; mRNA.
EMBL; U05235; AAC51349.1; -; Genomic_DNA.
EMBL; U05229; AAC51349.1; JOINED; Genomic_DNA.
EMBL; U05230; AAC51349.1; JOINED; Genomic_DNA.
EMBL; U05231; AAC51349.1; JOINED; Genomic_DNA.
EMBL; U05232; AAC51349.1; JOINED; Genomic_DNA.
EMBL; U05233; AAC51349.1; JOINED; Genomic_DNA.
EMBL; U05234; AAC51349.1; JOINED; Genomic_DNA.
EMBL; AK295687; BAH12156.1; -; mRNA.
EMBL; AC007386; AAF03519.1; -; Genomic_DNA.
EMBL; CH471053; EAW99932.1; -; Genomic_DNA.
EMBL; CH471053; EAW99933.1; -; Genomic_DNA.
EMBL; BC026216; AAH26216.1; -; mRNA.
EMBL; BC072423; AAH72423.1; -; mRNA.
CCDS; CCDS1879.1; -. [P43007-1]
CCDS; CCDS54362.1; -. [P43007-2]
PIR; I37188; I37188.
PIR; I55389; I55389.
RefSeq; NP_001180422.1; NM_001193493.1. [P43007-2]
RefSeq; NP_003029.2; NM_003038.4. [P43007-1]
UniGene; Hs.654352; -.
ProteinModelPortal; P43007; -.
BioGrid; 112400; 5.
IntAct; P43007; 1.
MINT; MINT-4656683; -.
STRING; 9606.ENSP00000234256; -.
DrugBank; DB00160; L-Alanine.
TCDB; 2.A.23.3.1; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
iPTMnet; P43007; -.
PhosphoSitePlus; P43007; -.
SwissPalm; P43007; -.
BioMuta; SLC1A4; -.
DMDM; 1173365; -.
EPD; P43007; -.
MaxQB; P43007; -.
PaxDb; P43007; -.
PeptideAtlas; P43007; -.
PRIDE; P43007; -.
DNASU; 6509; -.
Ensembl; ENST00000234256; ENSP00000234256; ENSG00000115902. [P43007-1]
Ensembl; ENST00000531327; ENSP00000431942; ENSG00000115902. [P43007-2]
GeneID; 6509; -.
KEGG; hsa:6509; -.
UCSC; uc010ypz.3; human. [P43007-1]
CTD; 6509; -.
DisGeNET; 6509; -.
EuPathDB; HostDB:ENSG00000115902.10; -.
GeneCards; SLC1A4; -.
HGNC; HGNC:10942; SLC1A4.
HPA; HPA034963; -.
HPA; HPA034964; -.
MalaCards; SLC1A4; -.
MIM; 600229; gene.
MIM; 616657; phenotype.
neXtProt; NX_P43007; -.
OpenTargets; ENSG00000115902; -.
PharmGKB; PA35829; -.
eggNOG; KOG3787; Eukaryota.
eggNOG; COG1301; LUCA.
GeneTree; ENSGT00760000119117; -.
HOGENOM; HOG000208776; -.
HOVERGEN; HBG000080; -.
InParanoid; P43007; -.
KO; K05615; -.
OMA; ISHIGER; -.
OrthoDB; EOG091G0UCE; -.
PhylomeDB; P43007; -.
TreeFam; TF315206; -.
Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
ChiTaRS; SLC1A4; human.
GeneWiki; SLC1A4; -.
GenomeRNAi; 6509; -.
PMAP-CutDB; P43007; -.
PRO; PR:P43007; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115902; -.
CleanEx; HS_SLC1A4; -.
Genevisible; P43007; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015184; F:L-cystine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015186; F:L-glutamine transmembrane transporter activity; TAS:BHF-UCL.
GO; GO:0034590; F:L-hydroxyproline transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015195; F:L-threonine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0006865; P:amino acid transport; TAS:Reactome.
GO; GO:0050890; P:cognition; IMP:UniProtKB.
GO; GO:0006868; P:glutamine transport; TAS:BHF-UCL.
GO; GO:0034589; P:hydroxyproline transport; IDA:UniProtKB.
GO; GO:0015808; P:L-alanine transport; IDA:UniProtKB.
GO; GO:0015811; P:L-cystine transport; IDA:UniProtKB.
GO; GO:0015825; P:L-serine transport; IDA:UniProtKB.
GO; GO:0015824; P:proline transport; IDA:UniProtKB.
GO; GO:0035249; P:synaptic transmission, glutamatergic; NAS:UniProtKB.
GO; GO:0015826; P:threonine transport; IDA:UniProtKB.
Gene3D; 1.10.3860.10; -; 1.
InterPro; IPR036458; Na-dicarbo_symporter_sf.
InterPro; IPR001991; Na-dicarboxylate_symporter.
InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
Pfam; PF00375; SDF; 1.
PRINTS; PR00173; EDTRNSPORT.
SUPFAM; SSF118215; SSF118215; 2.
PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Epilepsy; Glycoprotein; Membrane;
Mental retardation; Phosphoprotein; Polymorphism; Reference proteome;
Symport; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 532 Neutral amino acid transporter A.
/FTId=PRO_0000202079.
TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.
TRANSMEM 42 62 Helical. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TRANSMEM 119 139 Helical. {ECO:0000255}.
TOPO_DOM 140 216 Extracellular. {ECO:0000255}.
TRANSMEM 217 237 Helical. {ECO:0000255}.
TRANSMEM 257 277 Helical. {ECO:0000255}.
TRANSMEM 298 318 Helical. {ECO:0000255}.
TRANSMEM 328 348 Helical. {ECO:0000255}.
TRANSMEM 373 393 Helical. {ECO:0000255}.
TRANSMEM 418 438 Helical. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000250|UniProtKB:O35874}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000250|UniProtKB:O35874}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
VAR_SEQ 1 220 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042880.
VAR_SEQ 267 345 WYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFASILGHVI
HGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSS ->
C (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042881.
VARIANT 37 37 G -> R (in dbSNP:rs1064512).
/FTId=VAR_011878.
VARIANT 256 256 E -> K (in SPATCCM; does not affect
localization at the cell surface;
decreased uptake of L-serine and L-
alanine; Vmax is decreased by at least
50% for both substrates; 3-fold increase
of affinity for L-serine; 2-fold increase
of affinity for L-alanine;
dbSNP:rs201278558).
{ECO:0000269|PubMed:25930971,
ECO:0000269|PubMed:26041762,
ECO:0000269|PubMed:26138499}.
/FTId=VAR_075085.
VARIANT 399 399 V -> I (in dbSNP:rs759458).
/FTId=VAR_011879.
VARIANT 457 457 R -> W (in SPATCCM; does not affect
localization at the cell surface; loss of
uptake of L-serine and L-alanine;
dbSNP:rs761533681).
{ECO:0000269|PubMed:26041762}.
/FTId=VAR_075086.
CONFLICT 117 117 A -> R (in Ref. 1; AAA02761).
{ECO:0000305}.
CONFLICT 127 127 S -> T (in Ref. 2; AAA19438).
{ECO:0000305}.
SEQUENCE 532 AA; 55723 MW; 57925860042FCEB6 CRC64;
MEKSNETNGY LDSAQAGPAA GPGAPGTAAG RARRCAGFLR RQALVLLTVS GVLAGAGLGA
ALRGLSLSRT QVTYLAFPGE MLLRMLRMII LPLVVCSLVS GAASLDASCL GRLGGIAVAY
FGLTTLSASA LAVALAFIIK PGSGAQTLQS SDLGLEDSGP PPVPKETVDS FLDLARNLFP
SNLVVAAFRT YATDYKVVTQ NSSSGNVTHE KIPIGTEIEG MNILGLVLFA LVLGVALKKL
GSEGEDLIRF FNSLNEATMV LVSWIMWYVP VGIMFLVGSK IVEMKDIIVL VTSLGKYIFA
SILGHVIHGG IVLPLIYFVF TRKNPFRFLL GLLAPFATAF ATCSSSATLP SMMKCIEENN
GVDKRISRFI LPIGATVNMD GAAIFQCVAA VFIAQLNNVE LNAGQIFTIL VTATASSVGA
AGVPAGGVLT IAIILEAIGL PTHDLPLILA VDWIVDRTTT VVNVEGDALG AGILHHLNQK
ATKKGEQELA EVKVEAIPNC KSEEETSPLV THQNPAGPVA SAPELESKES VL


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