ID SATT_HUMAN Reviewed; 532 AA. AC P43007; B7Z3C0; D6W5F0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 198. DE RecName: Full=Neutral amino acid transporter A {ECO:0000303|PubMed:8101838}; DE AltName: Full=Alanine/serine/cysteine/threonine transporter 1 {ECO:0000303|PubMed:7896285}; DE Short=ASCT-1 {ECO:0000303|PubMed:7896285}; DE AltName: Full=Solute carrier family 1 member 4; GN Name=SLC1A4 {ECO:0000303|PubMed:7896285, ECO:0000312|HGNC:HGNC:10942}; GN Synonyms=ASCT1 {ECO:0000303|PubMed:7896285}, SATT GN {ECO:0000303|PubMed:8340364}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND RP SUBCELLULAR LOCATION. RC TISSUE=Brain cortex; RX PubMed=8101838; DOI=10.1016/s0021-9258(18)82257-8; RA Arriza J.L., Kavanaugh M.P., Fairman W.A., Wu Y.-N., Murdoch G.H., RA North R.A., Amara S.G.; RT "Cloning and expression of a human neutral amino acid transporter with RT structural similarity to the glutamate transporter gene family."; RL J. Biol. Chem. 268:15329-15332(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TRANSPORTER ACTIVITY. RC TISSUE=Hippocampus; RX PubMed=8340364; DOI=10.1016/s0021-9258(18)82263-3; RA Shafqat S., Tamarappoo B.K., Kilberg M.S., Puranam R.S., McNamara J.O., RA Guadano-Ferraz A., Fremeau R.T. Jr.; RT "Cloning and expression of a novel Na(+)-dependent neutral amino acid RT transporter structurally related to mammalian Na+/glutamate RT cotransporters."; RL J. Biol. Chem. 268:15351-15355(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX PubMed=7896285; DOI=10.1006/geno.1994.1577; RA Hofmann K., Dueker M., Fink T., Lichter P., Stoffel W.; RT "Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) RT and localization to chromosome 2p13-p15."; RL Genomics 24:20-26(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, and PNS; 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 [8] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=14502423; DOI=10.1007/s00232-003-2041-9; RA Pinilla-Tenas J., Barber A., Lostao M.P.; RT "Transport of proline and hydroxyproline by the neutral amino-acid RT exchanger ASCT1."; RL J. Membr. Biol. 195:27-32(2003). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201 AND ASN-206. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP INVOLVEMENT IN SPATCCM, AND VARIANT SPATCCM LYS-256. RX PubMed=25930971; DOI=10.1111/cge.12605; RA Srour M., Hamdan F.F., Gan-Or Z., Labuda D., Nassif C., Oskoui M., RA Gana-Weisz M., Orr-Urtreger A., Rouleau G.A., Michaud J.L.; RT "A homozygous mutation in SLC1A4 in siblings with severe intellectual RT disability and microcephaly."; RL Clin. Genet. 88:E1-E4(2015). RN [18] RP INVOLVEMENT IN SPATCCM, AND VARIANT SPATCCM LYS-256. RX PubMed=26138499; DOI=10.1111/cge.12637; RA Heimer G., Marek-Yagel D., Eyal E., Barel O., Oz Levi D., Hoffmann C., RA Ruzzo E.K., Ganelin-Cohen E., Lancet D., Pras E., Rechavi G., RA Nissenkorn A., Anikster Y., Goldstein D.B., Ben Zeev B.; RT "SLC1A4 mutations cause a novel disorder of intellectual disability, RT progressive microcephaly, spasticity and thin corpus callosum."; RL Clin. Genet. 88:327-335(2015). RN [19] RP FUNCTION, INVOLVEMENT IN SPATCCM, VARIANTS SPATCCM LYS-256 AND TRP-457, AND RP CHARACTERIZATION OF VARIANTS SPATCCM LYS-256 AND TRP-457. RX PubMed=26041762; DOI=10.1136/jmedgenet-2015-103104; RA Damseh N., Simonin A., Jalas C., Picoraro J.A., Shaag A., Cho M.T., RA Yaacov B., Neidich J., Al-Ashhab M., Juusola J., Bale S., Telegrafi A., RA Retterer K., Pappas J.G., Moran E., Cappell J., Anyane Yeboa K., RA Abu-Libdeh B., Hediger M.A., Chung W.K., Elpeleg O., Edvardson S.; RT "Mutations in SLC1A4, encoding the brain serine transporter, are associated RT with developmental delay, microcephaly and hypomyelination."; RL J. Med. Genet. 52:541-547(2015). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Sodium-dependent neutral amino-acid transporter that mediates CC transport of alanine, serine, cysteine, proline, hydroxyproline and CC threonine. {ECO:0000269|PubMed:14502423, ECO:0000269|PubMed:26041762, CC ECO:0000269|PubMed:8101838, ECO:0000269|PubMed:8340364}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out); CC Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926; CC Evidence={ECO:0000269|PubMed:8340364}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out); CC Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; CC Evidence={ECO:0000269|PubMed:8101838, ECO:0000269|PubMed:8340364}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out); CC Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235; CC Evidence={ECO:0000269|PubMed:8101838}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out); CC Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; CC Evidence={ECO:0000269|PubMed:14502423, ECO:0000269|PubMed:8101838, CC ECO:0000269|PubMed:8340364}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out); CC Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; CC Evidence={ECO:0000269|PubMed:14502423}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxy-L-proline(in) + Na(+)(in) = 4-hydroxy-L-proline(out) CC + Na(+)(out); Xref=Rhea:RHEA:70023, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:58419; Evidence={ECO:0000269|PubMed:14502423}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17081065}; Multi- CC pass membrane protein {ECO:0000255}. Melanosome CC {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in CC melanosome fractions from stage I to stage IV. CC {ECO:0000269|PubMed:17081065}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P43007-1; Sequence=Displayed; CC Name=2; CC IsoId=P43007-2; Sequence=VSP_042880, VSP_042881; CC -!- TISSUE SPECIFICITY: Expressed mostly in brain, muscle, and pancreas but CC detected in all tissues examined. {ECO:0000269|PubMed:8340364}. CC -!- DISEASE: Spastic tetraplegia, thin corpus callosum, and progressive CC microcephaly (SPATCCM) [MIM:616657]: A neurodevelopmental disorder CC characterized by thin corpus callosum, severe progressive microcephaly, CC severe intellectual disability, seizures, spasticity, and global CC developmental delay. Most patients are unable to achieve independent CC walking or speech. {ECO:0000269|PubMed:25930971, CC ECO:0000269|PubMed:26041762, ECO:0000269|PubMed:26138499}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter CC (DAACS) (TC 2.A.23) family. SLC1A4 subfamily. {ECO:0000305}. 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; L14595; AAA02761.1; -; mRNA. DR EMBL; L19444; AAA19438.1; -; mRNA. DR EMBL; U05235; AAC51349.1; -; Genomic_DNA. DR EMBL; U05229; AAC51349.1; JOINED; Genomic_DNA. DR EMBL; U05230; AAC51349.1; JOINED; Genomic_DNA. DR EMBL; U05231; AAC51349.1; JOINED; Genomic_DNA. DR EMBL; U05232; AAC51349.1; JOINED; Genomic_DNA. DR EMBL; U05233; AAC51349.1; JOINED; Genomic_DNA. DR EMBL; U05234; AAC51349.1; JOINED; Genomic_DNA. DR EMBL; AK295687; BAH12156.1; -; mRNA. DR EMBL; AC007386; AAF03519.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99932.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99933.1; -; Genomic_DNA. DR EMBL; BC026216; AAH26216.1; -; mRNA. DR EMBL; BC072423; AAH72423.1; -; mRNA. DR CCDS; CCDS1879.1; -. [P43007-1] DR CCDS; CCDS54362.1; -. [P43007-2] DR PIR; I37188; I37188. DR PIR; I55389; I55389. DR RefSeq; NP_001180422.1; NM_001193493.1. [P43007-2] DR RefSeq; NP_003029.2; NM_003038.4. [P43007-1] DR PDB; 7P4I; EM; 4.20 A; A/B/C=1-532. DR PDBsum; 7P4I; -. DR AlphaFoldDB; P43007; -. DR EMDB; EMD-13193; -. DR SMR; P43007; -. DR BioGRID; 112400; 26. DR IntAct; P43007; 9. DR MINT; P43007; -. DR STRING; 9606.ENSP00000234256; -. DR ChEMBL; CHEMBL2315; -. DR DrugBank; DB00160; Alanine. DR TCDB; 2.A.23.3.1; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family. DR GlyCosmos; P43007; 2 sites, No reported glycans. DR GlyGen; P43007; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; P43007; -. DR PhosphoSitePlus; P43007; -. DR SwissPalm; P43007; -. DR BioMuta; SLC1A4; -. DR DMDM; 1173365; -. DR EPD; P43007; -. DR jPOST; P43007; -. DR MassIVE; P43007; -. DR MaxQB; P43007; -. DR PaxDb; 9606-ENSP00000234256; -. DR PeptideAtlas; P43007; -. DR ProteomicsDB; 55572; -. [P43007-1] DR ProteomicsDB; 55573; -. [P43007-2] DR Pumba; P43007; -. DR Antibodypedia; 30840; 287 antibodies from 33 providers. DR DNASU; 6509; -. DR Ensembl; ENST00000234256.4; ENSP00000234256.3; ENSG00000115902.11. [P43007-1] DR Ensembl; ENST00000531327.5; ENSP00000431942.1; ENSG00000115902.11. [P43007-2] DR GeneID; 6509; -. DR KEGG; hsa:6509; -. DR MANE-Select; ENST00000234256.4; ENSP00000234256.3; NM_003038.5; NP_003029.2. DR UCSC; uc010ypz.3; human. [P43007-1] DR AGR; HGNC:10942; -. DR DisGeNET; 6509; -. DR GeneCards; SLC1A4; -. DR HGNC; HGNC:10942; SLC1A4. DR HPA; ENSG00000115902; Tissue enhanced (brain). DR MalaCards; SLC1A4; -. DR MIM; 600229; gene. DR MIM; 616657; phenotype. DR neXtProt; NX_P43007; -. DR OpenTargets; ENSG00000115902; -. DR Orphanet; 447997; Spastic tetraplegia-thin corpus callosum-progressive postnatal microcephaly syndrome. DR PharmGKB; PA35829; -. DR VEuPathDB; HostDB:ENSG00000115902; -. DR eggNOG; KOG3787; Eukaryota. DR GeneTree; ENSGT00940000157081; -. DR HOGENOM; CLU_019375_6_2_1; -. DR InParanoid; P43007; -. DR OMA; GIMFVVH; -. DR OrthoDB; 49426at2759; -. DR PhylomeDB; P43007; -. DR TreeFam; TF315206; -. DR PathwayCommons; P43007; -. DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane. DR SignaLink; P43007; -. DR BioGRID-ORCS; 6509; 10 hits in 1161 CRISPR screens. DR ChiTaRS; SLC1A4; human. DR GeneWiki; SLC1A4; -. DR GenomeRNAi; 6509; -. DR Pharos; P43007; Tbio. DR PRO; PR:P43007; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P43007; Protein. DR Bgee; ENSG00000115902; Expressed in buccal mucosa cell and 206 other cell types or tissues. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IMP:ARUK-UCL. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome. DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB. DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; TAS:BHF-UCL. DR GO; GO:0034590; F:L-hydroxyproline transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015195; F:L-threonine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0006865; P:amino acid transport; TAS:Reactome. DR GO; GO:0050890; P:cognition; IMP:UniProtKB. DR GO; GO:0006868; P:glutamine transport; TAS:BHF-UCL. DR GO; GO:0034589; P:hydroxyproline transport; IDA:UniProtKB. DR GO; GO:1904273; P:L-alanine import across plasma membrane; IMP:ARUK-UCL. DR GO; GO:0015808; P:L-alanine transport; IDA:UniProtKB. DR GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:ARUK-UCL. DR GO; GO:0015811; P:L-cystine transport; IDA:UniProtKB. DR GO; GO:0015813; P:L-glutamate transmembrane transport; IBA:GO_Central. DR GO; GO:1903812; P:L-serine import across plasma membrane; IMP:ARUK-UCL. DR GO; GO:0015825; P:L-serine transport; IDA:UniProtKB. DR GO; GO:0015824; P:proline transport; IDA:UniProtKB. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; NAS:UniProtKB. DR GO; GO:0015826; P:threonine transport; IDA:UniProtKB. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS. DR InterPro; IPR036458; Na:dicarbo_symporter_sf. DR PANTHER; PTHR11958:SF20; NEUTRAL AMINO ACID TRANSPORTER A; 1. DR PANTHER; PTHR11958; SODIUM/DICARBOXYLATE SYMPORTER-RELATED; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; Proton glutamate symport protein; 1. DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1. DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1. DR Genevisible; P43007; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Disease variant; Epilepsy; KW Glycoprotein; Intellectual disability; Membrane; Phosphoprotein; KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..532 FT /note="Neutral amino acid transporter A" FT /id="PRO_0000202079" FT TOPO_DOM 1..41 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 42..62 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 88..108 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 119..139 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 140..216 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 217..237 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 257..277 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 298..318 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 328..348 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 373..393 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 418..438 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 500..532 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 507 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 527 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35874" FT MOD_RES 530 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35874" FT CARBOHYD 201 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 206 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT VAR_SEQ 1..220 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042880" FT VAR_SEQ 267..345 FT /note="WYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFASILGHVIHGGIVLPLIYF FT VFTRKNPFRFLLGLLAPFATAFATCSS -> C (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042881" FT VARIANT 37 FT /note="G -> R (in dbSNP:rs1064512)" FT /id="VAR_011878" FT VARIANT 256 FT /note="E -> K (in SPATCCM; does not affect localization at FT the cell surface; decreased uptake of L-serine and FT L-alanine; Vmax is decreased by at least 50% for both FT substrates; 3-fold increase of affinity for L-serine; FT 2-fold increase of affinity for L-alanine; FT dbSNP:rs201278558)" FT /evidence="ECO:0000269|PubMed:25930971, FT ECO:0000269|PubMed:26041762, ECO:0000269|PubMed:26138499" FT /id="VAR_075085" FT VARIANT 399 FT /note="V -> I (in dbSNP:rs759458)" FT /id="VAR_011879" FT VARIANT 457 FT /note="R -> W (in SPATCCM; does not affect localization at FT the cell surface; loss of uptake of L-serine and L-alanine; FT dbSNP:rs761533681)" FT /evidence="ECO:0000269|PubMed:26041762" FT /id="VAR_075086" FT CONFLICT 117 FT /note="A -> R (in Ref. 1; AAA02761)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="S -> T (in Ref. 2; AAA19438)" FT /evidence="ECO:0000305" SQ 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 //