SATT_HUMAN
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 03-AUG-2022, entry version 189.
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},
GN SATT {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}.
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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 SMR; P43007; -.
DR BioGRID; 112400; 23.
DR IntAct; P43007; 8.
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 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; P43007; -.
DR PeptideAtlas; P43007; -.
DR PRIDE; P43007; -.
DR ProteomicsDB; 55572; -. [P43007-1]
DR ProteomicsDB; 55573; -. [P43007-2]
DR Antibodypedia; 30840; 256 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 CTD; 6509; -.
DR DisGeNET; 6509; -.
DR GeneCards; SLC1A4; -.
DR HGNC; HGNC:10942; SLC1A4.
DR HPA; ENSG00000115902; Low tissue specificity.
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; ICSFVVP; -.
DR OrthoDB; 1184392at2759; -.
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 1079 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 204 other tissues.
DR Genevisible; P43007; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IC: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:0043025; C:neuronal cell body; IEA:Ensembl.
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:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
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 L-
FT alanine; Vmax is decreased by at least 50% for both
FT substrates; 3-fold increase of affinity for L-serine; 2-
FT 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
