AAAT_HUMAN
ID AAAT_HUMAN Reviewed; 541 AA.
AC Q15758; A8K9H5; B4DR77; B4DWS4; B7ZB81; D0EYG6; E9PC01; O95720; Q96RL9;
AC Q9BWQ3; Q9UNP2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Neutral amino acid transporter B(0);
DE Short=ATB(0);
DE AltName: Full=Baboon M7 virus receptor;
DE AltName: Full=RD114/simian type D retrovirus receptor;
DE AltName: Full=Sodium-dependent neutral amino acid transporter type 2;
DE AltName: Full=Solute carrier family 1 member 5;
GN Name=SLC1A5; Synonyms=ASCT2, M7V1, RDR, RDRC;
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, AND SUBCELLULAR LOCATION.
RC TISSUE=Choriocarcinoma;
RX PubMed=8702519; DOI=10.1074/jbc.271.31.18657;
RA Kekuda R., Prasad P.D., Fei Y.-J., Torres-Zamorano V., Sinha S.,
RA Yang-Feng T.L., Leibach F.H., Ganapathy V.;
RT "Cloning of the sodium-dependent, broad-scope, neutral amino acid
RT transporter Bo from a human placental choriocarcinoma cell line.";
RL J. Biol. Chem. 271:18657-18661(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRAL RECEPTOR
RP (MICROBIAL INFECTION).
RX PubMed=10051606; DOI=10.1073/pnas.96.5.2129;
RA Rasko J.E.J., Battini J.L., Gottschalk R.J., Mazo I., Miller A.D.;
RT "The RD114/simian type D retrovirus receptor is a neutral amino acid
RT transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2129-2134(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRAL RECEPTOR
RP (MICROBIAL INFECTION).
RX PubMed=10196349; DOI=10.1128/jvi.73.5.4470-4474.1999;
RA Tailor C.S., Nouri A., Zhao Y., Takeuchi Y., Kabat D.;
RT "A sodium-dependent neutral-amino-acid transporter mediates infections of
RT feline and baboon endogenous retroviruses and simian type D retroviruses.";
RL J. Virol. 73:4470-4474(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ouyang D.-Y., Xu L.-H., He X.-H., Zha Q.-B., Guo H., Gao Q., Zhang Y.-T.;
RT "Cloning of ASCT2 cDNA from MCF-7 cells and its expression in B16 cells.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP LEU-512.
RC TISSUE=Esophagus, and Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-541 (ISOFORM 1), AND ALTERNATIVE
RP INITIATION.
RX PubMed=11350958; DOI=10.1074/jbc.m100737200;
RA Tailor C.S., Marin M., Nouri A., Kavanaugh M.P., Kabat D.;
RT "Truncated forms of the dual function human ASCT2 neutral amino acid
RT transporter/retroviral receptor are translationally initiated at multiple
RT alternative CUG and GUG codons.";
RL J. Biol. Chem. 276:27221-27230(2001).
RN [10]
RP FUNCTION.
RX PubMed=10708449; DOI=10.1128/jvi.74.7.3321-3329.2000;
RA Blond J.-L., Lavillette D., Cheynet V., Bouton O., Oriol G.,
RA Chapel-Fernandes S., Mandrand B., Mallet F., Cosset F.-L.;
RT "An envelope glycoprotein of the human endogenous retrovirus HERV-W is
RT expressed in the human placenta and fuses cells expressing the type D
RT mammalian retrovirus receptor.";
RL J. Virol. 74:3321-3329(2000).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-535, VARIANT
RP [LARGE SCALE ANALYSIS] LEU-512, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; THR-494; SER-535 AND
RP SER-539, AND 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 [22]
RP FUNCTION, INTERACTION WITH ERVH48-1, AND SUBCELLULAR LOCATION.
RX PubMed=23492904; DOI=10.1038/srep01462;
RA Sugimoto J., Sugimoto M., Bernstein H., Jinno Y., Schust D.;
RT "A novel human endogenous retroviral protein inhibits cell-cell fusion.";
RL Sci. Rep. 3:1462-1462(2013).
RN [23]
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).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 158-230, AND SUBUNIT.
RX PubMed=28424515; DOI=10.1038/nature22064;
RA Canul-Tec J.C., Assal R., Cirri E., Legrand P., Brier S., Chamot-Rooke J.,
RA Reyes N.;
RT "Structure and allosteric inhibition of excitatory amino acid transporter
RT 1.";
RL Nature 544:446-451(2017).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.85 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND SUBUNIT.
RX PubMed=29872227; DOI=10.1038/s41594-018-0076-y;
RA Garaeva A.A., Oostergetel G.T., Gati C., Guskov A., Paulino C.,
RA Slotboom D.J.;
RT "Cryo-EM structure of the human neutral amino acid transporter ASCT2.";
RL Nat. Struct. Mol. Biol. 25:515-521(2018).
CC -!- FUNCTION: Sodium-dependent amino acids transporter that has a broad
CC substrate specificity, with a preference for zwitterionic amino acids.
CC It accepts as substrates all neutral amino acids, including glutamine,
CC asparagine, and branched-chain and aromatic amino acids, and excludes
CC methylated, anionic, and cationic amino acids (PubMed:8702519,
CC PubMed:29872227). Through binding of the fusogenic protein syncytin-
CC 1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous
CC fusion of their plasma membranes, an essential process in placental
CC development (PubMed:10708449, PubMed:23492904).
CC {ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:23492904,
CC ECO:0000269|PubMed:29872227, ECO:0000269|PubMed:8702519}.
CC -!- FUNCTION: (Microbial infection) Acts as a cell surface receptor for
CC Feline endogenous virus RD114. {ECO:0000269|PubMed:10051606,
CC ECO:0000269|PubMed:10196349}.
CC -!- FUNCTION: (Microbial infection) Acts as a cell surface receptor for
CC Baboon M7 endogenous virus. {ECO:0000269|PubMed:10196349}.
CC -!- FUNCTION: (Microbial infection) Acts as a cell surface receptor for
CC type D simian retroviruses. {ECO:0000269|PubMed:10196349}.
CC -!- SUBUNIT: Homotrimer (Probable) (PubMed:29872227). Interacts with
CC ERVH48-1/suppressyn; may negatively regulate syncytialization
CC (PubMed:23492904). {ECO:0000269|PubMed:23492904,
CC ECO:0000269|PubMed:29872227, ECO:0000305|PubMed:28424515}.
CC -!- INTERACTION:
CC Q15758; O95236-2: APOL3; NbExp=3; IntAct=EBI-356576, EBI-11976321;
CC Q15758; P60201-2: PLP1; NbExp=3; IntAct=EBI-356576, EBI-12188331;
CC Q15758; Q99942: RNF5; NbExp=4; IntAct=EBI-356576, EBI-348482;
CC Q15758; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-356576, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8702519,
CC ECO:0000305|PubMed:29872227}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29872227}. Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Comment=A number of isoforms are produced by alternative initiation.
CC Isoforms start at multiple alternative CUG and GUG codons.
CC {ECO:0000269|PubMed:11350958};
CC Name=1;
CC IsoId=Q15758-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15758-2; Sequence=VSP_046354;
CC Name=3;
CC IsoId=Q15758-3; Sequence=VSP_046851;
CC -!- TISSUE SPECIFICITY: Placenta, lung, skeletal muscle, kidney, pancreas,
CC and intestine.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A5 subfamily. {ECO:0000305}.
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DR EMBL; U53347; AAC50629.1; -; mRNA.
DR EMBL; AF102826; AAD09812.1; -; mRNA.
DR EMBL; AF105423; AAD27806.1; -; mRNA.
DR EMBL; GQ919058; ACX53626.1; -; mRNA.
DR EMBL; AK292690; BAF85379.1; -; mRNA.
DR EMBL; AK299137; BAG61189.1; -; mRNA.
DR EMBL; AK301661; BAG63136.1; -; mRNA.
DR EMBL; AK316546; BAH14917.1; -; mRNA.
DR EMBL; AC008622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57446.1; -; Genomic_DNA.
DR EMBL; BC000062; AAH00062.1; -; mRNA.
DR EMBL; AF334818; AAK77026.1; -; mRNA.
DR CCDS; CCDS12692.1; -. [Q15758-1]
DR CCDS; CCDS46125.1; -. [Q15758-2]
DR CCDS; CCDS46126.1; -. [Q15758-3]
DR RefSeq; NP_001138616.1; NM_001145144.1. [Q15758-3]
DR RefSeq; NP_001138617.1; NM_001145145.1. [Q15758-2]
DR RefSeq; NP_005619.1; NM_005628.2. [Q15758-1]
DR PDB; 5LLM; X-ray; 3.25 A; A=158-230.
DR PDB; 5LLU; X-ray; 3.32 A; A=158-230.
DR PDB; 5LM4; X-ray; 3.10 A; A=158-230.
DR PDB; 5MJU; X-ray; 3.71 A; A=158-230.
DR PDB; 6GCT; EM; 3.85 A; A/B/C=1-541.
DR PDB; 6MP6; EM; 3.54 A; A/B/C=1-541.
DR PDB; 6MPB; EM; 3.84 A; A/B/C=1-541.
DR PDB; 6RVX; EM; 3.61 A; A/B/C=1-541.
DR PDB; 6RVY; EM; 4.13 A; A/B/C=1-541.
DR PDB; 7BCQ; EM; 3.43 A; A/B/C=1-541.
DR PDB; 7BCS; EM; 3.43 A; A/B/C=1-541.
DR PDB; 7BCT; EM; 3.37 A; A/B/C=1-541.
DR PDBsum; 5LLM; -.
DR PDBsum; 5LLU; -.
DR PDBsum; 5LM4; -.
DR PDBsum; 5MJU; -.
DR PDBsum; 6GCT; -.
DR PDBsum; 6MP6; -.
DR PDBsum; 6MPB; -.
DR PDBsum; 6RVX; -.
DR PDBsum; 6RVY; -.
DR PDBsum; 7BCQ; -.
DR PDBsum; 7BCS; -.
DR PDBsum; 7BCT; -.
DR AlphaFoldDB; Q15758; -.
DR SMR; Q15758; -.
DR BioGRID; 112401; 362.
DR IntAct; Q15758; 99.
DR MINT; Q15758; -.
DR STRING; 9606.ENSP00000444408; -.
DR BindingDB; Q15758; -.
DR ChEMBL; CHEMBL3562162; -.
DR DrugBank; DB00174; Asparagine.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB00130; L-Glutamine.
DR GuidetoPHARMACOLOGY; 874; -.
DR TCDB; 2.A.23.3.3; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR GlyConnect; 1562; 3 N-Linked glycans (1 site).
DR GlyGen; Q15758; 3 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q15758; -.
DR MetOSite; Q15758; -.
DR PhosphoSitePlus; Q15758; -.
DR SwissPalm; Q15758; -.
DR BioMuta; SLC1A5; -.
DR DMDM; 21542389; -.
DR EPD; Q15758; -.
DR jPOST; Q15758; -.
DR MassIVE; Q15758; -.
DR MaxQB; Q15758; -.
DR PaxDb; Q15758; -.
DR PeptideAtlas; Q15758; -.
DR PRIDE; Q15758; -.
DR ProteomicsDB; 19331; -.
DR ProteomicsDB; 5376; -.
DR ProteomicsDB; 60744; -. [Q15758-1]
DR ABCD; Q15758; 10 sequenced antibodies.
DR Antibodypedia; 18149; 270 antibodies from 33 providers.
DR DNASU; 6510; -.
DR Ensembl; ENST00000412532.6; ENSP00000397924.1; ENSG00000105281.12. [Q15758-3]
DR Ensembl; ENST00000434726.6; ENSP00000406532.1; ENSG00000105281.12. [Q15758-2]
DR Ensembl; ENST00000542575.6; ENSP00000444408.1; ENSG00000105281.12. [Q15758-1]
DR GeneID; 6510; -.
DR KEGG; hsa:6510; -.
DR MANE-Select; ENST00000542575.6; ENSP00000444408.1; NM_005628.3; NP_005619.1.
DR UCSC; uc002pfr.4; human. [Q15758-1]
DR CTD; 6510; -.
DR DisGeNET; 6510; -.
DR GeneCards; SLC1A5; -.
DR HGNC; HGNC:10943; SLC1A5.
DR HPA; ENSG00000105281; Low tissue specificity.
DR MIM; 109190; gene.
DR neXtProt; NX_Q15758; -.
DR OpenTargets; ENSG00000105281; -.
DR PharmGKB; PA35830; -.
DR VEuPathDB; HostDB:ENSG00000105281; -.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000159485; -.
DR HOGENOM; CLU_019375_3_3_1; -.
DR InParanoid; Q15758; -.
DR OMA; QATNTPM; -.
DR PhylomeDB; Q15758; -.
DR TreeFam; TF315206; -.
DR PathwayCommons; Q15758; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q15758; -.
DR SIGNOR; Q15758; -.
DR BioGRID-ORCS; 6510; 122 hits in 1100 CRISPR screens.
DR ChiTaRS; SLC1A5; human.
DR GeneWiki; SLC1A5; -.
DR GenomeRNAi; 6510; -.
DR Pharos; Q15758; Tchem.
DR PRO; PR:Q15758; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q15758; protein.
DR Bgee; ENSG00000105281; Expressed in stromal cell of endometrium and 198 other tissues.
DR ExpressionAtlas; Q15758; baseline and differential.
DR Genevisible; Q15758; HS.
DR GO; GO:0009925; C:basal plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0010585; P:glutamine secretion; IEA:Ensembl.
DR GO; GO:0006868; P:glutamine transport; IDA:UniProtKB.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:1903803; P:L-glutamine import across plasma membrane; IEA:Ensembl.
DR GO; GO:0015804; P:neutral amino acid transport; TAS:ProtInc.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISS: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 initiation; Alternative splicing;
KW Amino-acid transport; Cell membrane; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Sodium;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="Neutral amino acid transporter B(0)"
FT /id="PRO_0000202082"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 82..94
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 117..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 154..224
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..248
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 249..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..285
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 286..306
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..328
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 329..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 334..364
FT /note="Discontinuously helical"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 365..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..400
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 401..413
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 414..447
FT /note="Discontinuously helical"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 448..460
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..482
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305|PubMed:29872227"
FT TOPO_DOM 483..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 511..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 382
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 384
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 386
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 471
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 475
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 1..228
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046851"
FT VAR_SEQ 1..203
FT /note="MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRAN
FT LLVLLTVVAVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCS
FT LIGGAASLDPGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAG
FT SAENAPSKEVLDSFLDLARNIFPSNLVSAAFRS -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046354"
FT VARIANT 17
FT /note="P -> A (in dbSNP:rs3027956)"
FT /id="VAR_020439"
FT VARIANT 512
FT /note="V -> L (in dbSNP:rs3027961)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0007744|PubMed:19690332"
FT /id="VAR_013517"
FT CONFLICT 18..24
FT /note="TANGGLA -> PPTGAWQ (in Ref. 1; AAC50629)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="Q -> L (in Ref. 1; AAC50629)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..87
FT /note="ERLS -> GALE (in Ref. 1; AAC50629)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="V -> A (in Ref. 5; BAH14917)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="I -> V (in Ref. 2; AAD09812)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="D -> G (in Ref. 2; AAD09812)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="V -> A (in Ref. 2; AAD09812)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="D -> G (in Ref. 2; AAD09812)"
FT /evidence="ECO:0000305"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5LM4"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 78..102
FT /evidence="ECO:0007829|PDB:7BCQ"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 121..153
FT /evidence="ECO:0007829|PDB:7BCT"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:7BCT"
FT TURN 169..173
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5LM4"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5LM4"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 297..318
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:5LM4"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:7BCT"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 388..403
FT /evidence="ECO:0007829|PDB:7BCT"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:7BCT"
FT HELIX 476..480
FT /evidence="ECO:0007829|PDB:5LM4"
SQ SEQUENCE 541 AA; 56598 MW; AD61C789CCFFE934 CRC64;
MVADPPRDSK GLAAAEPTAN GGLALASIED QGAAAGGYCG SRDQVRRCLR ANLLVLLTVV
AVVAGVALGL GVSGAGGALA LGPERLSAFV FPGELLLRLL RMIILPLVVC SLIGGAASLD
PGALGRLGAW ALLFFLVTTL LASALGVGLA LALQPGAASA AINASVGAAG SAENAPSKEV
LDSFLDLARN IFPSNLVSAA FRSYSTTYEE RNITGTRVKV PVGQEVEGMN ILGLVVFAIV
FGVALRKLGP EGELLIRFFN SFNEATMVLV SWIMWYAPVG IMFLVAGKIV EMEDVGLLFA
RLGKYILCCL LGHAIHGLLV LPLIYFLFTR KNPYRFLWGI VTPLATAFGT SSSSATLPLM
MKCVEENNGV AKHISRFILP IGATVNMDGA ALFQCVAAVF IAQLSQQSLD FVKIITILVT
ATASSVGAAG IPAGGVLTLA IILEAVNLPV DHISLILAVD WLVDRSCTVL NVEGDALGAG
LLQNYVDRTE SRSTEPELIQ VKSELPLDPL PVPTEEGNPL LKHYRGPAGD ATVASEKESV
M
