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Neutral amino acid transporter B(0) (ATB(0)) (Baboon M7 virus receptor) (RD114/simian type D retrovirus receptor) (Sodium-dependent neutral amino acid transporter type 2) (Solute carrier family 1 member 5)

 AAAT_HUMAN              Reviewed;         541 AA.
Q15758; A8K9H5; B4DR77; B4DWS4; B7ZB81; D0EYG6; E9PC01; O95720;
Q96RL9; Q9BWQ3; Q9UNP2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
22-NOV-2017, entry version 174.
RecName: Full=Neutral amino acid transporter B(0);
Short=ATB(0);
AltName: Full=Baboon M7 virus receptor;
AltName: Full=RD114/simian type D retrovirus receptor;
AltName: Full=Sodium-dependent neutral amino acid transporter type 2;
AltName: Full=Solute carrier family 1 member 5;
Name=SLC1A5; Synonyms=ASCT2, M7V1, RDR, RDRC;
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), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Choriocarcinoma;
PubMed=8702519; DOI=10.1074/jbc.271.31.18657;
Kekuda R., Prasad P.D., Fei Y.-J., Torres-Zamorano V., Sinha S.,
Yang-Feng T.L., Leibach F.H., Ganapathy V.;
"Cloning of the sodium-dependent, broad-scope, neutral amino acid
transporter Bo from a human placental choriocarcinoma cell line.";
J. Biol. Chem. 271:18657-18661(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRAL
RECEPTOR (MICROBIAL INFECTION).
PubMed=10051606; DOI=10.1073/pnas.96.5.2129;
Rasko J.E.J., Battini J.L., Gottschalk R.J., Mazo I., Miller A.D.;
"The RD114/simian type D retrovirus receptor is a neutral amino acid
transporter.";
Proc. Natl. Acad. Sci. U.S.A. 96:2129-2134(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRAL
RECEPTOR (MICROBIAL INFECTION).
PubMed=10196349;
Tailor C.S., Nouri A., Zhao Y., Takeuchi Y., Kabat D.;
"A sodium-dependent neutral-amino-acid transporter mediates infections
of feline and baboon endogenous retroviruses and simian type D
retroviruses.";
J. Virol. 73:4470-4474(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ouyang D.-Y., Xu L.-H., He X.-H., Zha Q.-B., Guo H., Gao Q.,
Zhang Y.-T.;
"Cloning of ASCT2 cDNA from MCF-7 cells and its expression in B16
cells.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANT LEU-512.
TISSUE=Esophagus, and Thymus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-541 (ISOFORM 1), AND ALTERNATIVE
INITIATION.
PubMed=11350958; DOI=10.1074/jbc.M100737200;
Tailor C.S., Marin M., Nouri A., Kavanaugh M.P., Kabat D.;
"Truncated forms of the dual function human ASCT2 neutral amino acid
transporter/retroviral receptor are translationally initiated at
multiple alternative CUG and GUG codons.";
J. Biol. Chem. 276:27221-27230(2001).
[10]
FUNCTION.
PubMed=10708449; DOI=10.1128/JVI.74.7.3321-3329.2000;
Blond J.-L., Lavillette D., Cheynet V., Bouton O., Oriol G.,
Chapel-Fernandes S., Mandrand B., Mallet F., Cosset F.-L.;
"An envelope glycoprotein of the human endogenous retrovirus HERV-W is
expressed in the human placenta and fuses cells expressing the type D
mammalian retrovirus receptor.";
J. Virol. 74:3321-3329(2000).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, 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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-535, VARIANT
[LARGE SCALE ANALYSIS] LEU-512, AND 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND 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).
[18]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; THR-494; SER-535
AND SER-539, AND 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).
[22]
FUNCTION, INTERACTION WITH ERVH48-1, AND SUBCELLULAR LOCATION.
PubMed=23492904; DOI=10.1038/srep01462;
Sugimoto J., Sugimoto M., Bernstein H., Jinno Y., Schust D.;
"A novel human endogenous retroviral protein inhibits cell-cell
fusion.";
Sci. Rep. 3:1462-1462(2013).
[23]
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).
[24]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 158-230, AND SUBUNIT.
PubMed=28424515; DOI=10.1038/nature22064;
Canul-Tec J.C., Assal R., Cirri E., Legrand P., Brier S.,
Chamot-Rooke J., Reyes N.;
"Structure and allosteric inhibition of excitatory amino acid
transporter 1.";
Nature 544:446-451(2017).
-!- FUNCTION: Sodium-dependent amino acids transporter that has a
broad substrate specificity, with a preference for zwitterionic
amino acids. It accepts as substrates all neutral amino acids,
including glutamine, asparagine, and branched-chain and aromatic
amino acids, and excludes methylated, anionic, and cationic amino
acids (PubMed:8702519). Through binding of the fusogenic protein
syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the
spontaneous fusion of their plasma membranes, an essential process
in placental development (PubMed:10708449, PubMed:23492904).
{ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:23492904,
ECO:0000269|PubMed:8702519}.
-!- FUNCTION: (Microbial infection) Acts as a cell surface receptor
for feline endogenous virus RD114, baboon M7 endogenous virus and
type D simian retroviruses. {ECO:0000269|PubMed:10051606,
ECO:0000269|PubMed:10196349}.
-!- SUBUNIT: Homotrimer (Probable). Interacts with ERVH48-
1/suppressyn; may negatively regulate syncytialization
(PubMed:23492904). {ECO:0000269|PubMed:23492904,
ECO:0000305|PubMed:28424515}.
-!- INTERACTION:
Q99942:RNF5; NbExp=4; IntAct=EBI-356576, EBI-348482;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8702519};
Multi-pass membrane protein {ECO:0000305}. Melanosome.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Comment=A number of isoforms are produced by alternative
initiation. Isoforms start at multiple alternative CUG and GUG
codons. {ECO:0000269|PubMed:11350958};
Name=1;
IsoId=Q15758-1; Sequence=Displayed;
Name=2;
IsoId=Q15758-2; Sequence=VSP_046354;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q15758-3; Sequence=VSP_046851;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Placenta, lung, skeletal muscle, kidney,
pancreas, and intestine.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. SLC1A5 subfamily.
{ECO:0000305}.
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EMBL; U53347; AAC50629.1; -; mRNA.
EMBL; AF102826; AAD09812.1; -; mRNA.
EMBL; AF105423; AAD27806.1; -; mRNA.
EMBL; GQ919058; ACX53626.1; -; mRNA.
EMBL; AK292690; BAF85379.1; -; mRNA.
EMBL; AK299137; BAG61189.1; -; mRNA.
EMBL; AK301661; BAG63136.1; -; mRNA.
EMBL; AK316546; BAH14917.1; -; mRNA.
EMBL; AC008622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW57446.1; -; Genomic_DNA.
EMBL; BC000062; AAH00062.1; -; mRNA.
EMBL; AF334818; AAK77026.1; -; mRNA.
CCDS; CCDS12692.1; -. [Q15758-1]
CCDS; CCDS46125.1; -. [Q15758-2]
CCDS; CCDS46126.1; -. [Q15758-3]
RefSeq; NP_001138616.1; NM_001145144.1. [Q15758-3]
RefSeq; NP_001138617.1; NM_001145145.1. [Q15758-2]
RefSeq; NP_005619.1; NM_005628.2. [Q15758-1]
UniGene; Hs.631582; -.
PDB; 5LLM; X-ray; 3.25 A; A=158-230.
PDB; 5LLU; X-ray; 3.32 A; A=158-230.
PDB; 5LM4; X-ray; 3.10 A; A=158-230.
PDB; 5MJU; X-ray; 3.71 A; A=158-230.
PDBsum; 5LLM; -.
PDBsum; 5LLU; -.
PDBsum; 5LM4; -.
PDBsum; 5MJU; -.
ProteinModelPortal; Q15758; -.
SMR; Q15758; -.
BioGrid; 112401; 64.
IntAct; Q15758; 42.
MINT; MINT-5001314; -.
STRING; 9606.ENSP00000444408; -.
BindingDB; Q15758; -.
ChEMBL; CHEMBL3562162; -.
DrugBank; DB00174; L-Asparagine.
DrugBank; DB00130; L-Glutamine.
GuidetoPHARMACOLOGY; 874; -.
TCDB; 2.A.23.3.3; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
iPTMnet; Q15758; -.
PhosphoSitePlus; Q15758; -.
SwissPalm; Q15758; -.
BioMuta; SLC1A5; -.
DMDM; 21542389; -.
EPD; Q15758; -.
MaxQB; Q15758; -.
PaxDb; Q15758; -.
PeptideAtlas; Q15758; -.
PRIDE; Q15758; -.
DNASU; 6510; -.
Ensembl; ENST00000412532; ENSP00000397924; ENSG00000105281. [Q15758-3]
Ensembl; ENST00000434726; ENSP00000406532; ENSG00000105281. [Q15758-2]
Ensembl; ENST00000542575; ENSP00000444408; ENSG00000105281. [Q15758-1]
GeneID; 6510; -.
KEGG; hsa:6510; -.
UCSC; uc002pfr.4; human. [Q15758-1]
CTD; 6510; -.
DisGeNET; 6510; -.
EuPathDB; HostDB:ENSG00000105281.12; -.
GeneCards; SLC1A5; -.
H-InvDB; HIX0015262; -.
HGNC; HGNC:10943; SLC1A5.
HPA; HPA035239; -.
HPA; HPA035240; -.
MIM; 109190; gene.
neXtProt; NX_Q15758; -.
OpenTargets; ENSG00000105281; -.
PharmGKB; PA35830; -.
eggNOG; KOG3787; Eukaryota.
eggNOG; COG1301; LUCA.
GeneTree; ENSGT00760000119117; -.
HOGENOM; HOG000208776; -.
HOVERGEN; HBG000080; -.
InParanoid; Q15758; -.
KO; K05616; -.
OMA; LVRNIFP; -.
OrthoDB; EOG091G0UCE; -.
PhylomeDB; Q15758; -.
TreeFam; TF315206; -.
Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
ChiTaRS; SLC1A5; human.
GeneWiki; SLC1A5; -.
GenomeRNAi; 6510; -.
PRO; PR:Q15758; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105281; -.
CleanEx; HS_SLC1A5; -.
ExpressionAtlas; Q15758; baseline and differential.
Genevisible; Q15758; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0015186; F:L-glutamine transmembrane transporter activity; TAS:BHF-UCL.
GO; GO:0015194; F:L-serine transmembrane transporter activity; IEA:Ensembl.
GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; TAS:ProtInc.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0006865; P:amino acid transport; TAS:Reactome.
GO; GO:0010585; P:glutamine secretion; IEA:Ensembl.
GO; GO:0006868; P:glutamine transport; TAS:BHF-UCL.
GO; GO:1903803; P:L-glutamine import across plasma membrane; IEA:Ensembl.
GO; GO:0015804; P:neutral amino acid transport; TAS:ProtInc.
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; 1.
PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Amino-acid transport; Cell membrane;
Complete proteome; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 541 Neutral amino acid transporter B(0).
/FTId=PRO_0000202082.
TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.
TRANSMEM 53 73 Helical. {ECO:0000255}.
TRANSMEM 99 119 Helical. {ECO:0000255}.
TRANSMEM 133 153 Helical. {ECO:0000255}.
TOPO_DOM 154 224 Extracellular. {ECO:0000255}.
TRANSMEM 225 245 Helical. {ECO:0000255}.
TRANSMEM 266 286 Helical. {ECO:0000255}.
TRANSMEM 306 326 Helical. {ECO:0000255}.
TRANSMEM 336 356 Helical. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TRANSMEM 399 419 Helical. {ECO:0000255}.
TRANSMEM 426 446 Helical. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 494 494 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
VAR_SEQ 1 228 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046851.
VAR_SEQ 1 203 MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGS
RDQVRRCLRANLLVLLTVVAVVAGVALGLGVSGAGGALALG
PERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLDPGA
LGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINA
SVGAAGSAENAPSKEVLDSFLDLARNIFPSNLVSAAFRS
-> M (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046354.
VARIANT 17 17 P -> A (in dbSNP:rs3027956).
/FTId=VAR_020439.
VARIANT 512 512 V -> L (in dbSNP:rs3027961).
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_013517.
CONFLICT 18 24 TANGGLA -> PPTGAWQ (in Ref. 1; AAC50629).
{ECO:0000305}.
CONFLICT 44 44 Q -> L (in Ref. 1; AAC50629).
{ECO:0000305}.
CONFLICT 84 87 ERLS -> GALE (in Ref. 1; AAC50629).
{ECO:0000305}.
CONFLICT 341 341 V -> A (in Ref. 5; BAH14917).
{ECO:0000305}.
CONFLICT 453 453 I -> V (in Ref. 2; AAD09812).
{ECO:0000305}.
CONFLICT 460 460 D -> G (in Ref. 2; AAD09812).
{ECO:0000305}.
CONFLICT 463 463 V -> A (in Ref. 2; AAD09812).
{ECO:0000305}.
CONFLICT 508 508 D -> G (in Ref. 2; AAD09812).
{ECO:0000305}.
HELIX 54 62 {ECO:0000244|PDB:5LM4}.
HELIX 66 69 {ECO:0000244|PDB:5LM4}.
HELIX 104 107 {ECO:0000244|PDB:5LM4}.
HELIX 180 191 {ECO:0000244|PDB:5LM4}.
HELIX 196 199 {ECO:0000244|PDB:5LM4}.
STRAND 202 204 {ECO:0000244|PDB:5LM4}.
STRAND 225 228 {ECO:0000244|PDB:5LM4}.
HELIX 231 237 {ECO:0000244|PDB:5LM4}.
HELIX 239 245 {ECO:0000244|PDB:5LM4}.
HELIX 254 261 {ECO:0000244|PDB:5LM4}.
HELIX 266 270 {ECO:0000244|PDB:5LM4}.
HELIX 324 329 {ECO:0000244|PDB:5LM4}.
HELIX 476 480 {ECO:0000244|PDB:5LM4}.
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


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