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Y L amino acid transporter 1 (Monocyte amino acid permease 2) (MOP-2) (Solute carrier family 7 member 7) (y( )L-type amino acid transporter 1) (Y LAT1) (y LAT-1)

 YLAT1_HUMAN             Reviewed;         511 AA.
Q9UM01; B2RAU0; D3DS26; O95984; Q53XC1; Q86U07; Q9P2V5;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
28-MAR-2018, entry version 164.
RecName: Full=Y+L amino acid transporter 1;
AltName: Full=Monocyte amino acid permease 2;
Short=MOP-2;
AltName: Full=Solute carrier family 7 member 7;
AltName: Full=y(+)L-type amino acid transporter 1;
Short=Y+LAT1;
Short=y+LAT-1;
Name=SLC7A7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
VARIANT LPI ARG-334.
PubMed=9829974; DOI=10.1074/jbc.273.49.32437;
Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J.,
Shi Y.-B., Zorzano A., Palacin M.;
"Identification and characterization of a membrane protein (y+L amino
acid transporter-1) that associates with 4F2hc to encode the amino
acid transport activity y+L. A candidate gene for lysinuric protein
intolerance.";
J. Biol. Chem. 273:32437-32445(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBUNIT.
TISSUE=Testis;
PubMed=9878049; DOI=10.1093/emboj/18.1.49;
Pfeiffer R., Rossier G., Spindler B., Meier C., Kuehn L.C., Verrey F.;
"Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and
members of the glycoprotein-associated amino acid transporter
family.";
EMBO J. 18:49-57(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=10080183; DOI=10.1038/6815;
Borsani G., Bassi M.T., Sperandeo M.P., De Grandi A., Buoninconti A.,
Riboni M., Manzoni M., Incerti B., Pepe A., Andria G., Ballabio A.,
Sebastio G.;
"SLC7A7, encoding a putative permease-related protein, is mutated in
patients with lysinuric protein intolerance.";
Nat. Genet. 21:297-301(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10737982;
DOI=10.1002/(SICI)1098-1004(200004)15:4<367::AID-HUMU9>3.0.CO;2-C;
Noguchi A., Shoji Y., Koizumi A., Takahashi T., Shoji Y.,
Matsumori M., Kayo T., Ohata T., Wada Y., Yoshimura I., Maisawa S.,
Konishi M., Takasago Y., Takada G.;
"SLC7A7 genomic structure and novel variants in three Japanese
lysinuric protein intolerance families.";
Hum. Mutat. 15:367-372(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Takayama K., Yoshimoto M.;
"Molecular and biological characterization of a novel monocyte amino
acid permease, MOP-2.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-91.
TISSUE=Kidney;
Fukasawa Y., Segawa H., Endou H., Kanai Y.;
"Characterization of a human system y+L amino acid transporter.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell, and Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[11]
TISSUE SPECIFICITY.
PubMed=11078698;
Dall'Asta V., Bussolati O., Sala R., Rotoli B.M., Sebastio G.,
Sperandeo M.P., Andria G., Gazzola G.C.;
"Arginine transport through system y(+)L in cultured human
fibroblasts: normal phenotype of cells from LPI subjects.";
Am. J. Physiol. 279:C1829-C1837(2000).
[12]
TISSUE SPECIFICITY.
PubMed=11742806;
Sala R., Rotoli B.M., Colla E., Visigalli R., Parolari A.,
Bussolati O., Gazzola G.C., Dall'Asta V.;
"Two-way arginine transport in human endothelial cells: TNF-alpha
stimulation is restricted to system y(+).";
Am. J. Physiol. 282:C134-C143(2002).
[13]
FUNCTION.
PubMed=14603368; DOI=10.1113/eph8802647;
Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.;
"Nitric oxide synthesis requires activity of the cationic and neutral
amino acid transport system y+L in human umbilical vein endothelium.";
Exp. Physiol. 88:699-710(2003).
[14]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15280038; DOI=10.1016/j.febslet.2004.06.086;
Rotoli B.M., Bussolati O., Sala R., Barilli A., Talarico E.,
Gazzola G.C., Dall'Asta V.;
"INFgamma stimulates arginine transport through system y+L in human
monocytes.";
FEBS Lett. 571:177-181(2004).
[15]
FUNCTION, TISSUE SPECIFICITY, AND INHIBITION.
PubMed=17329401; DOI=10.1152/ajpcell.00323.2006;
Rotmann A., Simon A., Martine U., Habermeier A., Closs E.I.;
"Activation of classical protein kinase C decreases transport via
systems y+ and y+L.";
Am. J. Physiol. 292:C2259-C2268(2007).
[16]
TISSUE SPECIFICITY.
PubMed=17197568; DOI=10.1167/iovs.06-0398;
Kaneko S., Ando A., Okuda-Ashitaka E., Maeda M., Furuta K., Suzuki M.,
Matsumura M., Ito S.;
"Ornithine transport via cationic amino acid transporter-1 is involved
in ornithine cytotoxicity in retinal pigment epithelial cells.";
Invest. Ophthalmol. Vis. Sci. 48:464-471(2007).
[17]
VARIANT LPI ARG-334, AND CHARACTERIZATION OF VARIANT LPI ARG-334.
PubMed=10080182; DOI=10.1038/6809;
Torrents D., Mykkaenen J., Pineda M., Feliubadalo L., Estevez R.,
de Cid R., Sanjurjo P., Zorzano A., Nunes V., Huoponen K.,
Reinikainen A., Simell O., Savontaus M.-L., Aula P., Palacin M.;
"Identification of SLC7A7, encoding y+LAT-1, as the lysinuric protein
intolerance gene.";
Nat. Genet. 21:293-296(1999).
[18]
VARIANT LPI ARG-386.
PubMed=10631139; DOI=10.1086/302700;
Sperandeo M.P., Bassi M.T., Riboni M., Parenti G., Buoninconti A.,
Manzoni M., Incerti B., Larocca M.R., Di Rocco M., Strisciuglio P.,
Dianzani I., Parini R., Candito M., Endo F., Ballabio A., Andria G.,
Sebastio G., Borsani G.;
"Structure of the SLC7A7 gene and mutational analysis of patients
affected by lysinuric protein intolerance.";
Am. J. Hum. Genet. 66:92-99(2000).
[19]
VARIANTS LPI VAL-54 AND ASP-338, AND CHARACTERIZATION OF VARIANTS LPI
VAL-54 AND ARG-334.
PubMed=10655553; DOI=10.1093/hmg/9.3.431;
Mykkaenen J., Torrents D., Pineda M., Camps M., Yoldi M.E.,
Horelli-Kuitunen N., Huoponen K., Heinonen M., Oksanen J., Simell O.,
Savontaus M.-L., Zorzano A., Palacin M., Aula P.;
"Functional analysis of novel mutations in y+LAT-1 amino acid
transporter gene causing lysinuric protein intolerance (LPI).";
Hum. Mol. Genet. 9:431-438(2000).
[20]
VARIANTS LPI PHE-238 AND PRO-489.
PubMed=12402335; DOI=10.1002/humu.10140;
Shoji Y., Noguchi A., Shoji Y., Matsumori M., Takasago Y.,
Takayanagi M., Yoshida Y., Ihara K., Hara T., Yamaguchi S.,
Yoshino M., Kaji M., Yamamoto S., Nakai A., Koizumi A., Hokezu Y.,
Nagamatsu K., Mikami H., Kitajima I., Takada G.;
"Five novel SLC7A7 variants and y+L gene-expression pattern in
cultured lymphoblasts from Japanese patients with lysinuric protein
intolerance.";
Hum. Mutat. 20:375-381(2002).
[21]
CHARACTERIZATION OF VARIANTS LPI LEU-36 DEL AND LEU-152, AND
SUBCELLULAR LOCATION.
PubMed=15756301; DOI=10.1038/sj.ejhg.5201376;
Sperandeo M.P., Paladino S., Maiuri L., Maroupulos G.D., Zurzolo C.,
Taglialatela M., Andria G., Sebastio G.;
"A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity:
implications for the molecular pathogenesis of lysinuric protein
intolerance.";
Eur. J. Hum. Genet. 13:628-634(2005).
[22]
VARIANTS LPI LYS-50; ILE-188 AND MET-333, AND CHARACTERIZATION OF
VARIANTS LPI LYS-50; ILE-188 AND ARG-386.
PubMed=15776427; DOI=10.1002/humu.9323;
Sperandeo M.P., Annunziata P., Ammendola V., Fiorito V., Pepe A.,
Soldovieri M.V., Taglialatela M., Andria G., Sebastio G.;
"Lysinuric protein intolerance: identification and functional analysis
of mutations of the SLC7A7 gene.";
Hum. Mutat. 25:410-410(2005).
[23]
VARIANT [LARGE SCALE ANALYSIS] SER-413.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[24]
VARIANTS LPI ILE-5; GLU-36 DEL; LYS-50; LEU-53; VAL-54; PRO-124;
PRO-140; LEU-152; ILE-188; GLU-191; PHE-238; ASP-251; PRO-261;
MET-333; ARG-334; ASP-338; TYR-365; ARG-386 AND PRO-489.
PubMed=17764084; DOI=10.1002/humu.20589;
Sperandeo M.P., Andria G., Sebastio G.;
"Lysinuric protein intolerance: update and extended mutation analysis
of the SLC7A7 gene.";
Hum. Mutat. 29:14-21(2008).
-!- FUNCTION: Involved in the sodium-independent uptake of dibasic
amino acids and sodium-dependent uptake of some neutral amino
acids. Requires coexpression with SLC3A2/4F2hc to mediate the
uptake of arginine, leucine and glutamine. Plays a role in nitric
oxide synthesis in human umbilical vein endothelial cells (HUVECs)
via transport of L-arginine. Involved in the transport of L-
arginine in monocytes. {ECO:0000269|PubMed:14603368,
ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:17329401,
ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.
-!- ENZYME REGULATION: Arginine transport is inhibited by protein
kinase C (PKC) and treatment with phorbol-12-myristate-13-acetate
(PMA).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=31.7 uM for L-leucine (in the presence of 0.1 M NaCl)
{ECO:0000269|PubMed:9878049};
KM=16.2 uM for L-leucine (in the presence of 0.1 M LiCl)
{ECO:0000269|PubMed:9878049};
-!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
transport protein SLC3A2/4F2hc. {ECO:0000269|PubMed:9829974,
ECO:0000269|PubMed:9878049}.
-!- SUBCELLULAR LOCATION: Basolateral cell membrane
{ECO:0000269|PubMed:15756301}; Multi-pass membrane protein
{ECO:0000269|PubMed:15756301}.
-!- TISSUE SPECIFICITY: Highest expression in kidney and peripheral
blood leukocytes. Weaker expression is observed in lung, heart,
placenta, spleen, testis and small intestine. Expressed in normal
fibroblasts and those from LPI patients. Also expressed in HUVECs,
monocytes, retinal pigment epithelial cells, and various carcinoma
cell lines, with highest expression in a colon-carcinoma cell
line. {ECO:0000269|PubMed:10080183, ECO:0000269|PubMed:11078698,
ECO:0000269|PubMed:11742806, ECO:0000269|PubMed:15280038,
ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401,
ECO:0000269|PubMed:9829974}.
-!- INDUCTION: Expression is stimulated and enhanced by IFNG/IFN-
gamma. {ECO:0000269|PubMed:15280038}.
-!- DISEASE: Lysinuric protein intolerance (LPI) [MIM:222700]: A
metabolic disorder characterized by increased renal excretion of
cationic amino acid (CAA), reduced CAA absorption from intestine,
and orotic aciduria. On a normal diet, LPI patients present poor
feeding, vomiting, diarrhea, episodes of hyperammoniaemic coma and
growth retardation. Hepatosplenomegaly, osteoporosis and a life-
threatening pulmonary involvement (alveolar proteinosis) are also
seen. Biochemically LPI is characterized by defective transport of
dibasic amino acids at the basolateral membrane of epithelial
cells in kidney and intestine. {ECO:0000269|PubMed:10080182,
ECO:0000269|PubMed:10631139, ECO:0000269|PubMed:10655553,
ECO:0000269|PubMed:12402335, ECO:0000269|PubMed:15756301,
ECO:0000269|PubMed:15776427, ECO:0000269|PubMed:17764084,
ECO:0000269|PubMed:9829974}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA95120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAD62619.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF092032; AAC83706.1; -; mRNA.
EMBL; AJ130718; CAA10198.1; -; mRNA.
EMBL; Y18474; CAB40136.1; -; mRNA.
EMBL; AB031537; BAA95120.1; ALT_SEQ; Genomic_DNA.
EMBL; AB011263; BAB11849.1; -; mRNA.
EMBL; AB020532; BAA87623.1; -; mRNA.
EMBL; BX161519; CAD61952.1; -; mRNA.
EMBL; BX248291; CAD62619.1; ALT_INIT; mRNA.
EMBL; AK314351; BAG36987.1; -; mRNA.
EMBL; CH471078; EAW66245.1; -; Genomic_DNA.
EMBL; CH471078; EAW66246.1; -; Genomic_DNA.
EMBL; CH471078; EAW66247.1; -; Genomic_DNA.
EMBL; CH471078; EAW66248.1; -; Genomic_DNA.
EMBL; BC003062; AAH03062.1; -; mRNA.
EMBL; BC010107; AAH10107.1; -; mRNA.
CCDS; CCDS9574.1; -.
RefSeq; NP_001119577.1; NM_001126105.2.
RefSeq; NP_001119578.1; NM_001126106.2.
RefSeq; XP_006720365.1; XM_006720302.1.
RefSeq; XP_011535600.1; XM_011537298.2.
RefSeq; XP_011535601.1; XM_011537299.1.
UniGene; Hs.513147; -.
UniGene; Hs.732349; -.
ProteinModelPortal; Q9UM01; -.
BioGrid; 114518; 2.
IntAct; Q9UM01; 1.
STRING; 9606.ENSP00000285850; -.
DrugBank; DB08838; Agmatine.
TCDB; 2.A.3.8.22; the amino acid-polyamine-organocation (apc) family.
iPTMnet; Q9UM01; -.
PhosphoSitePlus; Q9UM01; -.
BioMuta; SLC7A7; -.
DMDM; 12643378; -.
MaxQB; Q9UM01; -.
PaxDb; Q9UM01; -.
PeptideAtlas; Q9UM01; -.
PRIDE; Q9UM01; -.
DNASU; 9056; -.
Ensembl; ENST00000285850; ENSP00000285850; ENSG00000155465.
Ensembl; ENST00000397528; ENSP00000380662; ENSG00000155465.
Ensembl; ENST00000397529; ENSP00000380663; ENSG00000155465.
Ensembl; ENST00000397532; ENSP00000380666; ENSG00000155465.
Ensembl; ENST00000555702; ENSP00000451881; ENSG00000155465.
GeneID; 9056; -.
KEGG; hsa:9056; -.
UCSC; uc001wgr.5; human.
CTD; 9056; -.
DisGeNET; 9056; -.
EuPathDB; HostDB:ENSG00000155465.18; -.
GeneCards; SLC7A7; -.
GeneReviews; SLC7A7; -.
HGNC; HGNC:11065; SLC7A7.
HPA; HPA036227; -.
MalaCards; SLC7A7; -.
MIM; 222700; phenotype.
MIM; 603593; gene.
neXtProt; NX_Q9UM01; -.
OpenTargets; ENSG00000155465; -.
Orphanet; 470; Lysinuric protein intolerance.
PharmGKB; PA35925; -.
eggNOG; KOG1287; Eukaryota.
eggNOG; COG0531; LUCA.
GeneTree; ENSGT00760000119037; -.
HOVERGEN; HBG000476; -.
InParanoid; Q9UM01; -.
KO; K13867; -.
OMA; YMVQPIF; -.
OrthoDB; EOG091G07EM; -.
PhylomeDB; Q9UM01; -.
TreeFam; TF313355; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
Reactome; R-HSA-5660862; Defective SLC7A7 causes lysinuric protein intolerance (LPI).
SABIO-RK; Q9UM01; -.
ChiTaRS; SLC7A7; human.
GeneWiki; SLC7A7; -.
GenomeRNAi; 9056; -.
PRO; PR:Q9UM01; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000155465; -.
CleanEx; HS_SLC7A7; -.
ExpressionAtlas; Q9UM01; baseline and differential.
Genevisible; Q9UM01; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
GO; GO:0006865; P:amino acid transport; TAS:Reactome.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0000821; P:regulation of arginine metabolic process; IBA:GO_Central.
InterPro; IPR002293; AA/rel_permease1.
Pfam; PF13520; AA_permease_2; 1.
PIRSF; PIRSF006060; AA_transporter; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 511 Y+L amino acid transporter 1.
/FTId=PRO_0000054281.
TRANSMEM 37 57 Helical. {ECO:0000255}.
TRANSMEM 69 89 Helical. {ECO:0000255}.
TRANSMEM 107 127 Helical. {ECO:0000255}.
TRANSMEM 133 153 Helical. {ECO:0000255}.
TRANSMEM 160 180 Helical. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TRANSMEM 222 242 Helical. {ECO:0000255}.
TRANSMEM 259 279 Helical. {ECO:0000255}.
TRANSMEM 304 324 Helical. {ECO:0000255}.
TRANSMEM 383 403 Helical. {ECO:0000255}.
TRANSMEM 416 436 Helical. {ECO:0000255}.
TRANSMEM 441 461 Helical. {ECO:0000255}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K8}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K8}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 5 5 T -> I (in LPI; dbSNP:rs386833792).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039092.
VARIANT 36 36 Missing (in LPI; failed to induce
cationic amino acid transport activity).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039093.
VARIANT 50 50 M -> K (in LPI; failed to induce cationic
amino acid transport activity;
dbSNP:rs386833811).
{ECO:0000269|PubMed:15776427,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_030595.
VARIANT 53 53 S -> L (in LPI; dbSNP:rs386833793).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039094.
VARIANT 54 54 G -> V (in LPI; failed to induce cationic
amino acid transport activity;
dbSNP:rs121908677).
{ECO:0000269|PubMed:10655553,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_010261.
VARIANT 91 91 A -> V (in dbSNP:rs11568438).
{ECO:0000269|Ref.6}.
/FTId=VAR_039095.
VARIANT 124 124 L -> P (in LPI; dbSNP:rs386833814).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039096.
VARIANT 140 140 A -> P (in LPI; dbSNP:rs386833815).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039097.
VARIANT 152 152 F -> L (in LPI; moderately reduced
cationic amino acid transport activity;
dbSNP:rs386833816).
{ECO:0000269|PubMed:15756301,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_039098.
VARIANT 159 159 R -> C (in dbSNP:rs11568437).
/FTId=VAR_039099.
VARIANT 188 188 T -> I (in LPI; failed to induce cationic
amino acid transport activity;
dbSNP:rs386833819).
{ECO:0000269|PubMed:15776427,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_030596.
VARIANT 191 191 K -> E (in LPI; dbSNP:rs386833820).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039100.
VARIANT 238 238 S -> F (in LPI; dbSNP:rs386833823).
{ECO:0000269|PubMed:12402335,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_030597.
VARIANT 251 251 E -> D (in LPI; dbSNP:rs386833824).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039101.
VARIANT 261 261 L -> P (in LPI; dbSNP:rs386833825).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039102.
VARIANT 333 333 R -> M (in LPI; dbSNP:rs386833829).
{ECO:0000269|PubMed:15776427,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_030598.
VARIANT 334 334 L -> R (in LPI; failed to induce cationic
amino acid transport activity;
dbSNP:rs72552272).
{ECO:0000269|PubMed:10080182,
ECO:0000269|PubMed:10655553,
ECO:0000269|PubMed:17764084,
ECO:0000269|PubMed:9829974}.
/FTId=VAR_010262.
VARIANT 338 338 G -> D (in LPI; dbSNP:rs386833795).
{ECO:0000269|PubMed:10655553,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_010999.
VARIANT 365 365 N -> Y (in LPI; dbSNP:rs386833797).
{ECO:0000269|PubMed:17764084}.
/FTId=VAR_039103.
VARIANT 386 386 S -> R (in LPI; failed to induce cationic
amino acid transport activity;
dbSNP:rs386833799).
{ECO:0000269|PubMed:10631139,
ECO:0000269|PubMed:15776427,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_011000.
VARIANT 413 413 P -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036609.
VARIANT 489 489 S -> P (in LPI; dbSNP:rs386833810).
{ECO:0000269|PubMed:12402335,
ECO:0000269|PubMed:17764084}.
/FTId=VAR_030599.
SEQUENCE 511 AA; 55991 MW; A71D677B6B075894 CRC64;
MVDSTEYEVA SQPEVETSPL GDGASPGPEQ VKLKKEISLL NGVCLIVGNM IGSGIFVSPK
GVLIYSASFG LSLVIWAVGG LFSVFGALCY AELGTTIKKS GASYAYILEA FGGFLAFIRL
WTSLLIIEPT SQAIIAITFA NYMVQPLFPS CFAPYAASRL LAAACICLLT FINCAYVKWG
TLVQDIFTYA KVLALIAVIV AGIVRLGQGA STHFENSFEG SSFAVGDIAL ALYSALFSYS
GWDTLNYVTE EIKNPERNLP LSIGISMPIV TIIYILTNVA YYTVLDMRDI LASDAVAVTF
ADQIFGIFNW IIPLSVALSC FGGLNASIVA ASRLFFVGSR EGHLPDAICM IHVERFTPVP
SLLFNGIMAL IYLCVEDIFQ LINYYSFSYW FFVGLSIVGQ LYLRWKEPDR PRPLKLSVFF
PIVFCLCTIF LVAVPLYSDT INSLIGIAIA LSGLPFYFLI IRVPEHKRPL YLRRIVGSAT
RYLQVLCMSV AAEMDLEDGG EMPKQRDPKS N


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