YLAT1_HUMAN
ID YLAT1_HUMAN Reviewed; 511 AA.
AC Q9UM01; B2RAU0; D3DS26; O95984; Q53XC1; Q86U07; Q9P2V5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Y+L amino acid transporter 1;
DE AltName: Full=Monocyte amino acid permease 2;
DE Short=MOP-2;
DE AltName: Full=Solute carrier family 7 member 7;
DE AltName: Full=y(+)L-type amino acid transporter 1;
DE Short=Y+LAT1;
DE Short=y+LAT-1;
GN Name=SLC7A7;
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], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP VARIANT LPI ARG-334.
RX PubMed=9829974; DOI=10.1074/jbc.273.49.32437;
RA Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J., Shi Y.-B.,
RA Zorzano A., Palacin M.;
RT "Identification and characterization of a membrane protein (y+L amino acid
RT transporter-1) that associates with 4F2hc to encode the amino acid
RT transport activity y+L. A candidate gene for lysinuric protein
RT intolerance.";
RL J. Biol. Chem. 273:32437-32445(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Testis;
RX PubMed=9878049; DOI=10.1093/emboj/18.1.49;
RA Pfeiffer R., Rossier G., Spindler B., Meier C., Kuehn L.C., Verrey F.;
RT "Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members
RT of the glycoprotein-associated amino acid transporter family.";
RL EMBO J. 18:49-57(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10080183; DOI=10.1038/6815;
RA Borsani G., Bassi M.T., Sperandeo M.P., De Grandi A., Buoninconti A.,
RA Riboni M., Manzoni M., Incerti B., Pepe A., Andria G., Ballabio A.,
RA Sebastio G.;
RT "SLC7A7, encoding a putative permease-related protein, is mutated in
RT patients with lysinuric protein intolerance.";
RL Nat. Genet. 21:297-301(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10737982;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<367::aid-humu9>3.0.co;2-c;
RA Noguchi A., Shoji Y., Koizumi A., Takahashi T., Shoji Y., Matsumori M.,
RA Kayo T., Ohata T., Wada Y., Yoshimura I., Maisawa S., Konishi M.,
RA Takasago Y., Takada G.;
RT "SLC7A7 genomic structure and novel variants in three Japanese lysinuric
RT protein intolerance families.";
RL Hum. Mutat. 15:367-372(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Takayama K., Yoshimoto M.;
RT "Molecular and biological characterization of a novel monocyte amino acid
RT permease, MOP-2.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-91.
RC TISSUE=Kidney;
RA Fukasawa Y., Segawa H., Endou H., Kanai Y.;
RT "Characterization of a human system y+L amino acid transporter.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
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 [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [11]
RP TISSUE SPECIFICITY.
RX PubMed=11078698; DOI=10.1152/ajpcell.2000.279.6.c1829;
RA Dall'Asta V., Bussolati O., Sala R., Rotoli B.M., Sebastio G.,
RA Sperandeo M.P., Andria G., Gazzola G.C.;
RT "Arginine transport through system y(+)L in cultured human fibroblasts:
RT normal phenotype of cells from LPI subjects.";
RL Am. J. Physiol. 279:C1829-C1837(2000).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=11742806; DOI=10.1152/ajpcell.2002.282.1.c134;
RA Sala R., Rotoli B.M., Colla E., Visigalli R., Parolari A., Bussolati O.,
RA Gazzola G.C., Dall'Asta V.;
RT "Two-way arginine transport in human endothelial cells: TNF-alpha
RT stimulation is restricted to system y(+).";
RL Am. J. Physiol. 282:C134-C143(2002).
RN [13]
RP FUNCTION.
RX PubMed=14603368; DOI=10.1113/eph8802647;
RA Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.;
RT "Nitric oxide synthesis requires activity of the cationic and neutral amino
RT acid transport system y+L in human umbilical vein endothelium.";
RL Exp. Physiol. 88:699-710(2003).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15280038; DOI=10.1016/j.febslet.2004.06.086;
RA Rotoli B.M., Bussolati O., Sala R., Barilli A., Talarico E., Gazzola G.C.,
RA Dall'Asta V.;
RT "INFgamma stimulates arginine transport through system y+L in human
RT monocytes.";
RL FEBS Lett. 571:177-181(2004).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND INHIBITION.
RX PubMed=17329401; DOI=10.1152/ajpcell.00323.2006;
RA Rotmann A., Simon A., Martine U., Habermeier A., Closs E.I.;
RT "Activation of classical protein kinase C decreases transport via systems
RT y+ and y+L.";
RL Am. J. Physiol. 292:C2259-C2268(2007).
RN [16]
RP TISSUE SPECIFICITY.
RX PubMed=17197568; DOI=10.1167/iovs.06-0398;
RA Kaneko S., Ando A., Okuda-Ashitaka E., Maeda M., Furuta K., Suzuki M.,
RA Matsumura M., Ito S.;
RT "Ornithine transport via cationic amino acid transporter-1 is involved in
RT ornithine cytotoxicity in retinal pigment epithelial cells.";
RL Invest. Ophthalmol. Vis. Sci. 48:464-471(2007).
RN [17]
RP VARIANT LPI ARG-334, AND CHARACTERIZATION OF VARIANT LPI ARG-334.
RX PubMed=10080182; DOI=10.1038/6809;
RA Torrents D., Mykkaenen J., Pineda M., Feliubadalo L., Estevez R.,
RA de Cid R., Sanjurjo P., Zorzano A., Nunes V., Huoponen K., Reinikainen A.,
RA Simell O., Savontaus M.-L., Aula P., Palacin M.;
RT "Identification of SLC7A7, encoding y+LAT-1, as the lysinuric protein
RT intolerance gene.";
RL Nat. Genet. 21:293-296(1999).
RN [18]
RP VARIANT LPI ARG-386.
RX PubMed=10631139; DOI=10.1086/302700;
RA Sperandeo M.P., Bassi M.T., Riboni M., Parenti G., Buoninconti A.,
RA Manzoni M., Incerti B., Larocca M.R., Di Rocco M., Strisciuglio P.,
RA Dianzani I., Parini R., Candito M., Endo F., Ballabio A., Andria G.,
RA Sebastio G., Borsani G.;
RT "Structure of the SLC7A7 gene and mutational analysis of patients affected
RT by lysinuric protein intolerance.";
RL Am. J. Hum. Genet. 66:92-99(2000).
RN [19]
RP VARIANTS LPI VAL-54 AND ASP-338, AND CHARACTERIZATION OF VARIANTS LPI
RP VAL-54 AND ARG-334.
RX PubMed=10655553; DOI=10.1093/hmg/9.3.431;
RA Mykkaenen J., Torrents D., Pineda M., Camps M., Yoldi M.E.,
RA Horelli-Kuitunen N., Huoponen K., Heinonen M., Oksanen J., Simell O.,
RA Savontaus M.-L., Zorzano A., Palacin M., Aula P.;
RT "Functional analysis of novel mutations in y+LAT-1 amino acid transporter
RT gene causing lysinuric protein intolerance (LPI).";
RL Hum. Mol. Genet. 9:431-438(2000).
RN [20]
RP VARIANTS LPI PHE-238 AND PRO-489.
RX PubMed=12402335; DOI=10.1002/humu.10140;
RA Shoji Y., Noguchi A., Shoji Y., Matsumori M., Takasago Y., Takayanagi M.,
RA Yoshida Y., Ihara K., Hara T., Yamaguchi S., Yoshino M., Kaji M.,
RA Yamamoto S., Nakai A., Koizumi A., Hokezu Y., Nagamatsu K., Mikami H.,
RA Kitajima I., Takada G.;
RT "Five novel SLC7A7 variants and y+L gene-expression pattern in cultured
RT lymphoblasts from Japanese patients with lysinuric protein intolerance.";
RL Hum. Mutat. 20:375-381(2002).
RN [21]
RP CHARACTERIZATION OF VARIANTS LPI LEU-36 DEL AND LEU-152, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15756301; DOI=10.1038/sj.ejhg.5201376;
RA Sperandeo M.P., Paladino S., Maiuri L., Maroupulos G.D., Zurzolo C.,
RA Taglialatela M., Andria G., Sebastio G.;
RT "A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity:
RT implications for the molecular pathogenesis of lysinuric protein
RT intolerance.";
RL Eur. J. Hum. Genet. 13:628-634(2005).
RN [22]
RP VARIANTS LPI LYS-50; ILE-188 AND MET-333, AND CHARACTERIZATION OF VARIANTS
RP LPI LYS-50; ILE-188 AND ARG-386.
RX PubMed=15776427; DOI=10.1002/humu.9323;
RA Sperandeo M.P., Annunziata P., Ammendola V., Fiorito V., Pepe A.,
RA Soldovieri M.V., Taglialatela M., Andria G., Sebastio G.;
RT "Lysinuric protein intolerance: identification and functional analysis of
RT mutations of the SLC7A7 gene.";
RL Hum. Mutat. 25:410-410(2005).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] SER-413.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [24]
RP VARIANTS LPI ILE-5; GLU-36 DEL; LYS-50; LEU-53; VAL-54; PRO-124; PRO-140;
RP LEU-152; ILE-188; GLU-191; PHE-238; ASP-251; PRO-261; MET-333; ARG-334;
RP ASP-338; TYR-365; ARG-386 AND PRO-489.
RX PubMed=17764084; DOI=10.1002/humu.20589;
RA Sperandeo M.P., Andria G., Sebastio G.;
RT "Lysinuric protein intolerance: update and extended mutation analysis of
RT the SLC7A7 gene.";
RL Hum. Mutat. 29:14-21(2008).
CC -!- FUNCTION: Involved in the sodium-independent uptake of dibasic amino
CC acids and sodium-dependent uptake of some neutral amino acids. Requires
CC coexpression with SLC3A2/4F2hc to mediate the uptake of arginine,
CC leucine and glutamine. Plays a role in nitric oxide synthesis in human
CC umbilical vein endothelial cells (HUVECs) via transport of L-arginine.
CC Involved in the transport of L-arginine in monocytes.
CC {ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15280038,
CC ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:9829974,
CC ECO:0000269|PubMed:9878049}.
CC -!- ACTIVITY REGULATION: Arginine transport is inhibited by protein kinase
CC C (PKC) and treatment with phorbol-12-myristate-13-acetate (PMA).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.7 uM for L-leucine (in the presence of 0.1 M NaCl)
CC {ECO:0000269|PubMed:9878049};
CC KM=16.2 uM for L-leucine (in the presence of 0.1 M LiCl)
CC {ECO:0000269|PubMed:9878049};
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000269|PubMed:9829974,
CC ECO:0000269|PubMed:9878049}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:15756301}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15756301}.
CC -!- TISSUE SPECIFICITY: Highest expression in kidney and peripheral blood
CC leukocytes. Weaker expression is observed in lung, heart, placenta,
CC spleen, testis and small intestine. Expressed in normal fibroblasts and
CC those from LPI patients. Also expressed in HUVECs, monocytes, retinal
CC pigment epithelial cells, and various carcinoma cell lines, with
CC highest expression in a colon-carcinoma cell line.
CC {ECO:0000269|PubMed:10080183, ECO:0000269|PubMed:11078698,
CC ECO:0000269|PubMed:11742806, ECO:0000269|PubMed:15280038,
CC ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401,
CC ECO:0000269|PubMed:9829974}.
CC -!- INDUCTION: Expression is stimulated and enhanced by IFNG/IFN-gamma.
CC {ECO:0000269|PubMed:15280038}.
CC -!- DISEASE: Lysinuric protein intolerance (LPI) [MIM:222700]: A metabolic
CC disorder characterized by increased renal excretion of cationic amino
CC acid (CAA), reduced CAA absorption from intestine, and orotic aciduria.
CC On a normal diet, LPI patients present poor feeding, vomiting,
CC diarrhea, episodes of hyperammoniaemic coma and growth retardation.
CC Hepatosplenomegaly, osteoporosis and a life-threatening pulmonary
CC involvement (alveolar proteinosis) are also seen. Biochemically LPI is
CC characterized by defective transport of dibasic amino acids at the
CC basolateral membrane of epithelial cells in kidney and intestine.
CC {ECO:0000269|PubMed:10080182, ECO:0000269|PubMed:10631139,
CC ECO:0000269|PubMed:10655553, ECO:0000269|PubMed:12402335,
CC ECO:0000269|PubMed:15756301, ECO:0000269|PubMed:15776427,
CC ECO:0000269|PubMed:17764084, ECO:0000269|PubMed:9829974}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD62619.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF092032; AAC83706.1; -; mRNA.
DR EMBL; AJ130718; CAA10198.1; -; mRNA.
DR EMBL; Y18474; CAB40136.1; -; mRNA.
DR EMBL; AB031537; BAA95120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB011263; BAB11849.1; -; mRNA.
DR EMBL; AB020532; BAA87623.1; -; mRNA.
DR EMBL; BX161519; CAD61952.1; -; mRNA.
DR EMBL; BX248291; CAD62619.1; ALT_INIT; mRNA.
DR EMBL; AK314351; BAG36987.1; -; mRNA.
DR EMBL; CH471078; EAW66245.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66246.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66247.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66248.1; -; Genomic_DNA.
DR EMBL; BC003062; AAH03062.1; -; mRNA.
DR EMBL; BC010107; AAH10107.1; -; mRNA.
DR CCDS; CCDS9574.1; -.
DR RefSeq; NP_001119577.1; NM_001126105.2.
DR RefSeq; NP_001119578.1; NM_001126106.2.
DR RefSeq; XP_006720365.1; XM_006720302.1.
DR RefSeq; XP_011535600.1; XM_011537298.2.
DR RefSeq; XP_011535601.1; XM_011537299.1.
DR AlphaFoldDB; Q9UM01; -.
DR SMR; Q9UM01; -.
DR BioGRID; 114518; 5.
DR IntAct; Q9UM01; 1.
DR STRING; 9606.ENSP00000380666; -.
DR DrugBank; DB08838; Agmatine.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB00130; L-Glutamine.
DR TCDB; 2.A.3.8.22; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; Q9UM01; 1 site.
DR iPTMnet; Q9UM01; -.
DR PhosphoSitePlus; Q9UM01; -.
DR BioMuta; SLC7A7; -.
DR DMDM; 12643378; -.
DR jPOST; Q9UM01; -.
DR MassIVE; Q9UM01; -.
DR MaxQB; Q9UM01; -.
DR PaxDb; Q9UM01; -.
DR PeptideAtlas; Q9UM01; -.
DR PRIDE; Q9UM01; -.
DR ProteomicsDB; 85165; -.
DR Antibodypedia; 22283; 79 antibodies from 19 providers.
DR DNASU; 9056; -.
DR Ensembl; ENST00000285850.11; ENSP00000285850.7; ENSG00000155465.20.
DR Ensembl; ENST00000397528.8; ENSP00000380662.4; ENSG00000155465.20.
DR Ensembl; ENST00000397529.6; ENSP00000380663.2; ENSG00000155465.20.
DR Ensembl; ENST00000397532.9; ENSP00000380666.4; ENSG00000155465.20.
DR Ensembl; ENST00000555702.5; ENSP00000451881.1; ENSG00000155465.20.
DR Ensembl; ENST00000674313.1; ENSP00000501493.1; ENSG00000155465.20.
DR GeneID; 9056; -.
DR KEGG; hsa:9056; -.
DR MANE-Select; ENST00000674313.1; ENSP00000501493.1; NM_003982.4; NP_003973.3.
DR UCSC; uc001wgr.5; human.
DR CTD; 9056; -.
DR DisGeNET; 9056; -.
DR GeneCards; SLC7A7; -.
DR GeneReviews; SLC7A7; -.
DR HGNC; HGNC:11065; SLC7A7.
DR HPA; ENSG00000155465; Tissue enhanced (intestine, kidney).
DR MalaCards; SLC7A7; -.
DR MIM; 222700; phenotype.
DR MIM; 603593; gene.
DR neXtProt; NX_Q9UM01; -.
DR OpenTargets; ENSG00000155465; -.
DR Orphanet; 470; Lysinuric protein intolerance.
DR PharmGKB; PA35925; -.
DR VEuPathDB; HostDB:ENSG00000155465; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000160134; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q9UM01; -.
DR OMA; VLAYYSF; -.
DR OrthoDB; 867824at2759; -.
DR PhylomeDB; Q9UM01; -.
DR TreeFam; TF313355; -.
DR PathwayCommons; Q9UM01; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-5660862; Defective SLC7A7 causes lysinuric protein intolerance (LPI).
DR SABIO-RK; Q9UM01; -.
DR SignaLink; Q9UM01; -.
DR BioGRID-ORCS; 9056; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; SLC7A7; human.
DR GeneWiki; SLC7A7; -.
DR GenomeRNAi; 9056; -.
DR Pharos; Q9UM01; Tbio.
DR PRO; PR:Q9UM01; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UM01; protein.
DR Bgee; ENSG00000155465; Expressed in secondary oocyte and 137 other tissues.
DR ExpressionAtlas; Q9UM01; baseline and differential.
DR Genevisible; Q9UM01; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990822; P:basic amino acid transmembrane transport; TAS:GO_Central.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IBA:GO_Central.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..511
FT /note="Y+L amino acid transporter 1"
FT /id="PRO_0000054281"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1K8"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1K8"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 5
FT /note="T -> I (in LPI; dbSNP:rs386833792)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039092"
FT VARIANT 36
FT /note="Missing (in LPI; failed to induce cationic amino
FT acid transport activity)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039093"
FT VARIANT 50
FT /note="M -> K (in LPI; failed to induce cationic amino acid
FT transport activity; dbSNP:rs386833811)"
FT /evidence="ECO:0000269|PubMed:15776427,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_030595"
FT VARIANT 53
FT /note="S -> L (in LPI; dbSNP:rs386833793)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039094"
FT VARIANT 54
FT /note="G -> V (in LPI; failed to induce cationic amino acid
FT transport activity; dbSNP:rs121908677)"
FT /evidence="ECO:0000269|PubMed:10655553,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_010261"
FT VARIANT 91
FT /note="A -> V (in dbSNP:rs11568438)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_039095"
FT VARIANT 124
FT /note="L -> P (in LPI; dbSNP:rs386833814)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039096"
FT VARIANT 140
FT /note="A -> P (in LPI; dbSNP:rs386833815)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039097"
FT VARIANT 152
FT /note="F -> L (in LPI; moderately reduced cationic amino
FT acid transport activity; dbSNP:rs386833816)"
FT /evidence="ECO:0000269|PubMed:15756301,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_039098"
FT VARIANT 159
FT /note="R -> C (in dbSNP:rs11568437)"
FT /id="VAR_039099"
FT VARIANT 188
FT /note="T -> I (in LPI; failed to induce cationic amino acid
FT transport activity; dbSNP:rs386833819)"
FT /evidence="ECO:0000269|PubMed:15776427,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_030596"
FT VARIANT 191
FT /note="K -> E (in LPI; dbSNP:rs386833820)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039100"
FT VARIANT 238
FT /note="S -> F (in LPI; dbSNP:rs386833823)"
FT /evidence="ECO:0000269|PubMed:12402335,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_030597"
FT VARIANT 251
FT /note="E -> D (in LPI; dbSNP:rs386833824)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039101"
FT VARIANT 261
FT /note="L -> P (in LPI; dbSNP:rs386833825)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039102"
FT VARIANT 333
FT /note="R -> M (in LPI; dbSNP:rs386833829)"
FT /evidence="ECO:0000269|PubMed:15776427,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_030598"
FT VARIANT 334
FT /note="L -> R (in LPI; failed to induce cationic amino acid
FT transport activity; dbSNP:rs72552272)"
FT /evidence="ECO:0000269|PubMed:10080182,
FT ECO:0000269|PubMed:10655553, ECO:0000269|PubMed:17764084,
FT ECO:0000269|PubMed:9829974"
FT /id="VAR_010262"
FT VARIANT 338
FT /note="G -> D (in LPI; dbSNP:rs386833795)"
FT /evidence="ECO:0000269|PubMed:10655553,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_010999"
FT VARIANT 365
FT /note="N -> Y (in LPI; dbSNP:rs386833797)"
FT /evidence="ECO:0000269|PubMed:17764084"
FT /id="VAR_039103"
FT VARIANT 386
FT /note="S -> R (in LPI; failed to induce cationic amino acid
FT transport activity; dbSNP:rs386833799)"
FT /evidence="ECO:0000269|PubMed:10631139,
FT ECO:0000269|PubMed:15776427, ECO:0000269|PubMed:17764084"
FT /id="VAR_011000"
FT VARIANT 413
FT /note="P -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036609"
FT VARIANT 489
FT /note="S -> P (in LPI; dbSNP:rs386833810)"
FT /evidence="ECO:0000269|PubMed:12402335,
FT ECO:0000269|PubMed:17764084"
FT /id="VAR_030599"
SQ 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
