ID   YLAT1_MOUSE             Reviewed;         510 AA.
AC   Q9Z1K8; Q9QWS1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Y+L amino acid transporter 1 {ECO:0000305};
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 {ECO:0000312|MGI:MGI:1337120};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, TISSUE SPECIFICITY, AND VARIANT THR-4.
RC   STRAIN=BALB/cJ, and NIH Swiss; TISSUE=Heart, and Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17376816; DOI=10.1152/ajpcell.00583.2006;
RA   Sperandeo M.P., Annunziata P., Bozzato A., Piccolo P., Maiuri L.,
RA   D'Armiento M., Ballabio A., Corso G., Andria G., Borsani G., Sebastio G.;
RT   "Slc7a7 disruption causes fetal growth retardation by downregulating Igf1
RT   in the mouse model of lysinuric protein intolerance.";
RL   Am. J. Physiol. 293:C191-C198(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-26, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=31653080; DOI=10.3390/ijms20215294;
RA   Bodoy S., Sotillo F., Espino-Guarch M., Sperandeo M.P., Ormazabal A.,
RA   Zorzano A., Sebastio G., Artuch R., Palacin M.;
RT   "Inducible Slc7a7 Knockout Mouse Model Recapitulates Lysinuric Protein
RT   Intolerance Disease.";
RL   Int. J. Mol. Sci. 20:0-0(2019).
CC   -!- FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter
CC       which operates as an efflux route by exporting cationic amino acids
CC       from inside the cells in exchange with neutral amino acids plus sodium
CC       ions and may participate in nitric oxide synthesis via the transport of
CC       L-arginine (PubMed:9878049). Also mediates L-arginine transport in non-
CC       polarized cells, such as monocytes, and is essential for the correct
CC       function of these cells (By similarity). The transport mechanism is
CC       electroneutral and operates with a stoichiometry of 1:1 (By
CC       similarity). In vitro, Na(+) and Li(+), but also H(+), are
CC       cotransported with the neutral amino acids (By similarity).
CC       {ECO:0000250|UniProtKB:Q9R0S5, ECO:0000250|UniProtKB:Q9UM01,
CC       ECO:0000269|PubMed:9878049}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-leucine(out) + Na(+)(out) = L-arginine(out)
CC         + L-leucine(in) + Na(+)(in); Xref=Rhea:RHEA:70831, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000250|UniProtKB:Q9R0S5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine(out) + L-lysine(in) + Na(+)(out) = L-leucine(in) +
CC         L-lysine(out) + Na(+)(in); Xref=Rhea:RHEA:74971, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000250|UniProtKB:Q9R0S5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine(out) + L-ornithine(in) + Na(+)(out) = L-leucine(in)
CC         + L-ornithine(out) + Na(+)(in); Xref=Rhea:RHEA:74963,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:46911, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000250|UniProtKB:Q9R0S5};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=91.5 uM for L-arginine (in the absence of NaCl)
CC         {ECO:0000269|PubMed:9878049};
CC         KM=340.8 uM for L-arginine (in the presence of 0.1 M NaCl)
CC         {ECO:0000269|PubMed:9878049};
CC         KM=21.7 uM for L-leucine (in the presence of 0.1 M NaCl)
CC         {ECO:0000269|PubMed:9878049};
CC         KM=1.36 mM for L-alanine (in the presence of 0.1 M NaCl)
CC         {ECO:0000269|PubMed:9878049};
CC         KM=47.9 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:9878049}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q9UM01}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in kidney and intestine. Weaker
CC       expression observed in epididymis, testis, ovary, thyroid pancreas,
CC       sub-gland and liver. {ECO:0000269|PubMed:9878049}.
CC   -!- DISRUPTION PHENOTYPE: A mouse model for human lysinuric protein
CC       intolerance (LPI), where homozygous knockout mice for Slc7a7 gene are
CC       born at a frequency lower than the expected Mendelian ratio
CC       (PubMed:17376816). Only two homozygous mice survived, whereas 16 of
CC       them died within 24 hours of birth (PubMed:17376816). Growth
CC       retardation is an ongoing feature of the two surviving mice kept on a
CC       low-protein diet with citrulline supplementation. After a planned
CC       withdrawal of the special diet both mice show an acute metabolic
CC       derangement, identical to that found in human LPI, leading to death of
CC       both animals after severe hyperammonemic neurological symptoms
CC       (PubMed:17376816). Tamoxifen-inducible Slc7a7 homozygous knockout mice
CC       model resembles the human LPI phenotype, including malabsorption and
CC       impaired reabsorption of cationic amino acid (CAA), hypoargininemia and
CC       hyperammonemia. Mice also develops pulmonar alveolar proteinosis (PAP)
CC       and neurological impairment (PubMed:31653080).
CC       {ECO:0000269|PubMed:17376816, ECO:0000269|PubMed:31653080}.
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}.
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DR   EMBL; AJ012754; CAA10170.1; -; mRNA.
DR   EMBL; AJ130943; CAA10255.1; -; mRNA.
DR   EMBL; AK150950; BAE29983.1; -; mRNA.
DR   EMBL; AK151718; BAE30637.1; -; mRNA.
DR   EMBL; AK152637; BAE31379.1; -; mRNA.
DR   EMBL; AK170851; BAE42073.1; -; mRNA.
DR   EMBL; BC014709; AAH14709.1; -; mRNA.
DR   CCDS; CCDS27087.1; -.
DR   RefSeq; NP_001240608.1; NM_001253679.1.
DR   RefSeq; NP_001240609.1; NM_001253680.1.
DR   RefSeq; NP_035535.2; NM_011405.4.
DR   RefSeq; XP_006518811.1; XM_006518748.2.
DR   RefSeq; XP_006518814.1; XM_006518751.2.
DR   RefSeq; XP_006518815.1; XM_006518752.1.
DR   RefSeq; XP_006518816.1; XM_006518753.1.
DR   RefSeq; XP_006518817.1; XM_006518754.3.
DR   RefSeq; XP_006518818.1; XM_006518755.3.
DR   AlphaFoldDB; Q9Z1K8; -.
DR   SMR; Q9Z1K8; -.
DR   BioGRID; 203319; 1.
DR   STRING; 10090.ENSMUSP00000143743; -.
DR   GlyCosmos; Q9Z1K8; 2 sites, No reported glycans.
DR   GlyGen; Q9Z1K8; 2 sites.
DR   iPTMnet; Q9Z1K8; -.
DR   PhosphoSitePlus; Q9Z1K8; -.
DR   jPOST; Q9Z1K8; -.
DR   MaxQB; Q9Z1K8; -.
DR   PaxDb; 10090-ENSMUSP00000000984; -.
DR   PeptideAtlas; Q9Z1K8; -.
DR   ProteomicsDB; 275226; -.
DR   Antibodypedia; 22283; 84 antibodies from 19 providers.
DR   DNASU; 20540; -.
DR   Ensembl; ENSMUST00000000984.9; ENSMUSP00000000984.5; ENSMUSG00000000958.11.
DR   Ensembl; ENSMUST00000195970.5; ENSMUSP00000143091.2; ENSMUSG00000000958.11.
DR   Ensembl; ENSMUST00000197440.5; ENSMUSP00000143743.2; ENSMUSG00000000958.11.
DR   Ensembl; ENSMUST00000226753.2; ENSMUSP00000154533.2; ENSMUSG00000000958.11.
DR   GeneID; 20540; -.
DR   KEGG; mmu:20540; -.
DR   UCSC; uc007tvv.2; mouse.
DR   AGR; MGI:1337120; -.
DR   CTD; 9056; -.
DR   MGI; MGI:1337120; Slc7a7.
DR   VEuPathDB; HostDB:ENSMUSG00000000958; -.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000160134; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q9Z1K8; -.
DR   OMA; YMAAWSW; -.
DR   OrthoDB; 1103451at2759; -.
DR   PhylomeDB; Q9Z1K8; -.
DR   TreeFam; TF313355; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   SABIO-RK; Q9Z1K8; -.
DR   BioGRID-ORCS; 20540; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q9Z1K8; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9Z1K8; Protein.
DR   Bgee; ENSMUSG00000000958; Expressed in small intestine Peyer's patch and 135 other cell types or tissues.
DR   ExpressionAtlas; Q9Z1K8; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IMP:MGI.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015820; P:leucine transport; ISS:UniProtKB.
DR   GO; GO:0000821; P:regulation of arginine metabolic process; IMP:MGI.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR11785:SF303; Y+L AMINO ACID TRANSPORTER 1; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; Q9Z1K8; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..510
FT                   /note="Y+L amino acid transporter 1"
FT                   /id="PRO_0000304935"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         4
FT                   /note="S -> T"
FT                   /evidence="ECO:0000269|PubMed:9878049"
SQ   SEQUENCE   510 AA;  55677 MW;  9F30FB1B88126F6C CRC64;
     MVNSTKYEVA AQHEADDGSA LGDGASPVAE QVKLKKEISL LNGVCLIVGN MIGSGIFVSP
     KGVLMYSASF GLSLVIWAVG GIFSVFGALC YAELGTTIKK SGASYAYILE AFGGFLAFIR
     LWTSLLIIEP TSQAVIAITF ANYMVQPLFP SCGAPYAAGR LLAAACICLL TFINCAYVKW
     GTLVQDIFTY AKVLALIAVI IAGIVRLGQG ATANFENSFE GSSFAMGDIA LALYSALFSY
     SGWDTLNYVT EEIRNPERNL PLSIGISMPI VTIIYLLTNV AYYSVLDIKE ILASDAVAVT
     FADQIFGVFN WIIPVAVAFS CFGGLNASIV AASRLLFVGS REGHLPDAIC MVHVERFTPV
     PSLLFNGVLS LVYLCVEDIF QLINYYSFSY WFFVGLSIVG QLYLRWKDPD RPRPLKLSLF
     FPIIFCLCTI FLVAVPLYSD TINSLIGIGI ALSGLPFYFF IIRVPEHKRP LFLRRIVASI
     TRYLQILCMS VAAEMDLEDG ELSKQDPKSK
//