ID   YLAT1_RAT               Reviewed;         512 AA.
AC   Q9R0S5; Q9QZ66;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 137.
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|RGD:619902};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Kidney;
RX   PubMed=10777485; DOI=10.1074/jbc.m000634200;
RA   Kanai Y., Fukasawa Y., Cha S.H., Segawa H., Chairoungdua A., Kim D.K.,
RA   Matsuo H., Kim J.Y., Miyamoto K., Takeda E., Endou H.;
RT   "Transport properties of a system y+L neutral and basic amino acid
RT   transporter. Insights into the mechanisms of substrate recognition.";
RL   J. Biol. Chem. 275:20787-20793(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Ng A.M.L., Yao S.Y.M., Cheeseman C.I., Young J.D.;
RT   "cDNA encoding rat jejunal amino acid transporter y+LAT1.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   TISSUE SPECIFICITY.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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:10777485). Also mediates L-arginine transport in
CC       non-polarized cells, such as monocytes, and is essential for the
CC       correct function of these cells (By similarity). The transport
CC       mechanism is electroneutral and operates with a stoichiometry of 1:1
CC       (PubMed:10777485). In vitro, Na(+) and Li(+), but also H(+), are
CC       cotransported with the neutral amino acids (PubMed:10777485).
CC       {ECO:0000250|UniProtKB:Q9UM01, ECO:0000269|PubMed:10777485}.
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:0000269|PubMed:10777485};
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:0000269|PubMed:10777485};
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:0000269|PubMed:10777485};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=44 uM for L-leucine (in presence of 100 mM Na(+))
CC         {ECO:0000269|PubMed:10777485};
CC         KM=423 uM for L-leucine (in absence of Na(+))
CC         {ECO:0000269|PubMed:10777485};
CC         KM=68 uM for L-lysine (in presence of 100 mM Na(+))
CC         {ECO:0000269|PubMed:10777485};
CC         KM=50 uM for L-lysine (in absence of Na(+))
CC         {ECO:0000269|PubMed:10777485};
CC         KM=383 uM for L-leucine (in absence of Na(+) and pH 7.5)
CC         {ECO:0000269|PubMed:10777485};
CC         KM=119 uM for L-leucine (in absence of Na(+) and pH 5.5)
CC         {ECO:0000269|PubMed:10777485};
CC         KM=74 uM for L-lysine (in absence of Na(+) and pH 7.5)
CC         {ECO:0000305|PubMed:10777485};
CC         KM=81 uM for L-lysine (in absence of Na(+) and pH 5.5)
CC         {ECO:0000305|PubMed:10777485};
CC         KM=71.8 uM for sodium ion (in absence of Na(+) and pH 7.5)
CC         {ECO:0000269|PubMed:10777485};
CC         KM=105.9 uM for L-leucine (in absence of Na(+) and pH 5.5)
CC         {ECO:0000269|PubMed:10777485};
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC       protein SLC3A2/4F2hc. {ECO:0000250|UniProtKB:Q9UM01}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q9UM01}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney cortex and intestine.
CC       {ECO:0000269|PubMed:9878049}.
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; AB020520; BAA87325.1; -; mRNA.
DR   EMBL; AF200684; AAF07216.1; -; mRNA.
DR   EMBL; BC091142; AAH91142.1; -; mRNA.
DR   RefSeq; NP_112631.1; NM_031341.1.
DR   RefSeq; XP_006252082.1; XM_006252020.3.
DR   RefSeq; XP_006252083.1; XM_006252021.3.
DR   RefSeq; XP_006252085.1; XM_006252023.3.
DR   RefSeq; XP_006252086.1; XM_006252024.3.
DR   RefSeq; XP_008768927.1; XM_008770705.2.
DR   RefSeq; XP_017455296.1; XM_017599807.1.
DR   RefSeq; XP_017455297.1; XM_017599808.1.
DR   RefSeq; XP_017455298.1; XM_017599809.1.
DR   AlphaFoldDB; Q9R0S5; -.
DR   SMR; Q9R0S5; -.
DR   STRING; 10116.ENSRNOP00000014391; -.
DR   TCDB; 2.A.3.8.7; the amino acid-polyamine-organocation (apc) family.
DR   GlyCosmos; Q9R0S5; 1 site, No reported glycans.
DR   GlyGen; Q9R0S5; 1 site.
DR   iPTMnet; Q9R0S5; -.
DR   PhosphoSitePlus; Q9R0S5; -.
DR   PaxDb; 10116-ENSRNOP00000014391; -.
DR   Ensembl; ENSRNOT00000014391.6; ENSRNOP00000014391.3; ENSRNOG00000010296.7.
DR   Ensembl; ENSRNOT00055020211; ENSRNOP00055016295; ENSRNOG00055011879.
DR   Ensembl; ENSRNOT00060047414; ENSRNOP00060039470; ENSRNOG00060027322.
DR   Ensembl; ENSRNOT00065053967; ENSRNOP00065044399; ENSRNOG00065031287.
DR   GeneID; 83509; -.
DR   KEGG; rno:83509; -.
DR   UCSC; RGD:619902; rat.
DR   AGR; RGD:619902; -.
DR   CTD; 9056; -.
DR   RGD; 619902; Slc7a7.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000160134; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q9R0S5; -.
DR   OMA; YMAAWSW; -.
DR   OrthoDB; 1103451at2759; -.
DR   PhylomeDB; Q9R0S5; -.
DR   TreeFam; TF313355; -.
DR   Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR   PRO; PR:Q9R0S5; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000010296; Expressed in adult mammalian kidney and 18 other cell types or tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; ISO:RGD.
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:1990822; P:basic amino acid transmembrane transport; ISO:RGD.
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; ISO:RGD.
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; Q9R0S5; RN.
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..512
FT                   /note="Y+L amino acid transporter 1"
FT                   /id="PRO_0000304936"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        3
FT                   /note="A -> N (in Ref. 2; AAF07216)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  55641 MW;  708905B2ACB0A824 CRC64;
     MVASTKYEVA AQNEADEADG SAQGDGAGPA AEQVKLKKEI SLLNGVCLIV GNMIGSGIFV
     SPKGVLMYSA SFGLSLVIWA VGGIFSVFGA LCYAELGTTI KKSGASYAYI LEAFGGFLAF
     IRLWTSLLII EPTSQAVIAI TFANYMVQPL FPSCGAPYAA GRLLAAACIC LLTFINCAYV
     KWGTLVQDIF TYAKVLALIA VIIAGIVRLG QGATTNFEDS FEGSSFAMGD IALALYSALF
     SYSGWDTLNY VTEEIRNPER NLPLSIGISM PIVTIIYLLT NVAYYSVLDI KDILASDAVA
     VTFADQIFGI FNWTIPLAVA LSCFGGLNAS IVAASRLLFV GSREGHLPDA ICMIHVERFT
     PVPSLLFNGI LALVYLCVED IFQLINYYSF SYWFFVGLSI VGQLYLRWKE PDRPRPLKLS
     LFFPIVFCLC TIFLVAVPLY SDTINSLIGI GIALSGLPFY FLIIRVPEHK RPLCLRRIVA
     STTRYLQIIC MSVAAEMDLE DGELPKQGPK SK
//