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Large neutral amino acids transporter small subunit 1 (4F2 light chain) (4F2 LC) (4F2LC) (L-type amino acid transporter 1) (LAT1 light chain) (Solute carrier family 7 member 5)

 LAT1_RABIT              Reviewed;         503 AA.
Q7YQK4;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
22-NOV-2017, entry version 67.
RecName: Full=Large neutral amino acids transporter small subunit 1;
AltName: Full=4F2 light chain;
Short=4F2 LC;
Short=4F2LC;
AltName: Full=L-type amino acid transporter 1;
AltName: Full=LAT1 light chain;
AltName: Full=Solute carrier family 7 member 5;
Name=SLC7A5 {ECO:0000250|UniProtKB:Q01650};
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1] {ECO:0000305, ECO:0000312|EMBL:AAP47189.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
AND MUTAGENESIS OF GLY-219 AND TRP-234.
STRAIN=New Zealand {ECO:0000269|PubMed:12614332};
TISSUE=Brain capillary {ECO:0000269|PubMed:12614332};
PubMed=12614332; DOI=10.1046/j.1471-4159.2003.01622.x;
Boado R.J., Li J.Y., Pardridge W.M.;
"Site-directed mutagenesis of rabbit LAT1 at amino acids 219 and
234.";
J. Neurochem. 84:1322-1331(2003).
[2] {ECO:0000305}
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
INHIBITION.
PubMed=12824232; DOI=10.1167/iovs.02-0907;
Jain-Vakkalagadda B., Dey S., Pal D., Mitra A.K.;
"Identification and functional characterization of a Na+-independent
large neutral amino acid transporter, LAT1, in human and rabbit
cornea.";
Invest. Ophthalmol. Vis. Sci. 44:2919-2927(2003).
[3] {ECO:0000305}
DEVELOPMENTAL STAGE.
PubMed=14764922; DOI=10.1203/01.PDR.0000113461.07950.72;
Boado R.J., Li J.Y., Pardridge W.M.;
"Developmental regulation of the rabbit blood-brain barrier LAT1 large
neutral amino acid transporter mRNA and protein.";
Pediatr. Res. 55:557-560(2004).
[4] {ECO:0000305}
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-88;
CYS-98; CYS-160; CYS-172; CYS-174; CYS-183; CYS-331; CYS-377; CYS-403;
CYS-439; CYS-454 AND CYS-492.
PubMed=16125134; DOI=10.1016/j.bbamem.2005.07.007;
Boado R.J., Li J.Y., Chu C., Ogoshi F., Wise P., Pardridge W.M.;
"Site-directed mutagenesis of cysteine residues of large neutral amino
acid transporter LAT1.";
Biochim. Biophys. Acta 1715:104-110(2005).
-!- FUNCTION: Sodium-independent, high-affinity transport of large
neutral amino acids such as phenylalanine, tyrosine, leucine,
arginine and tryptophan, when associated with SLC3A2/4F2hc.
Involved in cellular amino acid uptake. Acts as an amino acid
exchanger. Involved in the transport of L-DOPA across the blood-
brain barrier, and that of thyroid hormones triiodothyronine (T3)
and thyroxine (T4) across the cell membrane. Plays a role in
neuronal cell proliferation (neurogenesis) in brain. Involved in
the uptake of methylmercury (MeHg) when administered as the L-
cysteine or D,L-homocysteine complexes, and hence plays a role in
metal ion homeostasis and toxicity. Involved in the cellular
activity of small molecular weight nitrosothiols, via the
stereoselective transport of L-nitrosocysteine (L-CNSO) across the
transmembrane. Mediates blood-to-retina L-leucine transport across
the inner blood-retinal barrier which in turn may play a key role
in maintaining large neutral amino acids as well as
neurotransmitters in the neural retina. Acts as the major
transporter of tyrosine in fibroblasts. When associated with
LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote
leucine uptake into these organelles and is required for mTORC1
activation (By similarity). {ECO:0000250|UniProtKB:Q01650,
ECO:0000269|PubMed:12614332, ECO:0000269|PubMed:12824232,
ECO:0000269|PubMed:16125134}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=27.0 uM for phenylalanine (in frog oocytes)
{ECO:0000269|PubMed:12614332};
KM=19.8 uM for phenylalanine (in frog oocytes)
{ECO:0000269|PubMed:16125134};
KM=73 uM for L-phenylalanine (in the rabbit corneal cell line
SIRC) {ECO:0000269|PubMed:12614332, ECO:0000269|PubMed:12824232,
ECO:0000269|PubMed:16125134};
KM=33 uM for L-phenylalanine (in the rabbit cornea)
{ECO:0000269|PubMed:12614332, ECO:0000269|PubMed:12824232,
ECO:0000269|PubMed:16125134};
KM=47.8 uM for tryptophan (in frog oocytes)
{ECO:0000269|PubMed:12614332, ECO:0000269|PubMed:12824232,
ECO:0000269|PubMed:16125134};
-!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
transport protein SLC3A2/4F2hc. Interacts with LAPTM4B; recruits
SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into
these organelles and is required for mTORC1 activation.
{ECO:0000250|UniProtKB:Q01650}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Apical
cell membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}. Note=Located to the plasma membrane by
SLC3A2/4F2hc. Expressed in both luminal and abluminal membranes of
brain capillary endothelial cells. Localized to the apical
membrane of placental syncytiophoblastic cells. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expression detected in cornea.
{ECO:0000269|PubMed:12824232}.
-!- DEVELOPMENTAL STAGE: Levels remain unchanged during postnatal
development (at protein level). {ECO:0000269|PubMed:14764922}.
-!- MISCELLANEOUS: Phenylalanine transport is inhibited by mercury, L-
alanine and charged amino acids. {ECO:0000269|PubMed:12824232,
ECO:0000269|PubMed:16125134}.
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
family. {ECO:0000255}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF515772; AAP47189.1; -; mRNA.
RefSeq; NP_001075589.1; NM_001082120.1.
UniGene; Ocu.3084; -.
STRING; 9986.ENSOCUP00000025624; -.
GeneID; 100008844; -.
KEGG; ocu:100008844; -.
CTD; 8140; -.
eggNOG; KOG1287; Eukaryota.
eggNOG; COG0531; LUCA.
HOGENOM; HOG000098892; -.
HOVERGEN; HBG000476; -.
InParanoid; Q7YQK4; -.
KO; K13780; -.
SABIO-RK; Q7YQK4; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IPI:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
InterPro; IPR002293; AA/rel_permease1.
InterPro; IPR004760; L_AA_transporter.
Pfam; PF13520; AA_permease_2; 1.
PIRSF; PIRSF006060; AA_transporter; 1.
TIGRFAMs; TIGR00911; 2A0308; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Membrane; Neurogenesis; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 503 Large neutral amino acids transporter
small subunit 1.
/FTId=PRO_0000252233.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TRANSMEM 166 186 Helical. {ECO:0000255}.
TRANSMEM 195 215 Helical. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255}.
TRANSMEM 315 335 Helical. {ECO:0000255}.
TRANSMEM 366 386 Helical. {ECO:0000255}.
TRANSMEM 389 409 Helical. {ECO:0000255}.
TRANSMEM 427 447 Helical. {ECO:0000255}.
TRANSMEM 454 474 Helical. {ECO:0000255}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 88 88 C->S: No significant effect on inhibition
by HgCl(2). Decreased KM and Vmax for
Phe. Similar affect on KM and Vmax for
Phe; when associated with S-183.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 98 98 C->S: No significant effect on inhibition
by HgCl(2). Slightly decreased KM and
Vmax for Phe. Slightly less decreased KM
and Vmax for Phe; when associated with S-
183. {ECO:0000269|PubMed:16125134}.
MUTAGEN 160 160 C->S: No change to KM or Vmax for Phe.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 172 172 C->S: No change to KM or Vmax for Phe.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 174 174 C->S: No change to KM or Vmax for Phe.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 183 183 C->S: No significant effect on inhibition
by HgCl(2). Slightly decreased KM and
Vmax for Phe. Similar affect on KM and
Vmax for Phe; when associated with S-88.
Slightly less decreased KM and Vmax for
Phe; when associated with S-98.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 219 219 G->D: Decreased KM and Vmax for Trp.
Increased KM and Vmax for Phe; when
associated with L-234.
{ECO:0000269|PubMed:12614332}.
MUTAGEN 234 234 W->L: Decreased KM and Vmax for Trp.
Increased KM but decreased Vmax for Phe.
Increased KM and Vmax for Phe; when
associated with D-219.
{ECO:0000269|PubMed:12614332}.
MUTAGEN 331 331 C->S: No significant effect on inhibition
by HgCl(2). Increased KM and Vmax for
Phe. {ECO:0000269|PubMed:16125134}.
MUTAGEN 377 377 C->S: No significant effect on inhibition
by HgCl(2).
{ECO:0000269|PubMed:16125134}.
MUTAGEN 403 403 C->S: No significant effect on inhibition
by HgCl(2).
{ECO:0000269|PubMed:16125134}.
MUTAGEN 439 439 C->S: Prevents insertion into the plasma
membrane and possibly protein folding.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 454 454 C->S: No significant effect on inhibition
by HgCl(2). Slightly increased KM but
slightly decreased Vmax for Phe.
{ECO:0000269|PubMed:16125134}.
MUTAGEN 492 492 C->S: No significant effect on inhibition
by HgCl(2). Slightly decreased KM and
Vmax for Phe.
{ECO:0000269|PubMed:16125134}.
SEQUENCE 503 AA; 54783 MW; DB3D649A74E8F9B3 CRC64;
MAGAGPKRRA AAAAAPEEER QAREKMLAAR REAEAEGEGV ALQRNITLLN GVAIIVGTII
GSGIFVTPTG VLKEAGSPGL SLVVWAVCGV FSIVGALCYA ELGTTITKSG GDYAYMLEVY
GSLPAFLKLW IELLIIRPSS QYIVALVFAT YLLKPVFPTC PVPEEAAKLV ACLCVLLLTA
VNCYSVKAAT RVQDAFAAAK LLALALIILL GFVQIGKGGV SNLDPKFSFE GTNWDVGNIV
LALYSGLFAY GGWNYLNFVT EEMINPYRNL PLAIIISLPI CTLVYVLTNL AYFTTLSPEQ
MLASEAVAVD FGNHHLGVMS WVIPVFVGLS CFGSVNGSLF TSSRLFFVGS REGHLPSVLS
MIHPQLLTPV PSLVFTCAMT LLYAFSRDIF SVINFFSFFN WLCVALAIIG MMWLRYKKPE
LERPIKVNLA LPVFFILACL FLIAVSFWKT PVECGIGFTI ILSGLPVYFF GVWWKNKPKW
LLQGIFSATA LCQKLMQVVP QET


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