LAT2_RABIT
ID LAT2_RABIT Reviewed; 535 AA.
AC Q9N1Q4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Large neutral amino acids transporter small subunit 2;
DE AltName: Full=4F2-LC5;
DE AltName: Full=L-type amino acid transporter 2;
DE AltName: Full=Solute carrier family 7 member 8;
GN Name=SLC7A8 {ECO:0000250|UniProtKB:Q9UHI5};
GN Synonyms=LAT2 {ECO:0000250|UniProtKB:Q9UHI5};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF26282.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, TISSUE SPECIFICITY, AND INHIBITION.
RC TISSUE=Intestine {ECO:0000269|PubMed:10631289};
RX PubMed=10631289; DOI=10.1016/s0005-2736(99)00224-2;
RA Rajan D.P., Kekuda R., Huang W., Devoe L.D., Leibach F.H., Prasad P.D.,
RA Ganapathy V.;
RT "Cloning and functional characterization of a Na(+)-independent, broad-
RT specific neutral amino acid transporter from mammalian intestine.";
RL Biochim. Biophys. Acta 1463:6-14(2000).
CC -!- FUNCTION: Sodium-independent, high-affinity transport of small and
CC large neutral amino acids such as alanine, serine, threonine, cysteine,
CC phenylalanine, tyrosine, leucine, arginine and tryptophan, when
CC associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has
CC higher affinity for L-phenylalanine than LAT1 but lower affinity for
CC glutamine and serine. L-alanine is transported at physiological
CC concentrations. Plays a role in basolateral (re)absorption of neutral
CC amino acids. Involved in the uptake of methylmercury (MeHg) when
CC administered as the L-cysteine or D,L-homocysteine complexes, and hence
CC plays a role in metal ion homeostasis and toxicity. Involved in the
CC cellular activity of small molecular weight nitrosothiols, via the
CC stereoselective transport of L-nitrosocysteine (L-CNSO) across the
CC transmembrane. Plays an essential role in the reabsorption of neutral
CC amino acids from the epithelial cells to the bloodstream in the kidney.
CC {ECO:0000269|PubMed:10631289}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=316 uM for glutamine {ECO:0000269|PubMed:10631289};
CC KM=204 uM for serine {ECO:0000269|PubMed:10631289};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:10631289};
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000269|PubMed:10631289}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Basolateral cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=Localized to the cytoplasm when expressed alone. When coexpressed
CC with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized
CC with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal
CC tubules and small intestine epithelia of the villi. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in kidney and small intestine.
CC {ECO:0000269|PubMed:10631289}.
CC -!- MISCELLANEOUS: The transport of glutamine and serine was inhibited by
CC glutamine, leucine, alanine, serine, cysteine, phenylalanine,
CC tryptophan threonine and by 2-aminobicyclo-(2,2,1)heptane-2-carboxylic
CC acid (BCH) (a specific inhibitor of system L transport).
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:0000255}.
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DR EMBL; AF170106; AAF26282.1; -; mRNA.
DR RefSeq; NP_001076151.1; NM_001082682.1.
DR AlphaFoldDB; Q9N1Q4; -.
DR SMR; Q9N1Q4; -.
DR STRING; 9986.ENSOCUP00000019754; -.
DR Ensembl; ENSOCUT00000022234; ENSOCUP00000019754; ENSOCUG00000001685.
DR GeneID; 100009408; -.
DR KEGG; ocu:100009408; -.
DR CTD; 23428; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000158278; -.
DR InParanoid; Q9N1Q4; -.
DR OMA; FTHLWND; -.
DR OrthoDB; 621852at2759; -.
DR TreeFam; TF313355; -.
DR SABIO-RK; Q9N1Q4; -.
DR Proteomes; UP000001811; Chromosome 17.
DR Bgee; ENSOCUG00000001685; Expressed in kidney and 18 other tissues.
DR ExpressionAtlas; Q9N1Q4; baseline.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0042605; F:peptide antigen binding; IPI:UniProtKB.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:1904273; P:L-alanine import across plasma membrane; IEA:Ensembl.
DR GO; GO:1903801; P:L-leucine import across plasma membrane; IEA:Ensembl.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR GO; GO:0035524; P:proline transmembrane transport; IEA:Ensembl.
DR GO; GO:0015827; P:tryptophan transport; IEA:Ensembl.
DR GO; GO:0015829; P:valine transport; IEA:Ensembl.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004760; L_AA_transporter.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00911; 2A0308; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Cytoplasm; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..535
FT /note="Large neutral amino acids transporter small subunit
FT 2"
FT /id="PRO_0000252234"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXW9"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXW9"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXW9"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVR6"
SQ SEQUENCE 535 AA; 58321 MW; D4939C0F971CB190 CRC64;
MEKGARHRHN TDKNHAGGSE SEDFPEASSG GGGVALKKEI GLVSACGIIV GNIIGSGIFV
SPKGVLENAG SVGLAVIVWI VTGLITAVGA LCYAELGVTI PKSGGDYSYV KDIFGGLAGF
LRLWIAVLVI YPTNQAVIAL TFSNYVLQPL FPTCFPPDSG LRLLAAICLL LLTWVNCSSV
RWATRVQDIF TAGKLLALAL IIIMGVVQIC KGEYFWLEPK NAFDNFQEPD IGLIALAFLQ
GSFAYGGWNF LNYVTEELVD PYKNLPRAIF ISIPLVTFVY VFANVAYITA MSPQELLASN
AVAVTFGEKL LGVMAWIMPI SVALSTFGGV NGSLFTSSRL FFAGAREGHL PSVLAMIHVK
RCTPIPALLF TCLSTLLMLV TSDMYTLINY VGFINYLFYG VTVAGQIVLR WKKPDIPRPI
KINLLFPIIY LLFWAFLLIF SLWSEPVVCG IGLAIMLTGV PVYFLGVYWQ HKPKCFNDFI
ELLTLVSQKM CVVVYPEVDG GSGTEGTRED MEEQQQPICQ PSPGKDKDSL EQSQP
