LAT2_PONAB
ID LAT2_PONAB Reviewed; 535 AA.
AC Q5RAE3; Q5R9Q0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Large neutral amino acids transporter small subunit 2;
DE AltName: Full=L-type amino acid transporter 2;
DE AltName: Full=Solute carrier family 7 member 8;
GN Name=SLC7A8; Synonyms=LAT2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000250}.
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 -!- 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; CR859074; CAH91267.1; -; mRNA.
DR EMBL; CR859333; CAH91510.1; -; mRNA.
DR RefSeq; NP_001125888.1; NM_001132416.1.
DR AlphaFoldDB; Q5RAE3; -.
DR SMR; Q5RAE3; -.
DR STRING; 9601.ENSPPYP00000006436; -.
DR GeneID; 100172820; -.
DR KEGG; pon:100172820; -.
DR CTD; 23428; -.
DR eggNOG; KOG1287; Eukaryota.
DR InParanoid; Q5RAE3; -.
DR OrthoDB; 621852at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000297538"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
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 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXW9"
FT CONFLICT 2
FT /note="E -> G (in Ref. 1; CAH91267)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> T (in Ref. 1; CAH91510)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="W -> R (in Ref. 1; CAH91510)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="I -> M (in Ref. 1; CAH91267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 58364 MW; A852D546353F1E47 CRC64;
MEEGARHRNN TEKKHPGGGE SDASPEAGSG GGGVALKKEI GLVSACGIIV GNIIGSGIFV
SPKGVLENAG SVGLALIVWI VTGFITVVGA LCYAELGVTI PKSGGDYSYV KDIFGGLAGF
LRLWIAVLVI YPTNQAVIAL TFSNYVLQPL FPTCFPPESG LRLLAAICLL LLTWVNCSSV
RWATRVQDIF TAGKLLALAL IIIMGIVQIC KGEYFWLEPK NAFENFQEPD IGLVALAFLQ
GSFAYGGWNF LNYVTEELVD PYKNLPRAIF ISIPLVTFVY VFANVAYVTA MSPQELLASN
AVAVTFGEKL LGVMAWIMPI SVALSTFGGV NGSLFTSSRL FFAGAREGHL PSVLAMIHVK
RCTPIPALLF TCISTLLMLV TSDMYTLINY VGFINYLFYG VTVAGQIVLR WKKPDIPRPI
KINLLFPIIY LLFWAFLLVF SLWSEPVVCG IGLAIMLTGV PVYFLGVYWQ HKPKCFSDFI
ELLTLVSQKM CVVVYPEVER GSGTEEANED IEEQQQPMYQ PTPTKDKDVA GQPQP
