ID G3Q631_GASAC Unreviewed; 479 AA.
AC G3Q631;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Large neutral amino acids transporter small subunit 2 {ECO:0000256|ARBA:ARBA00040823};
DE AltName: Full=L-type amino acid transporter 2 {ECO:0000256|ARBA:ARBA00042153};
DE AltName: Full=Solute carrier family 7 member 8 {ECO:0000256|ARBA:ARBA00042897};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000025337.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000025337.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000025337.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-
CC thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015;
CC Evidence={ECO:0000256|ARBA:ARBA00036782};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812;
CC Evidence={ECO:0000256|ARBA:ARBA00036782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,3'-diiodo-L-thyronine(out) = 3,3'-diiodo-L-thyronine(in);
CC Xref=Rhea:RHEA:71823, ChEBI:CHEBI:176514;
CC Evidence={ECO:0000256|ARBA:ARBA00036268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71824;
CC Evidence={ECO:0000256|ARBA:ARBA00036268};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) + L-phenylalanine(out) = L-alanine(out) + L-
CC phenylalanine(in); Xref=Rhea:RHEA:71043, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) + L-phenylalanine(out) = L-cysteine(out) + L-
CC phenylalanine(in); Xref=Rhea:RHEA:71031, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(out) + L-methionine(in) = L-cysteine(in) + L-
CC methionine(out); Xref=Rhea:RHEA:71055, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57844; Evidence={ECO:0000256|ARBA:ARBA00036858};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dopa(out) + L-phenylalanine(in) = L-dopa(in) + L-
CC phenylalanine(out); Xref=Rhea:RHEA:71439, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-phenylalanine(out) = L-glutamine(out) + L-
CC phenylalanine(in); Xref=Rhea:RHEA:71027, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58359; Evidence={ECO:0000256|ARBA:ARBA00036982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine(in) + L-phenylalanine(out) = L-histidine(out) + L-
CC phenylalanine(in); Xref=Rhea:RHEA:71003, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-isoleucine(in) + L-phenylalanine(out) = L-isoleucine(out) +
CC L-phenylalanine(in); Xref=Rhea:RHEA:71011, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine(in) + L-phenylalanine(out) = L-leucine(out) + L-
CC phenylalanine(in); Xref=Rhea:RHEA:71023, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine(out) + L-methionine(in) = L-leucine(in) + L-
CC methionine(out); Xref=Rhea:RHEA:71051, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:57844; Evidence={ECO:0000256|ARBA:ARBA00036218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine(out) + S-methylmercury-L-cysteine(in) = L-
CC leucine(in) + S-methylmercury-L-cysteine(out); Xref=Rhea:RHEA:71107,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:190186;
CC Evidence={ECO:0000256|ARBA:ARBA00035915};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine(in) + L-phenylalanine(out) = L-methionine(out) +
CC L-phenylalanine(in); Xref=Rhea:RHEA:71039, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine(in) + S-methylmercury-L-cysteine(out) = L-
CC methionine(out) + S-methylmercury-L-cysteine(in);
CC Xref=Rhea:RHEA:71103, ChEBI:CHEBI:57844, ChEBI:CHEBI:190186;
CC Evidence={ECO:0000256|ARBA:ARBA00036006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(out) + L-serine(in) = L-phenylalanine(in) + L-
CC serine(out); Xref=Rhea:RHEA:71035, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00035793};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(out) + L-tryptophan(in) = L-phenylalanine(in)
CC + L-tryptophan(out); Xref=Rhea:RHEA:71007, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(out) + L-valine(in) = L-phenylalanine(in) + L-
CC valine(out); Xref=Rhea:RHEA:71019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036762};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(out) + S-methylmercury-L-cysteine(in) = L-
CC phenylalanine(in) + S-methylmercury-L-cysteine(out);
CC Xref=Rhea:RHEA:71111, ChEBI:CHEBI:58095, ChEBI:CHEBI:190186;
CC Evidence={ECO:0000256|ARBA:ARBA00036087};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) + L-phenylalanine(out) = glycine(out) + L-
CC phenylalanine(in); Xref=Rhea:RHEA:71047, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00037022};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004554}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034693}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:0000256|ARBA:ARBA00007040}.
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DR AlphaFoldDB; G3Q631; -.
DR Ensembl; ENSGACT00000025386.1; ENSGACP00000025337.1; ENSGACG00000019161.1.
DR GeneTree; ENSGT00940000158278; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000019161; Expressed in intestinal epithelial cell and 12 other cell types or tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015804; P:neutral amino acid transport; IEA:UniProt.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004760; L_AA_transporter.
DR NCBIfam; TIGR00911; 2A0308; 1.
DR PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR PANTHER; PTHR11785:SF113; LARGE NEUTRAL AMINO ACIDS TRANSPORTER SMALL SUBUNIT 2; 1.
DR Pfam; PF13520; AA_permease_2; 1.
DR PIRSF; PIRSF006060; AA_transporter; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 51898 MW; 3AD4D9D56D53B778 CRC64;
MTDGARKRSG TSGSAGDAAG EKDSGGGVAL KKEIGLVSAC GIIVGNIIGS GIFVSPKGVM
ENASSVGMAL IVWIVTGVIT AIGALCYAEL GVTIPKSGGD YSYVKDIFGG LAGFLRLWIA
VLVIYPTNQA VIALTFSNYV LQPLFPTCFP PENGLRLLAG VCLLLLTWVN CSSVRWATRV
QDVFTAGKLL ALALIIVMGL VQICKGEYYW LEPANAFEPF QEYDVGLIAL AFLQGSFAYG
GWNFLNYVTE ELVDPYVNLP RAIFISIPLV TFVYVFANIA YVTAMSPQEL LASNAVAVTF
GEKLLGVMSW IMPISVALST FGGVNGSLFT SSRLFFAGAR EGHLPSLLAM IHVKRCTPIP
ALLFTCLSTL LMLCTSDMYT LINYVGFINY LFYGVTVAGQ IVLRIRQPDM HRPIKISLIW
PVIYLLFWAF LLIFSLYSEP VVCGIGLAIM LTGVPVYFLG VYWDNKPQCF DAFVGKKHA
//
