SLC43A2
entrez
124935
canonical
uniprot
Q8N370
canonical
ensembl
ENSG00000167703
resolver
ensembl
ENSG00000278550
resolver
ensp
ENSP00000301335
resolver
ensp
ENSP00000408284
resolver
ensp
ENSP00000461382
resolver
ensp
ENSP00000622330
resolver
ensp
ENSP00000622331
resolver
ensp
ENSP00000651798
resolver
genesymbol
SLC43A2
resolver
genesymbol_syn
LAT4
resolver
hgnc
HGNC:23087
resolver
uniprot
B7Z6X9
resolver
uniprot
C9JNU8
resolver
uniprot
D3DTH9
resolver
uniprot
Q5CD75
resolver
uniprot
Q6IPM1
resolver
uniprot
Q8NBX1
resolver
uniprot
Q8NC21
resolver
uniprot
Q8WZ00
resolver
uniprot_entry
LAT4_HUMAN
resolver
uniprot_sec
B7Z6X9
resolver
uniprot_sec
C9JNU8
resolver
uniprot_sec
D3DTH9
resolver
uniprot_sec
Q5CD75
resolver
uniprot_sec
Q6IPM1
resolver
uniprot_sec
Q8NBX1
resolver
uniprot_sec
Q8NC21
resolver
uniprot_sec
Q8WZ00
resolver
activity_regulation
ACTIVITY REGULATION: Affinity and transport activity are regulated by a phosphorylation switch state at Ser-274 and Ser-297; increasing of affinity and amino acid transport activity via dephosphorylation at Ser-274 and phosphorylation at Ser-297. {ECO:0000269|PubMed:30379325}.
uniprot
proteins
amino_acid_sequence
MAPTLATAHRRRWWMACTAVLENLLFSAVLLGWGSLLIMLKSEGFYSYLCTEPENVTNGTVGGTAEPGHEEVSWMNGWLSCQAQDEMLNLAFTVGSFLLSAITLPLGIVMDKYGPRKLRLLGSACFAVSCLLIAYGASKPNALSVLIFIALALNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPGIKLIYDAGVSFIVVLVVWAGCSGLVFLNCFFNWPLEPFPGPEDMDYSVKIKFSWLGFDHKITGKQFYKQVTTVGRRLSVGSSMRSAKEQVALQEGHKLCLSTVDLEVKCQPDAAVAPSFMHSVFSPILLLSLVTMCVTQLRLIFYMGAMNNILKFLVSGDQKTVGLYTSIFGVLQLLCLLTAPVIGYIMDWRLKECEDASEEPEEKDANQGEKKKKKRDRQIQKITNAMRAFAFTNLLLVGFGVTCLIPNLPLQILSFILHTIVRGFIHSAVGGLYAAVYPSTQFGSLTGLQSLISALFALLQQPLFLAMMGPLQGDPLWVNVGLLLLSLLGFCLPLYLICYRRQLERQLQQRQEDDKLFLKINGSSNQEAFV
uniprot
proteins
function
FUNCTION: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine (PubMed:15659399, PubMed:30379325, PubMed:26305885). The transport activity is mediated through facilitated diffusion and is sodium ions-, chloride ions- and pH-independent (PubMed:15659399) Mediates the efflux of 3,3'-diiodo-L-thyronine (3,3'-T2) and 3-iodo-L-tyrosine (MIT) (PubMed:26305885). {ECO:0000269|PubMed:15659399, ECO:0000269|PubMed:26305885, ECO:0000269|PubMed:30379325}.
uniprot
proteins
mass_dalton
62747
uniprot
proteins
mutagenesis
MUTAGEN 274; /note="S->A: Increases affinity for phenylalanine. Increases phenylalanine transport activity. Strongly decreases glycosylation. Strongly decreases expression. Increases membrane localization."; /evidence="ECO:0000269|PubMed:30379325"; MUTAGEN 274; /note="S->E: Slightly decreases phenylalanine transport. Does not affect membrane localization."; /evidence="ECO:0000269|PubMed:30379325"; MUTAGEN 278; /note="S->A: Increases affinity for phenylalanine."; /evidence="ECO:0000269|PubMed:30379325"; MUTAGEN 278; /note="S->E: Slightly decreases phenylalanine transport."; /evidence="ECO:0000269|PubMed:30379325"; MUTAGEN 297; /note="S->A: Abolishes sensitivity to N-ethymaleimide. Severely decreases phenylalanine transport activity. Decreases affinity for phenylalanine. Strongly decreases glycosylation. Strongly decreases expression. Reduces membrane localization."; /evidence="ECO:0000269|PubMed:15659399, ECO:0000269|PubMed:30379325"; MUTAGEN 297; /note="S->E: Slightly decreases phenylalanine transport. Does not affect membrane localization."; /evidence="ECO:0000269|PubMed:30379325
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:30379325}.; PTM: Dephosphorylation at Ser-274 and phosphorylation at Ser-297 increase affinity and amino acid transport activity (PubMed:30379325). Phosphorylation-dephosphorylation cycle is regulated by food-entrained diurnal rhythm and dietary proteins (By similarity). {ECO:0000250|UniProtKB:Q8CGA3, ECO:0000269|PubMed:30379325}.
uniprot
proteins
protein_family
SLC43A transporter (TC 2.A.1.44) family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
15659399
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26305885
uniprot
proteins
pubmed
30379325
uniprot
proteins
sequence_length
569
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30379325}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8CGA3}. Note=Located at the basolateral membrane in the small intestine enterocytes, kidney proximal tubule, thick ascending limb and, to a minor extent, of distal convoluted tubule epithelial cells. {ECO:0000250|UniProtKB:Q8CGA3}.
uniprot
proteins
transmembrane_region
TRANSMEM 20..40; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 90..110; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 120..140; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 143..163; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 177..197; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 203..223; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 323..345; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 365..385; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 435..455; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 462..482; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 490..510; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 516..536; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins