Stra6
entrez
20897
canonical
uniprot
O70491
canonical
ensembl
ENSMUSG00000032327
resolver
ensp
ENSMUSP00000034880
resolver
ensp
ENSMUSP00000082820
resolver
ensp
ENSMUSP00000128417
resolver
ensp
ENSMUSP00000130232
resolver
ensp
ENSMUSP00000196362
resolver
ensp
ENSMUSP00000196365
resolver
ensp
ENSMUSP00000196366
resolver
enst
ENSMUST00000034880
resolver
enst
ENSMUST00000085677
resolver
enst
ENSMUST00000167479
resolver
enst
ENSMUST00000170397
resolver
genesymbol
Stra6
resolver
uniprot
A0A0R4J115
resolver
uniprot
Q6DIA8
resolver
uniprot_entry
A0A0R4J115_MOUSE
resolver
uniprot_entry
STRA6_MOUSE
resolver
uniprot_sec
Q6DIA8
resolver
amino_acid_sequence
MESQASENGSQTSSGVTDDYSSWYIEEPLGAEEVQPEGVIPLCQLTAPPALLHACLASLSFLVLLLLALLVRRRRLWPRCGHRGLGLPSPVDFLAGDLSWTVPAAVFVVLFSNLCLLLPDENPLPFLNLTAASSPDGEMETSRGPWKLLALLYYPALYYPLAACASAGHQAAFLLGTVLSWAHFGVQVWQKAECPQDPKIYKHYSLLASLPLLLGLGFLSLWYPVQLVQSLRHRTGAGSQGLQTSYSEKYLRTLLCPKKLDSCSHPASKRSLLSRAWAFSHHSIYTPQPGFRLPLKLVISATLTGTATYQVALLLLVSVVPTVQKVRAGINTDVSYLLAGFGIVLSEDRQEVVELVKHHLWTVEACYISALVLSCASTFLLLIRSLRTHRANLQALHRGAALDLDPPLQSIHPSRQAIVSWMSFCAYQTAFSCLGLLVQQVIFFLGTTSLAFLVFVPLLHGRNLLLLRSLESTWPFWLTVALAVILQNIAANWIFLRTHHGYPELTNRRMLCVATFLLFPINMLVGAIMAVWRVLISSLYNTVHLGQMDLSLLPQRAASLDPGYHTYQNFLRIEASQSHPGVIAFCALLLHAPSPQPRPPLAPQDSLRPAEEEEGMQLLQTKDLMAKGAGHKGSQSRARWGLAYTLLHNPSLQAFRKAALTSAKANGTQP
uniprot
proteins
function
FUNCTION: Functions as a retinol transporter (PubMed:23839944, PubMed:24852372). Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A (By similarity). Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin (PubMed:21368206, PubMed:23839944). Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid and 11-cis-retinal (PubMed:22467576, PubMed:24852372). STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency (PubMed:22467576, PubMed:23839944, PubMed:24852372). Does not transport retinoic acid (By similarity). {ECO:0000250|UniProtKB:Q9BX79, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:23839944, ECO:0000269|PubMed:24852372}.
uniprot
proteins
mass_dalton
73775
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues in response to RBP4 binding (PubMed:21368206). Phosphorylation requires the presence of LRAT, suggesting it may be triggered by the uptake of retinol that is then metabolized within the cell to retinoids that function as signaling molecules (By similarity). {ECO:0000250|UniProtKB:Q9BX79, ECO:0000269|PubMed:21368206}.
uniprot
proteins
pubmed
10727869
uniprot
proteins
pubmed
11358845
uniprot
proteins
pubmed
11832495
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21368206
uniprot
proteins
pubmed
22467576
uniprot
proteins
pubmed
23839944
uniprot
proteins
pubmed
24852372
uniprot
proteins
pubmed
7644503
uniprot
proteins
pubmed
8792610
uniprot
proteins
pubmed
9203140
uniprot
proteins
sequence_length
670
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9203140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the retinal pigment epithelium localizes to the basolateral membrane (PubMed:22467576, PubMed:24852372). Plasma membrane of the basal pole of Sertoli cells, absent in plasma membrane of neighboring spermatogonia (PubMed:9203140). {ECO:0000250|UniProtKB:Q0V8E7, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:9203140}.
uniprot
proteins
transmembrane_region
TRANSMEM 51..71; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 98..118; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 145..165; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 169..189; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 206..226; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 297..317; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 369..389; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 424..444; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4"; TRANSMEM 475..495; /note="Helical"; /evidence="ECO:0000250|UniProtKB:F1RAX4
uniprot
proteins