Stard3
entrez
59045
canonical
uniprot
Q61542
canonical
ensembl
ENSMUSG00000018167
resolver
ensp
ENSMUSP00000018311
resolver
ensp
ENSMUSP00000318381
resolver
ensp
ENSMUSP00000318402
resolver
enst
ENSMUST00000018311
resolver
genesymbol
Stard3
resolver
genesymbol_syn
Es64
resolver
genesymbol_syn
Mln64
resolver
uniprot
Q544C3
resolver
uniprot_entry
Q544C3_MOUSE
resolver
uniprot_entry
STAR3_MOUSE
resolver
amino_acid_sequence
MSKRPGDLACDLERSLPALASLGTSLSHSQSLSSHFIPPPLEKRRAISDVRRTFCLFVTFDLLFISLLWIIELNTNTGIRKNLEQEVIHYSFQSSFFDIFVLAFFRFSGLLLGYAVLRLQHWWVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAAQAAVARGPLLFSGALSEGQFYSPPESFAGSDNESDEEVTGKKSFSAQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGARA
uniprot
proteins
function
FUNCTION: Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes. The sterol transport mechanism is triggered by phosphorylation of FFAT motif that leads to membrane tethering between the endoplasmic reticulum and late endosomes via interaction with VAPA and VAPB. Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes. May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane. However, such results need additional experimental evidence; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes. Does not activate transcriptional cholesterol sensing. Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina. {ECO:0000250|UniProtKB:Q14849}.
uniprot
proteins
mass_dalton
50470
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-210 is necessary and sufficient for the direct interaction of the phosphorylated FFAT motif with the MSP domain of MOSPD2, VAPA and VAPB and allows the tethering of two membranes that participates in the formation of ER-endosome contacts. Phosphorylation of the FFAT motif leads to conformation changes. Additional phosphorylations around the core FFAT motif (QFYSPPE) are not essential but strengthen the interaction with MOSPD2, VAPA and VAPB. Phosphorylation at Ser-210 of FFAT motif drives membrane tethering between the endoplasmic reticulum and late endosomes via interaction with VAPA and VAPB that in turn allows the efficient transport of sterol mediated by the START domain. {ECO:0000250|UniProtKB:Q14849}.
uniprot
proteins
protein_family
STARD3 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7490069
uniprot
proteins
sequence_length
446
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q14849}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2. {ECO:0000250|UniProtKB:Q14849}.
uniprot
proteins
transmembrane_region
TRANSMEM 53..73; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"; TRANSMEM 96..116; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"; TRANSMEM 122..142; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"; TRANSMEM 150..170; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770
uniprot
proteins