STARD3
entrez
10948
canonical
uniprot
Q14849
canonical
ensembl
ENSG00000131748
resolver
ensp
ENSP00000337446
resolver
ensp
ENSP00000377794
resolver
ensp
ENSP00000439869
resolver
ensp
ENSP00000578933
resolver
ensp
ENSP00000578944
resolver
ensp
ENSP00000578947
resolver
ensp
ENSP00000672142
resolver
ensp
ENSP00000672147
resolver
ensp
ENSP00000726386
resolver
ensp
ENSP00000729924
resolver
genesymbol
STARD3
resolver
genesymbol_syn
CAB1
resolver
genesymbol_syn
MLN64
resolver
hgnc
HGNC:17579
resolver
uniprot
A8MXA4
resolver
uniprot
B4DUY1
resolver
uniprot
F5H0G2
resolver
uniprot
Q53Y53
resolver
uniprot
Q96HM9
resolver
uniprot_entry
STAR3_HUMAN
resolver
uniprot_sec
A8MXA4
resolver
uniprot_sec
B4DUY1
resolver
uniprot_sec
F5H0G2
resolver
uniprot_sec
Q53Y53
resolver
uniprot_sec
Q96HM9
resolver
amino_acid_sequence
MSKLPRELTRDLERSLPAVASLGSSLSHSQSLSSHLLPPPEKRRAISDVRRTFCLFVTFDLLFISLLWIIELNTNTGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLRHWWVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAAQVAVARGPLLFSGALSEGQFYSPPESFAGSDNESDEEVAGKKSFSAQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNPRVCTFVWILNTDLKGRLPRYLIHQSLAATMFEFAFHLRQRISELGARA
uniprot
proteins
function
FUNCTION: Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:11053434, PubMed:15930133, PubMed:22514632, PubMed:28377464, PubMed:33124732). 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 (PubMed:24105263, PubMed:28377464, PubMed:33124732). 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 (PubMed:28377464). May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane (PubMed:12070139, PubMed:19965586). However, such results need additional experimental evidence; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:28377464). Does not activate transcriptional cholesterol sensing (PubMed:28377464). Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina (PubMed:21322544). {ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:12070139, ECO:0000269|PubMed:15930133, ECO:0000269|PubMed:19965586, ECO:0000269|PubMed:21322544, ECO:0000269|PubMed:22514632, ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464, ECO:0000269|PubMed:33124732}.
uniprot
proteins
mass_dalton
50502
uniprot
proteins
mutagenesis
MUTAGEN 66..67; /note="LL->AS: Abolishes localization to late endosomes and leads to mislocalization to the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:11053434"; MUTAGEN 89; /note="Y->V: Abolishes localization to late endosomes and leads to mislocalization to the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:11053434"; MUTAGEN 113; /note="Y->A: Does not affect localization to late endosomes."; /evidence="ECO:0000269|PubMed:11053434"; MUTAGEN 206..212; /note="Missing: Abolishes interaction with VAPA and VAPB, thereby preventing contact with the endoplasmic reticulum membrane."; /evidence="ECO:0000269|PubMed:24105263"; MUTAGEN 207..208; /note="FY->AA: Abolishes interaction with VAPA, VAPB and MOSPD2, thereby preventing contact with the endoplasmic reticulum membrane. Abolishes cholesterol accumulation in endosomes."; /evidence="ECO:0000269|PubMed:28377464, ECO:0000269|PubMed:29858488"; MUTAGEN 209; /note="S->A: Impairs VAPA and VAPB interaction. Does not affect endoplasmic reticulum membrane location of VAPA, VAPB and MOSPD2. Is unable to make ER-endosome contacts. Does not accumulate cholesterol in late endosomes (LEs). Does not interact with MOSPD2."; /evidence="ECO:0000269|PubMed:33124732"; MUTAGEN 209; /note="S->D: Does not affect VAPA and VAPB interactions; when associated with A-210. Does not interact with VAPA and VAPB. Recruits VAPA and VAPB around the endosome; when associated with A-210. Restores cholesterol accumulation in late endosomes; when associated with A-210. Moderately interacts with MOSPD2. Almost impairs interaction with MOSPD2; when associated with A-210."; /evidence="ECO:0000269|PubMed:33124732"; MUTAGEN 210; /note="P->A: Does not affect VAPA and VAPB interactions; when associated with D-209. Improve VAPA interaction. Does not interact with VAPA and VAPB. Recruits VAPA and VAPB around the endosome; when associated with D-209. Restores cholesterol accumulation in late endosomes; when associated with A-209. Almost impairs interaction with MOSPD2; when associated with A-209."; /evidence="ECO:0000269|PubMed:33124732"; MUTAGEN 219; /note="N->A: Does not affect localization to late endosomes."; /evidence="ECO:0000269|PubMed:11053434"; MUTAGEN 307..311; /note="MVLWN->NVLWD: Abolishes ability to transfer cholesterol between membranes."; /evidence="ECO:0000269|PubMed:28377464"; MUTAGEN 311; /note="N->A: Does not affect localization to late endosomes."; /evidence="ECO:0000269|PubMed:11053434
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-209 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 (PubMed:33124732). Phosphorylation of the FFAT motif leads to conformation changes (PubMed:33124732). Additional phosphorylations around the core FFAT motif (QFYSPPE) are not essential but strengthen the interaction with MOSPD2, VAPA and VAPB (PubMed:33124732). Phosphorylation at Ser-209 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 (PubMed:33124732). {ECO:0000269|PubMed:33124732}.
uniprot
proteins
protein_family
STARD3 family
uniprot
proteins
pubmed
10802740
uniprot
proteins
pubmed
11053434
uniprot
proteins
pubmed
12070139
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15718238
uniprot
proteins
pubmed
15930133
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16709157
uniprot
proteins
pubmed
16990645
uniprot
proteins
pubmed
19965586
uniprot
proteins
pubmed
21322544
uniprot
proteins
pubmed
22514632
uniprot
proteins
pubmed
24105263
uniprot
proteins
pubmed
27487925
uniprot
proteins
pubmed
27679500
uniprot
proteins
pubmed
28377464
uniprot
proteins
pubmed
29858488
uniprot
proteins
pubmed
33124732
uniprot
proteins
pubmed
7490069
uniprot
proteins
pubmed
9270027
uniprot
proteins
sequence_length
445
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:16709157, ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464, ECO:0000269|PubMed:29858488}; 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:0000269|PubMed:24105263, ECO:0000269|PubMed:29858488}.
uniprot
proteins
transmembrane_region
TRANSMEM 52..72; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"; TRANSMEM 95..115; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"; TRANSMEM 121..141; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"; TRANSMEM 149..169; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00770
uniprot
proteins