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StAR-related lipid transfer protein 3 (Protein ES 64) (Protein MLN 64) (START domain-containing protein 3) (StARD3)

 STAR3_MOUSE             Reviewed;         446 AA.
Q61542;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=StAR-related lipid transfer protein 3 {ECO:0000305};
AltName: Full=Protein ES 64 {ECO:0000312|MGI:MGI:1929618};
AltName: Full=Protein MLN 64 {ECO:0000250|UniProtKB:Q14849};
AltName: Full=START domain-containing protein 3 {ECO:0000312|MGI:MGI:1929618};
Short=StARD3 {ECO:0000312|MGI:MGI:1929618};
Name=Stard3 {ECO:0000312|MGI:MGI:1929618};
Synonyms=Es64 {ECO:0000312|MGI:MGI:1929618},
Mln64 {ECO:0000250|UniProtKB:Q14849};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7490069; DOI=10.1006/geno.1995.1163;
Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G.,
Chenard M.-P., Lidereau R., Basset P., Rio M.-C.;
"Identification of four novel human genes amplified and overexpressed
in breast carcinoma and localized to the q11-q21.3 region of
chromosome 17.";
Genomics 28:367-376(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-218 AND
SER-222, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Sterol-binding protein that mediates cholesterol
transport from the endoplasmic reticulum to endosomes (By
similarity). Creates contact site between the endoplasmic
reticulum and late endosomes: localizes to late endosome membranes
and contacts the endoplasmic reticulum via interaction with VAPA
and VAPB (By similarity). 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 (By
similarity). May also mediate cholesterol transport between other
membranes, such as mitochondria membrane or cell membrane (By
similarity). However, such results need additional experimental
evidences; probably mainly mediates cholesterol transport from the
endoplasmic reticulum to endosomes (By similarity). Does not
activate transcriptional cholesterol sensing (By similarity).
{ECO:0000250|UniProtKB:F7B909, ECO:0000250|UniProtKB:Q14849}.
-!- SUBUNIT: Homodimer. Interacts (via the MENTAL domain) with
STARD3NL. Interacts (via FFAT motif) with VAPA. Interacts (via
FFAT motif) with VAPB. {ECO:0000250|UniProtKB:Q14849}.
-!- 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 and VAPB.
{ECO:0000250|UniProtKB:Q14849}.
-!- DOMAIN: The FFAT motif mediates interaction with VAPA and VAPB.
{ECO:0000250|UniProtKB:Q14849}.
-!- DOMAIN: The START domain mediates lipid-transfer between
membranes. It contains a hydrophobic cavity able to accommodate
one lipid molecule, thereby serving as a 'hydrophobic bridge'
across the aqueous gap between donor and acceptor organelle
membranes. {ECO:0000250|UniProtKB:Q14849}.
-!- DOMAIN: The MENTAL domain anchors the protein in endosome
membranes and exposes the START domain in the cytosol. It binds
cholesterol and mediates homotypic as well as heterotypic
interactions between STARD3 and STARD3NL.
{ECO:0000250|UniProtKB:Q14849}.
-!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X82457; CAA57834.1; -; mRNA.
EMBL; BC003313; AAH03313.1; -; mRNA.
CCDS; CCDS25345.1; -.
RefSeq; NP_067522.1; NM_021547.3.
RefSeq; XP_006533959.1; XM_006533896.3.
UniGene; Mm.265546; -.
UniGene; Mm.489827; -.
ProteinModelPortal; Q61542; -.
SMR; Q61542; -.
STRING; 10090.ENSMUSP00000018311; -.
iPTMnet; Q61542; -.
PhosphoSitePlus; Q61542; -.
EPD; Q61542; -.
MaxQB; Q61542; -.
PaxDb; Q61542; -.
PRIDE; Q61542; -.
Ensembl; ENSMUST00000018311; ENSMUSP00000018311; ENSMUSG00000018167.
GeneID; 59045; -.
KEGG; mmu:59045; -.
UCSC; uc007lgc.2; mouse.
CTD; 10948; -.
MGI; MGI:1929618; Stard3.
eggNOG; KOG3845; Eukaryota.
eggNOG; ENOG41100B5; LUCA.
GeneTree; ENSGT00530000063139; -.
HOGENOM; HOG000015362; -.
HOVERGEN; HBG052482; -.
InParanoid; Q61542; -.
OMA; FHLRQRI; -.
OrthoDB; EOG091G06RM; -.
PhylomeDB; Q61542; -.
TreeFam; TF313869; -.
Reactome; R-MMU-196108; Pregnenolone biosynthesis.
PRO; PR:Q61542; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018167; -.
CleanEx; MM_STARD3; -.
ExpressionAtlas; Q61542; baseline and differential.
Genevisible; Q61542; MM.
GO; GO:0005737; C:cytoplasm; ISS:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; TAS:MGI.
GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
GO; GO:0017127; F:cholesterol transporter activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030301; P:cholesterol transport; ISS:UniProtKB.
GO; GO:0006701; P:progesterone biosynthetic process; IMP:MGI.
GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; ISS:UniProtKB.
CDD; cd08906; START_STARD3-like; 1.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR019498; MENTAL.
InterPro; IPR000799; StAR-like.
InterPro; IPR029867; STARD3_MLN64_C.
InterPro; IPR023393; START-like_dom_sf.
InterPro; IPR002913; START_lipid-bd_dom.
Pfam; PF10457; MENTAL; 1.
Pfam; PF01852; START; 1.
PRINTS; PR00978; STARPROTEIN.
SMART; SM00234; START; 1.
PROSITE; PS51439; MENTAL; 1.
PROSITE; PS50848; START; 1.
1: Evidence at protein level;
Complete proteome; Endosome; Lipid transport; Lipid-binding; Membrane;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 446 StAR-related lipid transfer protein 3.
/FTId=PRO_0000220654.
TOPO_DOM 1 52 Cytoplasmic.
{ECO:0000250|UniProtKB:Q14849}.
TRANSMEM 53 73 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 74 95 Extracellular. {ECO:0000255}.
TRANSMEM 96 116 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 117 121 Cytoplasmic. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 143 149 Extracellular. {ECO:0000255}.
TRANSMEM 150 170 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 171 446 Cytoplasmic.
{ECO:0000250|UniProtKB:Q14849}.
DOMAIN 47 218 MENTAL. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
DOMAIN 231 444 START. {ECO:0000255|PROSITE-
ProRule:PRU00197}.
MOTIF 208 213 FFAT. {ECO:0000250|UniProtKB:Q14849}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 446 AA; 50470 MW; DBF4359604F3E1E2 CRC64;
MSKRPGDLAC DLERSLPALA SLGTSLSHSQ SLSSHFIPPP LEKRRAISDV RRTFCLFVTF
DLLFISLLWI IELNTNTGIR KNLEQEVIHY SFQSSFFDIF VLAFFRFSGL LLGYAVLRLQ
HWWVIAVTTL VSSAFLIVKV ILSELLSKGA FGYLLPIVSF VLAWLETWFL DFKVLPQEAE
EERWYLAAQA AVARGPLLFS GALSEGQFYS PPESFAGSDN ESDEEVTGKK SFSAQEREYI
RQGKEATAVV DQILAQEENW KFERSNEYGD TVYTIEVPFH GKTFILKTFL PCPAELVYQE
VILQPERMVL WNKTVTACQI LQRVEDNTLV SYDVSSGAAG GVVSPRDFVN VRRIERRRDR
YLSSGIATTH CSKPPTHKYV RGENGPGGFI VLKSANNPRV CTFVWILNTD LKGRLPRYLI
HQSLGATMFE FAFHLRQRVG ELGARA


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