STAR3_MOUSE
ID STAR3_MOUSE Reviewed; 446 AA.
AC Q61542;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=StAR-related lipid transfer protein 3 {ECO:0000305};
DE AltName: Full=Protein ES 64 {ECO:0000312|MGI:MGI:1929618};
DE AltName: Full=Protein MLN 64 {ECO:0000250|UniProtKB:Q14849};
DE AltName: Full=START domain-containing protein 3 {ECO:0000312|MGI:MGI:1929618};
DE Short=StARD3 {ECO:0000312|MGI:MGI:1929618};
GN Name=Stard3 {ECO:0000312|MGI:MGI:1929618};
GN Synonyms=Es64 {ECO:0000312|MGI:MGI:1929618},
GN Mln64 {ECO:0000250|UniProtKB:Q14849};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7490069; DOI=10.1006/geno.1995.1163;
RA Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P.,
RA Lidereau R., Basset P., Rio M.-C.;
RT "Identification of four novel human genes amplified and overexpressed in
RT breast carcinoma and localized to the q11-q21.3 region of chromosome 17.";
RL Genomics 28:367-376(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-218 AND SER-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Sterol-binding protein that mediates cholesterol transport
CC from the endoplasmic reticulum to endosomes (By similarity). Creates
CC contact site between the endoplasmic reticulum and late endosomes:
CC localizes to late endosome membranes and contacts the endoplasmic
CC reticulum via interaction with VAPA and VAPB (By similarity). Acts as a
CC lipid transfer protein that redirects sterol to the endosome at the
CC expense of the cell membrane and favors membrane formation inside
CC endosomes (By similarity). May also mediate cholesterol transport
CC between other membranes, such as mitochondria membrane or cell membrane
CC (By similarity). However, such results need additional experimental
CC evidences; probably mainly mediates cholesterol transport from the
CC endoplasmic reticulum to endosomes (By similarity). Does not activate
CC transcriptional cholesterol sensing (By similarity).
CC {ECO:0000250|UniProtKB:F7B909, ECO:0000250|UniProtKB:Q14849}.
CC -!- SUBUNIT: Homodimer. Interacts (via the MENTAL domain) with STARD3NL.
CC Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with
CC VAPB. Interacts (via FFAT motif) with MOSPD2 (via MSP domain).
CC {ECO:0000250|UniProtKB:Q14849}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q14849}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic
CC reticulum and late endosomes: associates with the endoplasmic reticulum
CC membrane via interaction with VAPA, VAPB or MOSPD2.
CC {ECO:0000250|UniProtKB:Q14849}.
CC -!- DOMAIN: The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2.
CC {ECO:0000250|UniProtKB:Q14849}.
CC -!- DOMAIN: The START domain mediates lipid-transfer between membranes. It
CC contains a hydrophobic cavity able to accommodate one lipid molecule,
CC thereby serving as a 'hydrophobic bridge' across the aqueous gap
CC between donor and acceptor organelle membranes.
CC {ECO:0000250|UniProtKB:Q14849}.
CC -!- DOMAIN: The MENTAL domain anchors the protein in endosome membranes and
CC exposes the START domain in the cytosol. It binds cholesterol and
CC mediates homotypic as well as heterotypic interactions between STARD3
CC and STARD3NL. {ECO:0000250|UniProtKB:Q14849}.
CC -!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
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DR EMBL; X82457; CAA57834.1; -; mRNA.
DR EMBL; BC003313; AAH03313.1; -; mRNA.
DR CCDS; CCDS25345.1; -.
DR RefSeq; NP_067522.1; NM_021547.3.
DR RefSeq; XP_006533959.1; XM_006533896.3.
DR AlphaFoldDB; Q61542; -.
DR SMR; Q61542; -.
DR BioGRID; 208509; 1.
DR STRING; 10090.ENSMUSP00000018311; -.
DR ChEMBL; CHEMBL4523333; -.
DR iPTMnet; Q61542; -.
DR PhosphoSitePlus; Q61542; -.
DR EPD; Q61542; -.
DR MaxQB; Q61542; -.
DR PaxDb; Q61542; -.
DR PRIDE; Q61542; -.
DR ProteomicsDB; 257448; -.
DR Antibodypedia; 28306; 80 antibodies from 22 providers.
DR DNASU; 59045; -.
DR Ensembl; ENSMUST00000018311; ENSMUSP00000018311; ENSMUSG00000018167.
DR GeneID; 59045; -.
DR KEGG; mmu:59045; -.
DR UCSC; uc007lgc.2; mouse.
DR CTD; 10948; -.
DR MGI; MGI:1929618; Stard3.
DR VEuPathDB; HostDB:ENSMUSG00000018167; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000159051; -.
DR HOGENOM; CLU_033480_0_0_1; -.
DR InParanoid; Q61542; -.
DR OMA; NQMGLDC; -.
DR OrthoDB; 1437203at2759; -.
DR PhylomeDB; Q61542; -.
DR TreeFam; TF313869; -.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR BioGRID-ORCS; 59045; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Stard3; mouse.
DR PRO; PR:Q61542; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61542; protein.
DR Bgee; ENSMUSG00000018167; Expressed in granulocyte and 256 other tissues.
DR ExpressionAtlas; Q61542; baseline and differential.
DR Genevisible; Q61542; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; TAS:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; ISS:UniProtKB.
DR GO; GO:0006701; P:progesterone biosynthetic process; IMP:MGI.
DR GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; ISS:UniProtKB.
DR CDD; cd08906; START_STARD3-like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR019498; MENTAL.
DR InterPro; IPR000799; StAR-like.
DR InterPro; IPR029867; STARD3_MLN64_C.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF10457; MENTAL; 1.
DR Pfam; PF01852; START; 1.
DR PRINTS; PR00978; STARPROTEIN.
DR SMART; SM00234; START; 1.
DR PROSITE; PS51439; MENTAL; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Endosome; Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..446
FT /note="StAR-related lipid transfer protein 3"
FT /id="PRO_0000220654"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 74..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 117..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 143..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 171..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
FT DOMAIN 47..218
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT DOMAIN 231..444
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT MOTIF 208..213
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ 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
