STAR4_MOUSE
ID STAR4_MOUSE Reviewed; 224 AA.
AC Q99JV5;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=StAR-related lipid transfer protein 4;
DE AltName: Full=START domain-containing protein 4;
DE Short=StARD4;
GN Name=Stard4;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J, and FVB/NJ; TISSUE=Liver;
RX PubMed=12011452; DOI=10.1073/pnas.052143799;
RA Soccio R.E., Adams R.M., Romanowski M.J., Sehayek E., Burley S.K.,
RA Breslow J.L.;
RT "The cholesterol-regulated StarD4 gene encodes a StAR-related lipid
RT transfer protein with two closely related homologues, StarD5 and StarD6.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6943-6948(2002).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12011453; DOI=10.1073/pnas.052140699;
RA Romanowski M.J., Soccio R.E., Breslow J.L., Burley S.K.;
RT "Crystal structure of the Mus musculus cholesterol-regulated START protein
RT 4 (StarD4) containing a StAR-related lipid transfer domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6949-6954(2002).
CC -!- FUNCTION: Involved in the intracellular transport of cholesterol. Binds
CC cholesterol or other sterols. {ECO:0000250|UniProtKB:Q96DR4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:Q96DR4};
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, with highest levels in
CC liver and in kidney. {ECO:0000269|PubMed:12011452}.
CC -!- INDUCTION: Down-regulated by dietary cholesterol.
CC {ECO:0000269|PubMed:12011452}.
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DR EMBL; AF480298; AAL87128.1; -; mRNA.
DR EMBL; AF480297; AAL87127.1; -; mRNA.
DR EMBL; BC005642; AAH05642.1; -; mRNA.
DR CCDS; CCDS29123.1; -.
DR RefSeq; NP_598535.1; NM_133774.5.
DR PDB; 1JSS; X-ray; 2.20 A; A/B=1-224.
DR PDB; 5BRL; X-ray; 2.00 A; A/B=13-222.
DR PDBsum; 1JSS; -.
DR PDBsum; 5BRL; -.
DR AlphaFoldDB; Q99JV5; -.
DR BMRB; Q99JV5; -.
DR SMR; Q99JV5; -.
DR STRING; 10090.ENSMUSP00000025236; -.
DR iPTMnet; Q99JV5; -.
DR PhosphoSitePlus; Q99JV5; -.
DR EPD; Q99JV5; -.
DR MaxQB; Q99JV5; -.
DR PaxDb; Q99JV5; -.
DR PRIDE; Q99JV5; -.
DR ProteomicsDB; 257449; -.
DR DNASU; 170459; -.
DR GeneID; 170459; -.
DR KEGG; mmu:170459; -.
DR CTD; 134429; -.
DR MGI; MGI:2156764; Stard4.
DR eggNOG; KOG3845; Eukaryota.
DR InParanoid; Q99JV5; -.
DR OrthoDB; 1469639at2759; -.
DR PhylomeDB; Q99JV5; -.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR BioGRID-ORCS; 170459; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Stard4; mouse.
DR EvolutionaryTrace; Q99JV5; -.
DR PRO; PR:Q99JV5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99JV5; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:CACAO.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005739; C:mitochondrion; TAS:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISA:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:MGI.
DR GO; GO:0034435; P:cholesterol esterification; IDA:CACAO.
DR GO; GO:0070508; P:cholesterol import; ISO:MGI.
DR GO; GO:0010879; P:cholesterol transport involved in cholesterol storage; ISO:MGI.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
DR GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; ISO:MGI.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR042555; StarD4.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR47006; PTHR47006; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid transport; Lipid-binding; Reference proteome;
KW Transport.
FT CHAIN 1..224
FT /note="StAR-related lipid transfer protein 4"
FT /id="PRO_0000220668"
FT DOMAIN 16..224
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT VARIANT 41
FT /note="K -> E (in strain: C57BL/6)"
FT VARIANT 51
FT /note="V -> A (in strain: C57BL/6)"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:5BRL"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 62..77
FT /evidence="ECO:0007829|PDB:5BRL"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5BRL"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:5BRL"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1JSS"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:5BRL"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:5BRL"
FT HELIX 199..221
FT /evidence="ECO:0007829|PDB:5BRL"
SQ SEQUENCE 224 AA; 25579 MW; 104B7D3052EEF064 CRC64;
MADPESPWSQ IGRKIKLEGL SDVASISTKL QNTLIQYHSI KEDEWRVAKK VKDVTVWRKP
SEEFNGYLYK AQGVMDDVVN NVIDHIRPGP WRLDWDRLMT SLDVLEHFEE NCCVMRYTTA
GQLLNIISPR EFVDFSYTVG YEEGLLSCGV SVEWSETRPE FVRGYNHPCG WFCVPLKDSP
SQSLLTGYIQ TDLRGMIPQS AVDTAMASTL ANFYSDLRKG LRKA
