STAR3_DANRE
ID STAR3_DANRE Reviewed; 448 AA.
AC Q9DFS4; Q6PH03;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=StAR-related lipid transfer protein 3 {ECO:0000305};
DE AltName: Full=MLN64-like protein {ECO:0000250|UniProtKB:Q14849};
DE AltName: Full=START domain-containing protein 3 {ECO:0000250|UniProtKB:Q14849};
DE Short=StARD3 {ECO:0000250|UniProtKB:Q14849};
GN Name=stard3 {ECO:0000250|UniProtKB:Q14849};
GN Synonyms=mln64 {ECO:0000250|UniProtKB:Q14849};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 210-448.
RX PubMed=11064158; DOI=10.1016/s0303-7207(00)00316-6;
RA Bauer M.P., Bridgham J.T., Langenau D.M., Johnson A.L., Goetz F.W.;
RT "Conservation of steroidogenic acute regulatory (StAR) protein structure
RT and expression in vertebrates.";
RL Mol. Cell. Endocrinol. 168:119-125(2000).
CC -!- FUNCTION: Sterol-binding protein that mediates cholesterol transport
CC from the endoplasmic reticulum to endosomes. Creates contact site
CC between the endoplasmic reticulum and late endosomes: localizes to late
CC endosome membranes and contacts the endoplasmic reticulum. 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. {ECO:0000250|UniProtKB:Q14849}.
CC -!- SUBUNIT: Homodimer. {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 and VAPB.
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.
CC {ECO:0000250|UniProtKB:Q14849}.
CC -!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
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DR EMBL; BC056766; AAH56766.1; -; mRNA.
DR EMBL; AF258786; AAG28603.1; -; mRNA.
DR RefSeq; NP_571737.1; NM_131662.1.
DR RefSeq; XP_005159410.1; XM_005159353.3.
DR AlphaFoldDB; Q9DFS4; -.
DR SMR; Q9DFS4; -.
DR STRING; 7955.ENSDARP00000007948; -.
DR PaxDb; Q9DFS4; -.
DR PRIDE; Q9DFS4; -.
DR Ensembl; ENSDART00000003634; ENSDARP00000007948; ENSDARG00000017809.
DR GeneID; 63998; -.
DR KEGG; dre:63998; -.
DR CTD; 10948; -.
DR ZFIN; ZDB-GENE-001120-2; stard3.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000159051; -.
DR HOGENOM; CLU_033480_1_0_1; -.
DR InParanoid; Q9DFS4; -.
DR OMA; NQMGLDC; -.
DR OrthoDB; 1437203at2759; -.
DR PhylomeDB; Q9DFS4; -.
DR TreeFam; TF313869; -.
DR Reactome; R-DRE-196108; Pregnenolone biosynthesis.
DR PRO; PR:Q9DFS4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000017809; Expressed in mature ovarian follicle and 28 other tissues.
DR ExpressionAtlas; Q9DFS4; baseline and differential.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
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: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 2: Evidence at transcript level;
KW Endosome; Lipid transport; Lipid-binding; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..448
FT /note="StAR-related lipid transfer protein 3"
FT /id="PRO_0000220655"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT DOMAIN 47..219
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT DOMAIN 232..445
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT MOTIF 209..214
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
FT CONFLICT 210..220
FT /note="YSPPESLAGSE -> PGRPRVRPRVR (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 50751 MW; 716A18C127B59C5D CRC64;
MPSAVDYSEL GGSLPAIASL NASYSQASLS LPSPYYCPLP PGERKAFSDV RRTFCLFVTF
DLLFITLLWI IELNISKSIW NSLENEVVHY NFKSSFFDIF LLAVFRFLCL QLGYAAFRLR
HWWVIAITTL VTTAFLIAKV ILSDLFSQNA FGYVLPITSF VVAWLETWFL DFKVLTQEAE
DERVYLAAVN AACEPAPLIC PRPVSDGQFY SPPESLAGSE DDLDEEGLGR RAVTEQEKAF
VRQGREAMAV VEQILTQEEN WKFEKTNELG DAVYTLEIPF HGKTFILKGL LQCTAELVYQ
EVILQPEKMV QWNRTVSVCQ ILQRVDDNTM VSYDVSAGAA GGVVSPRDFV NVRRVERRRD
CYISAGMATN HNSKPHHSRY VRGENGPGGF VVLKSSSNPS VCTFIWVLNT DLKGRLPRYL
IHQSLAATMF EFMSHLRQRI NEVHVSYR
