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StAR-related lipid transfer protein 3 (Metastatic lymph node gene 64 protein) (MLN 64) (Protein CAB1) (START domain-containing protein 3) (StARD3)

 STAR3_HUMAN             Reviewed;         445 AA.
Q14849; A8MXA4; B4DUY1; F5H0G2; Q53Y53; Q96HM9;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 172.
RecName: Full=StAR-related lipid transfer protein 3 {ECO:0000305};
AltName: Full=Metastatic lymph node gene 64 protein {ECO:0000303|PubMed:11053434};
Short=MLN 64 {ECO:0000303|PubMed:11053434};
AltName: Full=Protein CAB1 {ECO:0000303|PubMed:9270027};
AltName: Full=START domain-containing protein 3 {ECO:0000303|PubMed:21322544};
Short=StARD3 {ECO:0000303|PubMed:21322544};
Name=STARD3 {ECO:0000312|HGNC:HGNC:17579};
Synonyms=CAB1 {ECO:0000303|PubMed:9270027},
MLN64 {ECO:0000303|PubMed:11053434};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-117.
TISSUE=Mammary carcinoma;
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 [MRNA] (ISOFORM 1), AND VARIANT GLN-117.
TISSUE=Esophageal carcinoma;
PubMed=9270027;
Akiyama N., Sasaki H., Ishizuka T., Kishi T., Sakamoto H., Onda M.,
Hirai H., Yazaki Y., Sugimura T., Terada M.;
"Isolation of a candidate gene, CAB1, for cholesterol transport to
mitochondria from the c-ERBB-2 amplicon by a modified cDNA selection
method.";
Cancer Res. 57:3548-3553(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-117.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
GLN-117.
TISSUE=Placenta, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLN-117 AND ALA-216.
TISSUE=Lung, Skin, and Spleen;
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).
[7]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF
66-LEU-LEU-67; TYR-89; TYR-113; ASN-219 AND ASN-311.
PubMed=11053434; DOI=10.1074/jbc.M006279200;
Alpy F., Stoeckel M.-E., Dierich A., Escola J.-M., Wendling C.,
Chenard M.-P., Vanier M.T., Gruenberg J., Tomasetto C., Rio M.-C.;
"The steroidogenic acute regulatory protein homolog MLN64, a late
endosomal cholesterol-binding protein.";
J. Biol. Chem. 276:4261-4269(2001).
[8]
FUNCTION.
PubMed=12070139; DOI=10.1074/jbc.M200003200;
Zhang M., Liu P., Dwyer N.K., Christenson L.K., Fujimoto T.,
Martinez F., Comly M., Hanover J.A., Blanchette-Mackie E.J.,
Strauss J.F. III;
"MLN64 mediates mobilization of lysosomal cholesterol to steroidogenic
mitochondria.";
J. Biol. Chem. 277:33300-33310(2002).
[9]
SUBUNIT, INTERACTION WITH STARD3NL, AND DOMAIN.
PubMed=15718238; DOI=10.1074/jbc.M500723200;
Alpy F., Latchumanan V.K., Kedinger V., Janoshazi A., Thiele C.,
Wendling C., Rio M.C., Tomasetto C.;
"Functional characterization of the MENTAL domain.";
J. Biol. Chem. 280:17945-17952(2005).
[10]
FUNCTION.
PubMed=15930133; DOI=10.1091/mbc.E04-12-1105;
Hoelttae-Vuori M., Alpy F., Tanhuanpaeae K., Jokitalo E., Mutka A.L.,
Ikonen E.;
"MLN64 is involved in actin-mediated dynamics of late endocytic
organelles.";
Mol. Biol. Cell 16:3873-3886(2005).
[11]
SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH STARD3NL, AND DOMAIN.
PubMed=16709157; DOI=10.1042/BST0340343;
Alpy F., Tomasetto C.;
"MLN64 and MENTHO, two mediators of endosomal cholesterol transport.";
Biochem. Soc. Trans. 34:343-345(2006).
[12]
3D-STRUCTURE MODELING.
PubMed=16990645; DOI=10.1194/jlr.M600232-JLR200;
Murcia M., Faraldo-Gomez J.D., Maxfield F.R., Roux B.;
"Modeling the structure of the StART domains of MLN64 and StAR
proteins in complex with cholesterol.";
J. Lipid Res. 47:2614-2630(2006).
[13]
FUNCTION.
PubMed=19965586; DOI=10.1194/jlr.M002345;
Charman M., Kennedy B.E., Osborne N., Karten B.;
"MLN64 mediates egress of cholesterol from endosomes to mitochondria
in the absence of functional Niemann-Pick Type C1 protein.";
J. Lipid Res. 51:1023-1034(2010).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21322544; DOI=10.1021/bi101906y;
Li B., Vachali P., Frederick J.M., Bernstein P.S.;
"Identification of StARD3 as a lutein-binding protein in the macula of
the primate retina.";
Biochemistry 50:2541-2549(2011).
[15]
FUNCTION.
PubMed=22514632; DOI=10.1371/journal.pone.0034424;
Liapis A., Chen F.W., Davies J.P., Wang R., Ioannou Y.A.;
"MLN64 transport to the late endosome is regulated by binding to 14-3-
3 via a non-canonical binding site.";
PLoS ONE 7:E34424-E34424(2012).
[16]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAPA AND VAPB,
MUTAGENESIS OF 206-GLN--GLU-211, FFAT MOTIF, AND DOMAIN.
PubMed=24105263; DOI=10.1242/jcs.139295;
Alpy F., Rousseau A., Schwab Y., Legueux F., Stoll I., Wendling C.,
Spiegelhalter C., Kessler P., Mathelin C., Rio M.C., Levine T.P.,
Tomasetto C.;
"STARD3 or STARD3NL and VAP form a novel molecular tether between late
endosomes and the ER.";
J. Cell Sci. 126:5500-5512(2013).
[17]
INDUCTION.
PubMed=27679500; DOI=10.1007/s13238-016-0315-0;
Pinto J.B., Graham A.;
"The role of endosomal cholesterol trafficking protein, StAR-related
lipid transfer domain 3 (StarD3/MLN64), in BRIN-BD11 insulinoma
cells.";
Protein Cell 7:833-838(2016).
[18]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAPA AND VAPB,
LIPID-BINDING, AND MUTAGENESIS OF 207-PHE-TYR-208 AND
307-MET--ASN-311.
PubMed=28377464; DOI=10.15252/embj.201695917;
Wilhelm L.P., Wendling C., Vedie B., Kobayashi T., Chenard M.P.,
Tomasetto C., Drin G., Alpy F.;
"STARD3 mediates endoplasmic reticulum-to-endosome cholesterol
transport at membrane contact sites.";
EMBO J. 36:1412-1433(2017).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 216-445.
PubMed=10802740; DOI=10.1038/75192;
Tsujishita Y., Hurley J.H.;
"Structure and lipid transport mechanism of a StAR-related domain.";
Nat. Struct. Biol. 7:408-414(2000).
[20] {ECO:0000244|PDB:5I9J}
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 216-444.
PubMed=27487925; DOI=10.1107/S2053230X16010694;
Horvath M.P., George E.W., Tran Q.T., Baumgardner K., Zharov G.,
Lee S., Sharifzadeh H., Shihab S., Mattinson T., Li B.,
Bernstein P.S.;
"Structure of the lutein-binding domain of human StARD3 at 1.74A
resolution and model of a complex with lutein.";
Acta Crystallogr. F 72:609-618(2016).
-!- FUNCTION: Sterol-binding protein that mediates cholesterol
transport from the endoplasmic reticulum to endosomes
(PubMed:11053434, PubMed:15930133, PubMed:22514632,
PubMed:28377464). 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 (PubMed:24105263, PubMed:28377464). 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 evidences; 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}.
-!- SUBUNIT: Homodimer (PubMed:15718238, PubMed:16709157). Interacts
(via the MENTAL domain) with STARD3NL (PubMed:15718238,
PubMed:16709157). Interacts (via FFAT motif) with VAPA
(PubMed:24105263, PubMed:28377464). Interacts (via FFAT motif)
with VAPB (PubMed:24105263, PubMed:28377464).
{ECO:0000269|PubMed:15718238, ECO:0000269|PubMed:16709157,
ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464}.
-!- INTERACTION:
Q9HD26:GOPC; NbExp=3; IntAct=EBI-9819324, EBI-349832;
Q9P0L0:VAPA; NbExp=4; IntAct=EBI-9819369, EBI-1059156;
-!- SUBCELLULAR LOCATION: Late endosome membrane
{ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:16709157,
ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464}; 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 (PubMed:24105263).
{ECO:0000269|PubMed:24105263}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14849-1; Sequence=Displayed;
Name=2;
IsoId=Q14849-2; Sequence=VSP_042710;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q14849-3; Sequence=VSP_045361;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in retina.
{ECO:0000269|PubMed:21322544}.
-!- INDUCTION: Not regulated by increases in total cholesterol
content, or by marked alterations in cholesterol flux.
{ECO:0000269|PubMed:27679500}.
-!- DOMAIN: The FFAT motif mediates interaction with VAPA and VAPB.
{ECO:0000269|PubMed:24105263}.
-!- 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:0000305|PubMed:28377464}.
-!- DOMAIN: The MENTAL domain anchors the protein in endosome
membranes and exposes the START domain in the cytosol
(PubMed:11053434). It binds cholesterol and mediates homotypic as
well as heterotypic interactions between STARD3 and STARD3NL
(PubMed:15718238, PubMed:16709157). {ECO:0000269|PubMed:11053434,
ECO:0000269|PubMed:15718238, ECO:0000269|PubMed:16709157}.
-!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
-!- CAUTION: STARD3 was reported to function in cholesterol transport
to the mitochondria or to the cell membrane (PubMed:12070139,
PubMed:19965586). Other reports however showed that it mediates
cholesterol transport from the endoplasmic reticulum to endosomes
(PubMed:11053434, PubMed:28377464). Discrepancies may be due to
the different cell type used and the cellular physiological state
(PubMed:28377464). {ECO:0000269|PubMed:11053434,
ECO:0000269|PubMed:12070139, ECO:0000269|PubMed:19965586,
ECO:0000269|PubMed:28377464}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MLN64ID202.html";
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EMBL; X80198; CAA56489.1; -; mRNA.
EMBL; D38255; BAA22525.1; -; mRNA.
EMBL; BT006964; AAP35610.1; -; mRNA.
EMBL; AK300176; BAG61955.1; -; mRNA.
EMBL; AK300842; BAG62493.1; -; mRNA.
EMBL; AC087491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008356; AAH08356.1; -; mRNA.
EMBL; BC008747; AAH08747.1; -; mRNA.
EMBL; BC025679; AAH25679.1; -; mRNA.
CCDS; CCDS11341.1; -. [Q14849-1]
CCDS; CCDS54117.1; -. [Q14849-3]
CCDS; CCDS54118.1; -. [Q14849-2]
PIR; I38027; I38027.
RefSeq; NP_001159409.1; NM_001165937.1. [Q14849-3]
RefSeq; NP_001159410.1; NM_001165938.1. [Q14849-2]
RefSeq; NP_006795.3; NM_006804.3. [Q14849-1]
RefSeq; XP_016879530.1; XM_017024041.1. [Q14849-1]
UniGene; Hs.728838; -.
PDB; 1EM2; X-ray; 2.20 A; A=216-444.
PDB; 2I92; Model; -; A=230-443.
PDB; 5I9J; X-ray; 1.74 A; A=216-444.
PDBsum; 1EM2; -.
PDBsum; 2I92; -.
PDBsum; 5I9J; -.
ProteinModelPortal; Q14849; -.
SMR; Q14849; -.
BioGrid; 116148; 17.
IntAct; Q14849; 3.
STRING; 9606.ENSP00000337446; -.
SwissLipids; SLP:000000712; -.
TCDB; 9.B.64.1.1; the putative cholesterol transporter (start1) family.
iPTMnet; Q14849; -.
PhosphoSitePlus; Q14849; -.
BioMuta; STARD3; -.
DMDM; 116242802; -.
MaxQB; Q14849; -.
PaxDb; Q14849; -.
PeptideAtlas; Q14849; -.
PRIDE; Q14849; -.
DNASU; 10948; -.
Ensembl; ENST00000336308; ENSP00000337446; ENSG00000131748. [Q14849-1]
Ensembl; ENST00000394250; ENSP00000377794; ENSG00000131748. [Q14849-2]
Ensembl; ENST00000544210; ENSP00000439869; ENSG00000131748. [Q14849-3]
GeneID; 10948; -.
KEGG; hsa:10948; -.
UCSC; uc002hsd.4; human. [Q14849-1]
CTD; 10948; -.
DisGeNET; 10948; -.
EuPathDB; HostDB:ENSG00000131748.15; -.
GeneCards; STARD3; -.
HGNC; HGNC:17579; STARD3.
HPA; CAB017021; -.
MIM; 607048; gene.
neXtProt; NX_Q14849; -.
OpenTargets; ENSG00000131748; -.
PharmGKB; PA134981867; -.
eggNOG; KOG3845; Eukaryota.
eggNOG; ENOG41100B5; LUCA.
GeneTree; ENSGT00530000063139; -.
HOGENOM; HOG000015362; -.
HOVERGEN; HBG052482; -.
InParanoid; Q14849; -.
PhylomeDB; Q14849; -.
TreeFam; TF313869; -.
Reactome; R-HSA-196108; Pregnenolone biosynthesis.
ChiTaRS; STARD3; human.
EvolutionaryTrace; Q14849; -.
GenomeRNAi; 10948; -.
PRO; PR:Q14849; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131748; -.
CleanEx; HS_STARD3; -.
ExpressionAtlas; Q14849; baseline and differential.
Genevisible; Q14849; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0044232; C:organelle membrane contact site; IDA:UniProtKB.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0017127; F:cholesterol transporter activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; TAS:Reactome.
GO; GO:0008203; P:cholesterol metabolic process; TAS:ProtInc.
GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0006839; P:mitochondrial transport; TAS:ProtInc.
GO; GO:0006701; P:progesterone biosynthetic process; IEA:Ensembl.
GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc.
GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; IDA: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;
3D-structure; Alternative splicing; Complete proteome; Endosome;
Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 445 StAR-related lipid transfer protein 3.
/FTId=PRO_0000220653.
TOPO_DOM 1 51 Cytoplasmic.
{ECO:0000305|PubMed:11053434}.
TRANSMEM 52 72 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 73 94 Extracellular. {ECO:0000255}.
TRANSMEM 95 115 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 116 120 Cytoplasmic. {ECO:0000255}.
TRANSMEM 121 141 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 142 148 Extracellular. {ECO:0000255}.
TRANSMEM 149 169 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
TOPO_DOM 170 445 Cytoplasmic.
{ECO:0000305|PubMed:11053434}.
DOMAIN 46 217 MENTAL. {ECO:0000255|PROSITE-
ProRule:PRU00770}.
DOMAIN 230 443 START. {ECO:0000255|PROSITE-
ProRule:PRU00197}.
MOTIF 207 212 FFAT. {ECO:0000269|PubMed:24105263}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000250|UniProtKB:Q61542}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000250|UniProtKB:Q61542}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:Q61542}.
VAR_SEQ 122 183 WVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLA
WLETWFLDFKVLPQEAEEERW -> SRRWCPVHSSLSRSSS
LSCSAKGHLATCSPSSLLSSPGWRPGSLTSKSYPRKLKRSD
SAPPG (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045361.
VAR_SEQ 126 143 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042710.
VARIANT 117 117 R -> Q (in dbSNP:rs1877031).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7490069,
ECO:0000269|PubMed:9270027,
ECO:0000269|Ref.3}.
/FTId=VAR_027877.
VARIANT 216 216 G -> A (in dbSNP:rs11556624).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027878.
MUTAGEN 66 67 LL->AS: Abolishes localization to late
endosomes and leads to mislocalization to
the endoplasmic reticulum.
{ECO:0000269|PubMed:11053434}.
MUTAGEN 89 89 Y->V: Abolishes localization to late
endosomes and leads to mislocalization to
the endoplasmic reticulum.
{ECO:0000269|PubMed:11053434}.
MUTAGEN 113 113 Y->A: Does not affect localization to
late endosomes.
{ECO:0000269|PubMed:11053434}.
MUTAGEN 206 212 Missing: Abolishes interaction with VAPA
and VAPB, thereby preventing contact with
the endoplasmic reticulum membrane.
{ECO:0000269|PubMed:24105263}.
MUTAGEN 207 208 FY->AA: Abolishes interaction with VAPA
and VAPB, thereby preventing contact with
the endoplasmic reticulum membrane.
Abolishes cholesterol accumulation in
endosomes. {ECO:0000269|PubMed:28377464}.
MUTAGEN 219 219 N->A: Does not affect localization to
late endosomes.
{ECO:0000269|PubMed:11053434}.
MUTAGEN 307 311 MVLWN->NVLWD: Abolishes ability to
transfer cholesterol between membranes.
{ECO:0000269|PubMed:28377464}.
MUTAGEN 311 311 N->A: Does not affect localization to
late endosomes.
{ECO:0000269|PubMed:11053434}.
HELIX 233 254 {ECO:0000244|PDB:5I9J}.
HELIX 255 258 {ECO:0000244|PDB:5I9J}.
STRAND 260 264 {ECO:0000244|PDB:5I9J}.
STRAND 270 276 {ECO:0000244|PDB:5I9J}.
TURN 277 279 {ECO:0000244|PDB:5I9J}.
STRAND 280 291 {ECO:0000244|PDB:5I9J}.
HELIX 293 300 {ECO:0000244|PDB:5I9J}.
HELIX 304 310 {ECO:0000244|PDB:5I9J}.
STRAND 314 323 {ECO:0000244|PDB:5I9J}.
TURN 324 326 {ECO:0000244|PDB:5I9J}.
STRAND 327 334 {ECO:0000244|PDB:5I9J}.
STRAND 340 342 {ECO:0000244|PDB:5I9J}.
STRAND 345 355 {ECO:0000244|PDB:5I9J}.
STRAND 357 366 {ECO:0000244|PDB:5I9J}.
STRAND 378 380 {ECO:0000244|PDB:5I9J}.
STRAND 385 392 {ECO:0000244|PDB:5I9J}.
STRAND 400 406 {ECO:0000244|PDB:5I9J}.
STRAND 412 414 {ECO:0000244|PDB:5I9J}.
HELIX 416 443 {ECO:0000244|PDB:5I9J}.
SEQUENCE 445 AA; 50502 MW; 8EBFBAF013CFDC7E CRC64;
MSKLPRELTR DLERSLPAVA SLGSSLSHSQ SLSSHLLPPP EKRRAISDVR RTFCLFVTFD
LLFISLLWII ELNTNTGIRK NLEQEIIQYN FKTSFFDIFV LAFFRFSGLL LGYAVLRLRH
WWVIAVTTLV SSAFLIVKVI LSELLSKGAF GYLLPIVSFV LAWLETWFLD FKVLPQEAEE
ERWYLAAQVA VARGPLLFSG ALSEGQFYSP PESFAGSDNE SDEEVAGKKS FSAQEREYIR
QGKEATAVVD QILAQEENWK FEKNNEYGDT VYTIEVPFHG KTFILKTFLP CPAELVYQEV
ILQPERMVLW NKTVTACQIL QRVEDNTLIS YDVSAGAAGG VVSPRDFVNV RRIERRRDRY
LSSGIATSHS AKPPTHKYVR GENGPGGFIV LKSASNPRVC TFVWILNTDL KGRLPRYLIH
QSLAATMFEF AFHLRQRISE LGARA


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