STAR3_HUMAN
ID STAR3_HUMAN Reviewed; 445 AA.
AC Q14849; A8MXA4; B4DUY1; F5H0G2; Q53Y53; Q96HM9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=StAR-related lipid transfer protein 3 {ECO:0000305};
DE AltName: Full=Metastatic lymph node gene 64 protein {ECO:0000303|PubMed:11053434};
DE Short=MLN 64 {ECO:0000303|PubMed:11053434};
DE AltName: Full=Protein CAB1 {ECO:0000303|PubMed:9270027};
DE AltName: Full=START domain-containing protein 3 {ECO:0000303|PubMed:21322544};
DE Short=StARD3 {ECO:0000303|PubMed:21322544};
GN Name=STARD3 {ECO:0000312|HGNC:HGNC:17579};
GN Synonyms=CAB1 {ECO:0000303|PubMed:9270027},
GN MLN64 {ECO:0000303|PubMed:11053434};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-117.
RC TISSUE=Mammary carcinoma;
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 [MRNA] (ISOFORM 1), AND VARIANT GLN-117.
RC TISSUE=Esophageal carcinoma;
RX PubMed=9270027;
RA Akiyama N., Sasaki H., Ishizuka T., Kishi T., Sakamoto H., Onda M.,
RA Hirai H., Yazaki Y., Sugimura T., Terada M.;
RT "Isolation of a candidate gene, CAB1, for cholesterol transport to
RT mitochondria from the c-ERBB-2 amplicon by a modified cDNA selection
RT method.";
RL Cancer Res. 57:3548-3553(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-117.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP GLN-117.
RC TISSUE=Placenta, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-117
RP AND ALA-216.
RC TISSUE=Lung, Skin, and Spleen;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF
RP 66-LEU-LEU-67; TYR-89; TYR-113; ASN-219 AND ASN-311.
RX PubMed=11053434; DOI=10.1074/jbc.m006279200;
RA Alpy F., Stoeckel M.-E., Dierich A., Escola J.-M., Wendling C.,
RA Chenard M.-P., Vanier M.T., Gruenberg J., Tomasetto C., Rio M.-C.;
RT "The steroidogenic acute regulatory protein homolog MLN64, a late endosomal
RT cholesterol-binding protein.";
RL J. Biol. Chem. 276:4261-4269(2001).
RN [8]
RP FUNCTION.
RX PubMed=12070139; DOI=10.1074/jbc.m200003200;
RA Zhang M., Liu P., Dwyer N.K., Christenson L.K., Fujimoto T., Martinez F.,
RA Comly M., Hanover J.A., Blanchette-Mackie E.J., Strauss J.F. III;
RT "MLN64 mediates mobilization of lysosomal cholesterol to steroidogenic
RT mitochondria.";
RL J. Biol. Chem. 277:33300-33310(2002).
RN [9]
RP SUBUNIT, INTERACTION WITH STARD3NL, AND DOMAIN.
RX PubMed=15718238; DOI=10.1074/jbc.m500723200;
RA Alpy F., Latchumanan V.K., Kedinger V., Janoshazi A., Thiele C.,
RA Wendling C., Rio M.C., Tomasetto C.;
RT "Functional characterization of the MENTAL domain.";
RL J. Biol. Chem. 280:17945-17952(2005).
RN [10]
RP FUNCTION.
RX PubMed=15930133; DOI=10.1091/mbc.e04-12-1105;
RA Hoelttae-Vuori M., Alpy F., Tanhuanpaeae K., Jokitalo E., Mutka A.L.,
RA Ikonen E.;
RT "MLN64 is involved in actin-mediated dynamics of late endocytic
RT organelles.";
RL Mol. Biol. Cell 16:3873-3886(2005).
RN [11]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH STARD3NL, AND DOMAIN.
RX PubMed=16709157; DOI=10.1042/bst0340343;
RA Alpy F., Tomasetto C.;
RT "MLN64 and MENTHO, two mediators of endosomal cholesterol transport.";
RL Biochem. Soc. Trans. 34:343-345(2006).
RN [12]
RP 3D-STRUCTURE MODELING.
RX PubMed=16990645; DOI=10.1194/jlr.m600232-jlr200;
RA Murcia M., Faraldo-Gomez J.D., Maxfield F.R., Roux B.;
RT "Modeling the structure of the StART domains of MLN64 and StAR proteins in
RT complex with cholesterol.";
RL J. Lipid Res. 47:2614-2630(2006).
RN [13]
RP FUNCTION.
RX PubMed=19965586; DOI=10.1194/jlr.m002345;
RA Charman M., Kennedy B.E., Osborne N., Karten B.;
RT "MLN64 mediates egress of cholesterol from endosomes to mitochondria in the
RT absence of functional Niemann-Pick Type C1 protein.";
RL J. Lipid Res. 51:1023-1034(2010).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21322544; DOI=10.1021/bi101906y;
RA Li B., Vachali P., Frederick J.M., Bernstein P.S.;
RT "Identification of StARD3 as a lutein-binding protein in the macula of the
RT primate retina.";
RL Biochemistry 50:2541-2549(2011).
RN [15]
RP FUNCTION.
RX PubMed=22514632; DOI=10.1371/journal.pone.0034424;
RA Liapis A., Chen F.W., Davies J.P., Wang R., Ioannou Y.A.;
RT "MLN64 transport to the late endosome is regulated by binding to 14-3-3 via
RT a non-canonical binding site.";
RL PLoS ONE 7:E34424-E34424(2012).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAPA AND VAPB, MUTAGENESIS
RP OF 206-GLN--GLU-211, FFAT MOTIF, AND DOMAIN.
RX PubMed=24105263; DOI=10.1242/jcs.139295;
RA Alpy F., Rousseau A., Schwab Y., Legueux F., Stoll I., Wendling C.,
RA Spiegelhalter C., Kessler P., Mathelin C., Rio M.C., Levine T.P.,
RA Tomasetto C.;
RT "STARD3 or STARD3NL and VAP form a novel molecular tether between late
RT endosomes and the ER.";
RL J. Cell Sci. 126:5500-5512(2013).
RN [17]
RP INDUCTION.
RX PubMed=27679500; DOI=10.1007/s13238-016-0315-0;
RA Pinto J.B., Graham A.;
RT "The role of endosomal cholesterol trafficking protein, StAR-related lipid
RT transfer domain 3 (StarD3/MLN64), in BRIN-BD11 insulinoma cells.";
RL Protein Cell 7:833-838(2016).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAPA AND VAPB,
RP LIPID-BINDING, AND MUTAGENESIS OF 207-PHE-TYR-208 AND 307-MET--ASN-311.
RX PubMed=28377464; DOI=10.15252/embj.201695917;
RA Wilhelm L.P., Wendling C., Vedie B., Kobayashi T., Chenard M.P.,
RA Tomasetto C., Drin G., Alpy F.;
RT "STARD3 mediates endoplasmic reticulum-to-endosome cholesterol transport at
RT membrane contact sites.";
RL EMBO J. 36:1412-1433(2017).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MOSPD2, SUBCELLULAR
RP LOCATION, DOMAIN, FFAT MOTIF, AND MUTAGENESIS OF 207-PHE-TYR-208.
RX PubMed=29858488; DOI=10.15252/embr.201745453;
RA Di Mattia T., Wilhelm L.P., Ikhlef S., Wendling C., Spehner D., Nomine Y.,
RA Giordano F., Mathelin C., Drin G., Tomasetto C., Alpy F.;
RT "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum
RT membrane contact sites.";
RL EMBO Rep. 19:0-0(2018).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 216-445.
RX PubMed=10802740; DOI=10.1038/75192;
RA Tsujishita Y., Hurley J.H.;
RT "Structure and lipid transport mechanism of a StAR-related domain.";
RL Nat. Struct. Biol. 7:408-414(2000).
RN [21] {ECO:0007744|PDB:5I9J}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 216-444.
RX PubMed=27487925; DOI=10.1107/s2053230x16010694;
RA Horvath M.P., George E.W., Tran Q.T., Baumgardner K., Zharov G., Lee S.,
RA Sharifzadeh H., Shihab S., Mattinson T., Li B., Bernstein P.S.;
RT "Structure of the lutein-binding domain of human StARD3 at 1.74A resolution
RT and model of a complex with lutein.";
RL Acta Crystallogr. F 72:609-618(2016).
CC -!- FUNCTION: Sterol-binding protein that mediates cholesterol transport
CC from the endoplasmic reticulum to endosomes (PubMed:11053434,
CC PubMed:15930133, PubMed:22514632, PubMed:28377464). Creates contact
CC site between the endoplasmic reticulum and late endosomes: localizes to
CC late endosome membranes and contacts the endoplasmic reticulum via
CC interaction with VAPA and VAPB (PubMed:24105263, PubMed:28377464). Acts
CC as a lipid transfer protein that redirects sterol to the endosome at
CC the expense of the cell membrane and favors membrane formation inside
CC endosomes (PubMed:28377464). May also mediate cholesterol transport
CC between other membranes, such as mitochondria membrane or cell membrane
CC (PubMed:12070139, PubMed:19965586). However, such results need
CC additional experimental evidences; probably mainly mediates cholesterol
CC transport from the endoplasmic reticulum to endosomes
CC (PubMed:28377464). Does not activate transcriptional cholesterol
CC sensing (PubMed:28377464). Able to bind other lipids, such as lutein, a
CC xanthophyll carotenoids that form the macular pigment of the retina
CC (PubMed:21322544). {ECO:0000269|PubMed:11053434,
CC ECO:0000269|PubMed:12070139, ECO:0000269|PubMed:15930133,
CC ECO:0000269|PubMed:19965586, ECO:0000269|PubMed:21322544,
CC ECO:0000269|PubMed:22514632, ECO:0000269|PubMed:24105263,
CC ECO:0000269|PubMed:28377464}.
CC -!- SUBUNIT: Homodimer (PubMed:15718238, PubMed:16709157). Interacts (via
CC the MENTAL domain) with STARD3NL (PubMed:15718238, PubMed:16709157).
CC Interacts (via FFAT motif) with VAPA (PubMed:24105263,
CC PubMed:28377464). Interacts (via FFAT motif) with VAPB
CC (PubMed:24105263, PubMed:28377464). Interacts (via FFAT motif) with
CC MOSPD2 (via MSP domain) (PubMed:29858488).
CC {ECO:0000269|PubMed:15718238, ECO:0000269|PubMed:16709157,
CC ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464,
CC ECO:0000269|PubMed:29858488}.
CC -!- INTERACTION:
CC Q14849; Q13520: AQP6; NbExp=3; IntAct=EBI-9819324, EBI-13059134;
CC Q14849; Q9HD26: GOPC; NbExp=3; IntAct=EBI-9819324, EBI-349832;
CC Q14849; Q8NHP6: MOSPD2; NbExp=6; IntAct=EBI-9819324, EBI-2812848;
CC Q14849; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-9819324, EBI-12055631;
CC Q14849-1; Q9P0L0: VAPA; NbExp=4; IntAct=EBI-9819369, EBI-1059156;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:16709157,
CC ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464,
CC ECO:0000269|PubMed:29858488}; 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:0000269|PubMed:24105263, ECO:0000269|PubMed:29858488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14849-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14849-2; Sequence=VSP_042710;
CC Name=3;
CC IsoId=Q14849-3; Sequence=VSP_045361;
CC -!- TISSUE SPECIFICITY: Expressed in retina. {ECO:0000269|PubMed:21322544}.
CC -!- INDUCTION: Not regulated by increases in total cholesterol content, or
CC by marked alterations in cholesterol flux.
CC {ECO:0000269|PubMed:27679500}.
CC -!- DOMAIN: The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2.
CC {ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:29858488}.
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:0000305|PubMed:28377464}.
CC -!- DOMAIN: The MENTAL domain anchors the protein in endosome membranes and
CC exposes the START domain in the cytosol (PubMed:11053434). It binds
CC cholesterol and mediates homotypic as well as heterotypic interactions
CC between STARD3 and STARD3NL (PubMed:15718238, PubMed:16709157).
CC {ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:15718238,
CC ECO:0000269|PubMed:16709157}.
CC -!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
CC -!- CAUTION: STARD3 was reported to function in cholesterol transport to
CC the mitochondria or to the cell membrane (PubMed:12070139,
CC PubMed:19965586). Other reports however showed that it mediates
CC cholesterol transport from the endoplasmic reticulum to endosomes
CC (PubMed:11053434, PubMed:28377464). Discrepancies may be due to the
CC different cell type used and the cellular physiological state
CC (PubMed:28377464). {ECO:0000269|PubMed:11053434,
CC ECO:0000269|PubMed:12070139, ECO:0000269|PubMed:19965586,
CC ECO:0000269|PubMed:28377464}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MLN64ID202.html";
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DR EMBL; X80198; CAA56489.1; -; mRNA.
DR EMBL; D38255; BAA22525.1; -; mRNA.
DR EMBL; BT006964; AAP35610.1; -; mRNA.
DR EMBL; AK300176; BAG61955.1; -; mRNA.
DR EMBL; AK300842; BAG62493.1; -; mRNA.
DR EMBL; AC087491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008356; AAH08356.1; -; mRNA.
DR EMBL; BC008747; AAH08747.1; -; mRNA.
DR EMBL; BC025679; AAH25679.1; -; mRNA.
DR CCDS; CCDS11341.1; -. [Q14849-1]
DR CCDS; CCDS54117.1; -. [Q14849-3]
DR CCDS; CCDS54118.1; -. [Q14849-2]
DR PIR; I38027; I38027.
DR RefSeq; NP_001159409.1; NM_001165937.1. [Q14849-3]
DR RefSeq; NP_001159410.1; NM_001165938.1. [Q14849-2]
DR RefSeq; NP_006795.3; NM_006804.3. [Q14849-1]
DR RefSeq; XP_016879530.1; XM_017024041.1. [Q14849-1]
DR PDB; 1EM2; X-ray; 2.20 A; A=216-444.
DR PDB; 5I9J; X-ray; 1.74 A; A=216-444.
DR PDB; 6TQR; X-ray; 1.85 A; E/F=200-216.
DR PDB; 6TQU; X-ray; 2.40 A; C/D=196-216.
DR PDBsum; 1EM2; -.
DR PDBsum; 5I9J; -.
DR PDBsum; 6TQR; -.
DR PDBsum; 6TQU; -.
DR AlphaFoldDB; Q14849; -.
DR SMR; Q14849; -.
DR BioGRID; 116148; 93.
DR IntAct; Q14849; 19.
DR STRING; 9606.ENSP00000337446; -.
DR BindingDB; Q14849; -.
DR ChEMBL; CHEMBL4523297; -.
DR SwissLipids; SLP:000000712; -.
DR TCDB; 9.B.64.1.1; the putative cholesterol transporter (start1) family.
DR iPTMnet; Q14849; -.
DR MetOSite; Q14849; -.
DR PhosphoSitePlus; Q14849; -.
DR BioMuta; STARD3; -.
DR DMDM; 116242802; -.
DR EPD; Q14849; -.
DR jPOST; Q14849; -.
DR MassIVE; Q14849; -.
DR MaxQB; Q14849; -.
DR PaxDb; Q14849; -.
DR PeptideAtlas; Q14849; -.
DR PRIDE; Q14849; -.
DR ProteomicsDB; 25332; -.
DR ProteomicsDB; 60208; -. [Q14849-1]
DR ProteomicsDB; 60209; -. [Q14849-2]
DR Antibodypedia; 28306; 80 antibodies from 22 providers.
DR DNASU; 10948; -.
DR Ensembl; ENST00000336308.10; ENSP00000337446.5; ENSG00000131748.16. [Q14849-1]
DR Ensembl; ENST00000394250.8; ENSP00000377794.4; ENSG00000131748.16. [Q14849-2]
DR Ensembl; ENST00000544210.6; ENSP00000439869.2; ENSG00000131748.16. [Q14849-3]
DR GeneID; 10948; -.
DR KEGG; hsa:10948; -.
DR MANE-Select; ENST00000336308.10; ENSP00000337446.5; NM_006804.4; NP_006795.3.
DR UCSC; uc002hsd.4; human. [Q14849-1]
DR CTD; 10948; -.
DR DisGeNET; 10948; -.
DR GeneCards; STARD3; -.
DR HGNC; HGNC:17579; STARD3.
DR HPA; ENSG00000131748; Low tissue specificity.
DR MIM; 607048; gene.
DR neXtProt; NX_Q14849; -.
DR OpenTargets; ENSG00000131748; -.
DR PharmGKB; PA134981867; -.
DR VEuPathDB; HostDB:ENSG00000131748; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000159051; -.
DR HOGENOM; CLU_033480_0_0_1; -.
DR InParanoid; Q14849; -.
DR OMA; NQMGLDC; -.
DR OrthoDB; 1437203at2759; -.
DR PhylomeDB; Q14849; -.
DR TreeFam; TF313869; -.
DR PathwayCommons; Q14849; -.
DR Reactome; R-HSA-196108; Pregnenolone biosynthesis.
DR SignaLink; Q14849; -.
DR BioGRID-ORCS; 10948; 19 hits in 1072 CRISPR screens.
DR ChiTaRS; STARD3; human.
DR EvolutionaryTrace; Q14849; -.
DR GenomeRNAi; 10948; -.
DR Pharos; Q14849; Tbio.
DR PRO; PR:Q14849; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14849; protein.
DR Bgee; ENSG00000131748; Expressed in right lung and 172 other tissues.
DR ExpressionAtlas; Q14849; baseline and differential.
DR Genevisible; Q14849; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0044232; C:organelle membrane contact site; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; TAS:ProtInc.
DR GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006839; P:mitochondrial transport; TAS:ProtInc.
DR GO; GO:0006701; P:progesterone biosynthetic process; IEA:Ensembl.
DR GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc.
DR GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; IDA:UniProtKB.
DR CDD; cd08906; START_STARD3-like; 1.
DR DisProt; DP02835; -.
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 3D-structure; Alternative splicing; Endosome; Lipid transport;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="StAR-related lipid transfer protein 3"
FT /id="PRO_0000220653"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11053434"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 73..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 116..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 142..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 170..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11053434"
FT DOMAIN 46..217
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT DOMAIN 230..443
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT MOTIF 207..212
FT /note="FFAT"
FT /evidence="ECO:0000269|PubMed:24105263,
FT ECO:0000269|PubMed:29858488"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61542"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61542"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61542"
FT VAR_SEQ 122..183
FT /note="WVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKV
FT LPQEAEEERW -> SRRWCPVHSSLSRSSSLSCSAKGHLATCSPSSLLSSPGWRPGSLT
FT SKSYPRKLKRSDSAPPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045361"
FT VAR_SEQ 126..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042710"
FT VARIANT 117
FT /note="R -> Q (in dbSNP:rs1877031)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7490069,
FT ECO:0000269|PubMed:9270027, ECO:0000269|Ref.3"
FT /id="VAR_027877"
FT VARIANT 216
FT /note="G -> A (in dbSNP:rs11556624)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027878"
FT MUTAGEN 66..67
FT /note="LL->AS: Abolishes localization to late endosomes and
FT leads to mislocalization to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:11053434"
FT MUTAGEN 89
FT /note="Y->V: Abolishes localization to late endosomes and
FT leads to mislocalization to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:11053434"
FT MUTAGEN 113
FT /note="Y->A: Does not affect localization to late
FT endosomes."
FT /evidence="ECO:0000269|PubMed:11053434"
FT MUTAGEN 206..212
FT /note="Missing: Abolishes interaction with VAPA and VAPB,
FT thereby preventing contact with the endoplasmic reticulum
FT membrane."
FT /evidence="ECO:0000269|PubMed:24105263"
FT MUTAGEN 207..208
FT /note="FY->AA: Abolishes interaction with VAPA, VAPB and
FT MOSPD2, thereby preventing contact with the endoplasmic
FT reticulum membrane. Abolishes cholesterol accumulation in
FT endosomes."
FT /evidence="ECO:0000269|PubMed:28377464,
FT ECO:0000269|PubMed:29858488"
FT MUTAGEN 219
FT /note="N->A: Does not affect localization to late
FT endosomes."
FT /evidence="ECO:0000269|PubMed:11053434"
FT MUTAGEN 307..311
FT /note="MVLWN->NVLWD: Abolishes ability to transfer
FT cholesterol between membranes."
FT /evidence="ECO:0000269|PubMed:28377464"
FT MUTAGEN 311
FT /note="N->A: Does not affect localization to late
FT endosomes."
FT /evidence="ECO:0000269|PubMed:11053434"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:5I9J"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:5I9J"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:5I9J"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:5I9J"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:5I9J"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 357..366
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:5I9J"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5I9J"
FT HELIX 416..443
FT /evidence="ECO:0007829|PDB:5I9J"
SQ 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
