STAR3_MACMU
ID STAR3_MACMU Reviewed; 445 AA.
AC F7B909; G7NI18;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=StAR-related lipid transfer protein 3 {ECO:0000250|UniProtKB:Q14849};
DE AltName: Full=Metastatic lymph node gene 64 protein {ECO:0000250|UniProtKB:Q14849};
DE Short=MLN 64 {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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Caudate nucleus, Testis, and Thymus;
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B. Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573;
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
RN [4]
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).
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). Able to bind other
CC lipids, such as lutein, a xanthophyll carotenoids that form the macular
CC pigment of the retina (PubMed:21322544). {ECO:0000250|UniProtKB:Q14849,
CC ECO:0000269|PubMed:21322544}.
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 -!- TISSUE SPECIFICITY: Present in retina. Localizes to all neurons of
CC macular retina and especially cone inner segments and axons (at protein
CC level). {ECO:0000269|PubMed:21322544}.
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; JU332651; AFE76406.1; -; mRNA.
DR EMBL; JU474094; AFH30898.1; -; mRNA.
DR EMBL; JV046016; AFI36087.1; -; mRNA.
DR EMBL; JSUE03016792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM001268; EHH24897.1; -; Genomic_DNA.
DR RefSeq; XP_001089498.1; XM_001089498.3.
DR RefSeq; XP_014975020.1; XM_015119534.1.
DR AlphaFoldDB; F7B909; -.
DR SMR; F7B909; -.
DR STRING; 9544.ENSMMUP00000034626; -.
DR Ensembl; ENSMMUT00000001900; ENSMMUP00000001793; ENSMMUG00000001343.
DR Ensembl; ENSMMUT00000001901; ENSMMUP00000001794; ENSMMUG00000001343.
DR Ensembl; ENSMMUT00000086675; ENSMMUP00000073324; ENSMMUG00000001343.
DR Ensembl; ENSMMUT00000088987; ENSMMUP00000071893; ENSMMUG00000001343.
DR Ensembl; ENSMMUT00000096482; ENSMMUP00000062822; ENSMMUG00000001343.
DR Ensembl; ENSMMUT00000105634; ENSMMUP00000073397; ENSMMUG00000001343.
DR GeneID; 697212; -.
DR KEGG; mcc:697212; -.
DR CTD; 10948; -.
DR VEuPathDB; HostDB:ENSMMUG00000001343; -.
DR VGNC; VGNC:77941; STARD3.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000159051; -.
DR HOGENOM; CLU_128806_0_0_1; -.
DR InParanoid; F7B909; -.
DR OMA; NQMGLDC; -.
DR OrthoDB; 1437203at2759; -.
DR TreeFam; TF333228; -.
DR Proteomes; UP000006718; Chromosome 16.
DR Proteomes; UP000013456; Chromosome 16.
DR Bgee; ENSMMUG00000001343; Expressed in hindlimb stylopod muscle and 21 other tissues.
DR ExpressionAtlas; F7B909; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0006701; P:progesterone biosynthetic process; IEA:Ensembl.
DR GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; IBA:GO_Central.
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..445
FT /note="StAR-related lipid transfer protein 3"
FT /id="PRO_0000440953"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TOPO_DOM 73..94
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TOPO_DOM 116..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TOPO_DOM 142..148
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00770"
FT TOPO_DOM 170..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
FT DOMAIN 46..217
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT DOMAIN 248..443
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT MOTIF 207..212
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q14849"
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 CONFLICT 341
FT /note="M -> V (in Ref. 1; AFE76406/AFH30898/AFI36087 and 3;
FT EHH24897)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="L -> P (in Ref. 1; AFE76406/AFH30898/AFI36087 and 3;
FT EHH24897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50229 MW; F28A8B147FAEC321 CRC64;
MSKLPGELAR DLECSLPAVA SLGSSLSHSQ SLSSHLLPPP EKRRAISDVR RTFCLFVTFD
LLFISLLWII ELNTNTGIRK NLEQEIIQYN FKTSFFDIFV LAFFRFSGLL LGYAVLRLQH
WWVIAVTTLV SSAFLIVKVI LSELLSKGAF GYLLPIVSFV LAWLETWFLD FKVLPQEAEE
ERWYLAAQAA VARGPLLFSG ALSEGQFYSP PESFAGSDNE SDEEVAGKKS FSAQEREYIR
QGKEATAVVD QILAQEENWK FEKNNEYGDT VYTIEVPFHG KTFILKTFLP CPAELVYQEV
ILQPERMVLW NKTVTACQIL QRVEDNTLIS YDVSAGAAGG MVSPRDFVNV RRIERRRDRY
LSSGIATAHS AKPLTHKYVR GENGPGGFVV LKSASNPCVC TFVWILNTDL KGRLPRYLIH
QSLAATMFEF AFHLRQRISE LGARA
