STAR_MOUSE
ID STAR_MOUSE Reviewed; 284 AA.
AC P51557; Q543A5; Q924Y5; Q9D2G1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Steroidogenic acute regulatory protein, mitochondrial;
DE Short=StAR;
DE AltName: Full=Luteinizing hormone-induced protein;
DE AltName: Full=START domain-containing protein 1;
DE Short=StARD1;
DE Flags: Precursor;
GN Name=Star;
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], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7961770; DOI=10.1016/s0021-9258(18)46930-x;
RA Clark B.J., Wells J., King S.R., Stocco D.M.;
RT "The purification, cloning, and expression of a novel luteinizing hormone-
RT induced mitochondrial protein in MA-10 mouse Leydig tumor cells.
RT Characterization of the steroidogenic acute regulatory protein (StAR).";
RL J. Biol. Chem. 269:28314-28322(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129;
RX PubMed=12486153; DOI=10.1523/jneurosci.22-24-10613.2002;
RA King S.R., Manna P.R., Ishii T., Syapin P.J., Ginsberg S.D., Wilson K.,
RA Walsh L.P., Parker K.L., Stocco D.M., Smith R.G., Lamb D.J.;
RT "An essential component in steroid synthesis, the steroidogenic acute
RT regulatory protein, is expressed in discrete regions of the brain.";
RL J. Neurosci. 22:10613-10620(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP PHOSPHORYLATION.
RX PubMed=1797581; DOI=10.1016/0303-7207(91)90210-j;
RA Epstein L.F., Orme-Johnson N.R.;
RT "Acute action of luteinizing hormone on mouse Leydig cells: accumulation of
RT mitochondrial phosphoproteins and stimulation of testosterone synthesis.";
RL Mol. Cell. Endocrinol. 81:113-126(1991).
RN [6]
RP SUBCELLULAR LOCATION, AND TRANSIT PEPTIDE CLEAVAGE SITE.
RX PubMed=7588255; DOI=10.1210/endo.136.11.7588255;
RA King S.R., Ronen-Fuhrmann T., Timberg R., Clark B.J., Orly J., Stocco D.M.;
RT "Steroid production after in vitro transcription, translation, and
RT mitochondrial processing of protein products of complementary
RT deoxyribonucleic acid for steroidogenic acute regulatory protein.";
RL Endocrinology 136:5165-5176(1995).
CC -!- FUNCTION: Plays a key role in steroid hormone synthesis by enhancing
CC the metabolism of cholesterol into pregnenolone. Transporter that binds
CC to and transport cholesterol through the intermembrane space of the
CC mitochondrion. {ECO:0000250|UniProtKB:P49675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:P49675};
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000250|UniProtKB:P49675}.
CC -!- SUBUNIT: May interact with TSPO. {ECO:0000250|UniProtKB:P79245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7588255,
CC ECO:0000269|PubMed:7961770}.
CC -!- TISSUE SPECIFICITY: Expressed within glia and neurons in discrete
CC regions of the brain. {ECO:0000269|PubMed:12486153}.
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DR EMBL; L36062; AAB94783.1; -; mRNA.
DR EMBL; AY032730; AAK50433.2; -; Genomic_DNA.
DR EMBL; AK019725; BAB31842.1; -; mRNA.
DR EMBL; AK054470; BAC35791.1; -; mRNA.
DR EMBL; AK136327; BAE22934.1; -; mRNA.
DR EMBL; BC082283; AAH82283.1; -; mRNA.
DR CCDS; CCDS22203.1; -.
DR PIR; A55455; A55455.
DR RefSeq; NP_035615.2; NM_011485.5.
DR AlphaFoldDB; P51557; -.
DR SMR; P51557; -.
DR IntAct; P51557; 1.
DR STRING; 10090.ENSMUSP00000033979; -.
DR ChEMBL; CHEMBL2029195; -.
DR iPTMnet; P51557; -.
DR PhosphoSitePlus; P51557; -.
DR MaxQB; P51557; -.
DR PaxDb; P51557; -.
DR PRIDE; P51557; -.
DR ProteomicsDB; 257368; -.
DR Antibodypedia; 23510; 337 antibodies from 35 providers.
DR DNASU; 20845; -.
DR Ensembl; ENSMUST00000033979; ENSMUSP00000033979; ENSMUSG00000031574.
DR GeneID; 20845; -.
DR KEGG; mmu:20845; -.
DR UCSC; uc009lhb.1; mouse.
DR CTD; 6770; -.
DR MGI; MGI:102760; Star.
DR VEuPathDB; HostDB:ENSMUSG00000031574; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000155477; -.
DR HOGENOM; CLU_093200_1_0_1; -.
DR InParanoid; P51557; -.
DR OMA; KMPEQKG; -.
DR OrthoDB; 1437203at2759; -.
DR PhylomeDB; P51557; -.
DR TreeFam; TF313869; -.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR UniPathway; UPA00296; -.
DR BioGRID-ORCS; 20845; 3 hits in 74 CRISPR screens.
DR PRO; PR:P51557; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P51557; protein.
DR Bgee; ENSMUSG00000031574; Expressed in adrenal gland and 110 other tissues.
DR ExpressionAtlas; P51557; baseline and differential.
DR Genevisible; P51557; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; IDA:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0018879; P:biphenyl metabolic process; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
DR GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071378; P:cellular response to growth hormone stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042747; P:circadian sleep/wake cycle, REM sleep; IEA:Ensembl.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl.
DR GO; GO:0016101; P:diterpenoid metabolic process; IEA:Ensembl.
DR GO; GO:0006703; P:estrogen biosynthetic process; ISO:MGI.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
DR GO; GO:0017143; P:insecticide metabolic process; IEA:Ensembl.
DR GO; GO:0032367; P:intracellular cholesterol transport; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:Ensembl.
DR GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl.
DR GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IDA:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
DR GO; GO:0009635; P:response to herbicide; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
DR GO; GO:0044321; P:response to leptin; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0061370; P:testosterone biosynthetic process; IEA:Ensembl.
DR CDD; cd08905; START_STARD1-like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR029866; StAR.
DR InterPro; IPR000799; StAR-like.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR46489; PTHR46489; 1.
DR Pfam; PF01852; START; 1.
DR PRINTS; PR00978; STARPROTEIN.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipid transport; Lipid-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Steroidogenesis; Transit peptide;
KW Transport.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7588255"
FT CHAIN 63..284
FT /note="Steroidogenic acute regulatory protein,
FT mitochondrial"
FT /id="PRO_0000033318"
FT DOMAIN 66..279
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT MOD_RES 56
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P49675"
FT MOD_RES 194
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P49675"
FT CONFLICT 139
FT /note="R -> H (in Ref. 3; BAB31842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 31626 MW; 9BB13E52D4439B72 CRC64;
MFLATFKLCA GSSYRHMRNM KGLRHQAVLA IGQELNWRAL GDSSPGWMGQ VRRRSSLLGS
QLEATLYSDQ ELSYIQQGEV AMQKALGILN NQEGWKKESQ QENGDEVLSK MVPDVGKVFR
LEVVVDQPMD RLYEELVDRM EAMGEWNPNV KEIKVLQRIG KDTVITHELA AAAAGNLVGP
RDFVSVRCTK RRGSTCVLAG MATHFGEMPE QSGVIRAEHG PTCMVLHPLA GSPSKTKLTW
LLSIDLKGWL PKTIINQVLS QTQIEFANHL RKRLEASPAS EAQC
