STAR_BOVIN
ID STAR_BOVIN Reviewed; 285 AA.
AC Q28918; Q2YDI1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Steroidogenic acute regulatory protein, mitochondrial;
DE Short=StAR;
DE AltName: Full=START domain-containing protein 1;
DE Short=StARD1;
DE Flags: Precursor;
GN Name=STAR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Corpus luteum;
RX PubMed=7488004; DOI=10.1006/bbrc.1995.2513;
RA Hartung S., Rust W., Balvers M., Ivell R.;
RT "Molecular cloning and in vivo expression of the bovine steroidogenic acute
RT regulatory protein.";
RL Biochem. Biophys. Res. Commun. 215:646-653(1995).
RN [2]
RP SEQUENCE REVISION TO 85 AND 174.
RA Hartung S., Rust W., Balvers M., Ivell R.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION.
RX PubMed=7626524; DOI=10.1016/0960-0760(95)00026-v;
RA Hartigan J.A., Green E.G., Mortensen R.M., Menachery A., Williams G.H.,
RA Orme-Johnson N.R.;
RT "Comparison of protein phosphorylation patterns produced in adrenal cells
RT by activation of cAMP-dependent protein kinase and Ca-dependent protein
RT kinase.";
RL J. Steroid Biochem. Mol. Biol. 53:95-101(1995).
CC -!- FUNCTION: Plays a key role in steroid hormone synthesis by enhancing
CC the metabolism of cholesterol into pregnenolone. Mediates the transfer
CC of cholesterol from the outer mitochondrial membrane to the inner
CC mitochondrial membrane where it is cleaved to pregnenolone (By
CC similarity). {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:0000250|UniProtKB:P51557}.
CC -!- TISSUE SPECIFICITY: Corpus luteum and adrenal gland.
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DR EMBL; Y17259; CAA76717.1; -; mRNA.
DR EMBL; Y17260; CAA76718.1; -; Genomic_DNA.
DR EMBL; BC110213; AAI10214.1; -; mRNA.
DR PIR; JC4315; JC4315.
DR RefSeq; NP_776614.1; NM_174189.2.
DR AlphaFoldDB; Q28918; -.
DR SMR; Q28918; -.
DR STRING; 9913.ENSBTAP00000044633; -.
DR PaxDb; Q28918; -.
DR Ensembl; ENSBTAT00000047426; ENSBTAP00000044633; ENSBTAG00000033345.
DR GeneID; 281507; -.
DR KEGG; bta:281507; -.
DR CTD; 6770; -.
DR VEuPathDB; HostDB:ENSBTAG00000033345; -.
DR VGNC; VGNC:35360; STAR.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000155477; -.
DR HOGENOM; CLU_093200_1_0_1; -.
DR InParanoid; Q28918; -.
DR OMA; KMPEQKG; -.
DR OrthoDB; 1437203at2759; -.
DR TreeFam; TF313869; -.
DR Reactome; R-BTA-196108; Pregnenolone biosynthesis.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000033345; Expressed in diaphragm and 101 other tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032367; P:intracellular cholesterol transport; IBA:GO_Central.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
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 Lipid transport; Lipid-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Steroidogenesis; Transit peptide; Transport.
FT TRANSIT 1..63
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 64..285
FT /note="Steroidogenic acute regulatory protein,
FT mitochondrial"
FT /id="PRO_0000033314"
FT DOMAIN 67..280
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT MOD_RES 57
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P49675"
FT MOD_RES 195
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P49675"
FT CONFLICT 75
FT /note="Y -> H (in Ref. 1; CAA76717)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> K (in Ref. 1; CAA76718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31871 MW; FB5C4174FF888E55 CRC64;
MLLATFKLCA GSSYRHVRSM KGLQQQAVLA IGQELNRRAL GGPAPAAWIN QVRRRGSLLG
SQLEDPLYSD QELAYIQQGE EAMQRALGIL KDQEGWKKES RQANGDEVLS KVIPDVGKVF
RLEVVVDQPM ERLYEELVER MEAMGEWNPN VKEIKVLQKI GKDTVITHEL AAEVAGNLVG
PRDFVSVRCT KRRGSMCVLA GMATLYEEMP QQKGVIRAEH GPTCMVLRPL AGSPSRTKLT
WLLSIDLKGW LPKTIINQVL SQTQVDFANH LRKRLESCPA LEARC
