ID   STAR_SHEEP              Reviewed;         285 AA.
AC   P79245; Q9GMD0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   25-MAY-2022, entry version 99.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TSPO.
RX   PubMed=11145616; DOI=10.1210/endo.142.1.8052;
RA   West L.A., Horvat R.D., Roess D.A., Barisas B.G., Juengel J.L.,
RA   Niswender G.D.;
RT   "Steroidogenic acute regulatory protein and peripheral-type benzodiazepine
RT   receptor associate at the mitochondrial membrane.";
RL   Endocrinology 142:502-505(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 97-217.
RC   TISSUE=Corpus luteum;
RX   PubMed=7588291; DOI=10.1210/endo.136.12.7588291;
RA   Juengel J.L., Meberg B.M., Turzillo A.M., Nett T.M., Niswender G.D.;
RT   "Hormonal regulation of messenger ribonucleic acid encoding steroidogenic
RT   acute regulatory protein in ovine corpora lutea.";
RL   Endocrinology 136:5423-5429(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:0000269|PubMed:11145616}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P51557}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF290202; AAG02464.1; -; mRNA.
DR   EMBL; S80098; AAB47088.1; -; mRNA.
DR   RefSeq; NP_001009243.1; NM_001009243.1.
DR   AlphaFoldDB; P79245; -.
DR   SMR; P79245; -.
DR   STRING; 9940.ENSOARP00000001315; -.
DR   GeneID; 443122; -.
DR   KEGG; oas:443122; -.
DR   CTD; 6770; -.
DR   eggNOG; KOG3845; Eukaryota.
DR   OrthoDB; 1437203at2759; -.
DR   UniPathway; UPA00296; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0015485; F:cholesterol binding; IEA:InterPro.
DR   GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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_0000033321"
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        100
FT                   /note="S -> N (in Ref. 2; AAB47088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="V -> A (in Ref. 2; AAB47088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        186
FT                   /note="S -> R (in Ref. 2; AAB47088)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  31895 MW;  AB130FD90A1DF295 CRC64;
     MLLATFKLCA GSSYRHVRSM KGLRQQAVLA IGQELNRRAL GGPAPAAWIY QVRRRGSLLG
     SQLEDSLYSD QELAYIQQGE EAMQRALGIL KDQEGWKKES RQVNGDEVLS KVIPDVGKVF
     RLEVVVDQPM ERLYEELVER MEAMGEWNPS VKEIKVLQKI GKDTIITHEL AAEAAGNLVG
     PRDFVSVRCT KRRGSMCVLA GTATLYEEMP QQKGVIRAEH GPTCMVLRPL AGSPSRTKLT
     WLLSIDLKGW LPKTIINQVL SQTQVDFANH LRKRLESCPA LEARC