ID   STAR_PIG                Reviewed;         285 AA.
AC   Q28996; Q53Z33; Q95259;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 104.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9048613; DOI=10.1210/endo.138.3.5003;
RA   Pilon N., Daneau I., Brisson C., Ethier J.-F., Lussier J.G.,
RA   Silversides D.W.;
RT   "Porcine and bovine steroidogenic acute regulatory protein (StAR) gene
RT   expression during gestation.";
RL   Endocrinology 138:1085-1091(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Hwang K.-C., Ok D.-W., Kwon D.-N., Choi Y.-J., Kim J.-H.;
RT   "Analysis of pig genes.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 132-210.
RC   TISSUE=Corpus luteum;
RX   PubMed=8977433; DOI=10.1210/endo.138.1.4894;
RA   Balasubramanian K., Lavoie H.A., Garmey J.C., Stocco D.M., Veldhuis J.D.;
RT   "Regulation of porcine granulosa cell steroidogenic acute regulatory
RT   protein (StAR) by insulin-like growth factor I: synergism with follicle-
RT   stimulating hormone or protein kinase A agonist.";
RL   Endocrinology 138:433-439(1997).
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: Expressed in adult and fetal steroidogenic tissues,
CC       including adult testes and ovaries and adult adrenal glands as well as
CC       steroidogenic tissues of pregnancy, including developing fetal testes,
CC       corpus luteum, and pregnancy, but not in the fetal ovary.
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DR   EMBL; U53020; AAB04953.1; -; mRNA.
DR   EMBL; AY368628; AAQ76091.1; -; mRNA.
DR   EMBL; U72195; AAB50555.1; -; mRNA.
DR   AlphaFoldDB; Q28996; -.
DR   SMR; Q28996; -.
DR   STRING; 9823.ENSSSCP00000020269; -.
DR   PaxDb; Q28996; -.
DR   eggNOG; KOG3845; Eukaryota.
DR   InParanoid; Q28996; -.
DR   UniPathway; UPA00296; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   2: Evidence at transcript 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_0000033319"
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        188
FT                   /note="R -> G (in Ref. 1; AAB04953)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  31932 MW;  26C102B7E4CE7413 CRC64;
     MLLATFKLCA GSSYRHVRNM KGLRHQAVLA LGQELNRRAL GGPTSGSWIN QVRRRSSLLG
     SQLEDTFYSD QDLAYIQQGE EAMQRALDIL SNQEGWKKES RQENGDEVLS KVIPDVGKVF
     RLEVVVDQPM ERLYEELVER MEAMGEWNPS VKKIKILQKI GKDTVITHEL AAEAAGNLVG
     PRDFVSVRCT KRRGSVCVLA GMATDFGEMP EQKGVIRAEH GPTCMVLHPL AGSPSKTKLT
     WLLSIDLKGW LPKTIINQVL SQTQVDFANH LRKRLESRPA LEARC