STRT1_DROME
ID STRT1_DROME Reviewed; 583 AA.
AC Q9W145; Q8MZH4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Steroidogenic acute regulatory protein-like {ECO:0000305};
GN Name=Start1 {ECO:0000312|FlyBase:FBgn0035028};
GN ORFNames=CG3522 {ECO:0000312|FlyBase:FBgn0035028};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAR19767.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=14745013; DOI=10.1073/pnas.0308212100;
RA Roth G.E., Gierl M.S., Vollborn L., Meise M., Lintermann R., Korge G.;
RT "The Drosophila gene Start1: a putative cholesterol transporter and key
RT regulator of ecdysteroid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1601-1606(2004).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAM27512.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM27512.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May bind to and transport cholesterol and may play a role in
CC ecdysteroid biosynthesis. {ECO:0000303|PubMed:14745013}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0035028}; Synonyms=C
CC {ECO:0000312|FlyBase:FBgn0035028};
CC IsoId=Q9W145-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0035028};
CC IsoId=Q9W145-2; Sequence=VSP_058446, VSP_058447;
CC -!- TISSUE SPECIFICITY: Expressed in larval prothoracic gland cells (at
CC protein level). Detected in larval ring gland, imaginal disk and
CC salivary gland and in adult head, ovary and testis. Expressed in nurse
CC cells of stage 10 egg chambers in 2-day-old adult ovary. No expression
CC detected in adult brain. {ECO:0000269|PubMed:14745013}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo from stage 16. In the
CC larva, abundant at the end of both the second and third instar but is
CC almost undetectable in freshly hatched third instar larvae and declines
CC in white prepupae. Also expressed in the adult.
CC {ECO:0000269|PubMed:14745013}.
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DR EMBL; AY455866; AAR19767.1; -; mRNA.
DR EMBL; AE013599; AAF47232.2; -; Genomic_DNA.
DR EMBL; AE013599; AFH08248.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64770.1; -; Genomic_DNA.
DR EMBL; AY102683; AAM27512.1; -; mRNA.
DR RefSeq; NP_001246495.1; NM_001259566.2. [Q9W145-1]
DR RefSeq; NP_611936.2; NM_138092.3. [Q9W145-1]
DR RefSeq; NP_995939.1; NM_206217.3. [Q9W145-2]
DR AlphaFoldDB; Q9W145; -.
DR SMR; Q9W145; -.
DR IntAct; Q9W145; 2.
DR STRING; 7227.FBpp0088807; -.
DR TCDB; 9.B.64.1.2; the putative cholesterol transporter (start1) family.
DR PaxDb; Q9W145; -.
DR PRIDE; Q9W145; -.
DR DNASU; 37927; -.
DR EnsemblMetazoa; FBtr0089867; FBpp0088806; FBgn0035028. [Q9W145-2]
DR EnsemblMetazoa; FBtr0089868; FBpp0088807; FBgn0035028. [Q9W145-1]
DR EnsemblMetazoa; FBtr0305054; FBpp0293591; FBgn0035028. [Q9W145-1]
DR GeneID; 37927; -.
DR KEGG; dme:Dmel_CG3522; -.
DR UCSC; CG3522-RA; d. melanogaster. [Q9W145-1]
DR UCSC; CG3522-RB; d. melanogaster.
DR CTD; 112046; -.
DR FlyBase; FBgn0035028; Start1.
DR VEuPathDB; VectorBase:FBgn0035028; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000169699; -.
DR HOGENOM; CLU_033480_1_0_1; -.
DR InParanoid; Q9W145; -.
DR OMA; NQMGLDC; -.
DR PhylomeDB; Q9W145; -.
DR BioGRID-ORCS; 37927; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Start1; fly.
DR GenomeRNAi; 37927; -.
DR PRO; PR:Q9W145; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0035028; Expressed in oviduct (Drosophila) and 32 other tissues.
DR ExpressionAtlas; Q9W145; baseline and differential.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:FlyBase.
DR GO; GO:0015485; F:cholesterol binding; ISS:FlyBase.
DR GO; GO:0030301; P:cholesterol transport; ISS:FlyBase.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 3.30.530.20; -; 2.
DR InterPro; IPR019498; MENTAL.
DR InterPro; IPR000799; StAR-like.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF10457; MENTAL; 1.
DR Pfam; PF01852; START; 2.
DR PRINTS; PR00978; STARPROTEIN.
DR PROSITE; PS51439; MENTAL; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid transport; Lipid-binding; Membrane;
KW Reference proteome; Steroidogenesis; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..583
FT /note="Steroidogenic acute regulatory protein-like"
FT /id="PRO_0000436917"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 85..104
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 128..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 154..161
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 183..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 56..227
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT DOMAIN 263..573
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT VAR_SEQ 510..545
FT /note="RGQNIVSGFAFREIVGKSDSCIVEWVLCLDLKGYIP -> SRLTLQFSEGRT
FT LSVGLRFVKSLENRIAALWSGCFA (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_058446"
FT VAR_SEQ 546..583
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_058447"
SQ SEQUENCE 583 AA; 65823 MW; F043047A5ADD6FF1 CRC64;
MSNMDPSDVR STAQLILANA RQGNSAYNMQ YDMSRAHSIN LITEDFLAGY MQDGRMSVVR
RFFCLFVTFD LVFVSLLWLI CIVINGDNIF TAFHKQIVEY TIYKSLFDVV AVAICRFLVL
IFFYAILYIN HWSIIALSTS GSCLFLISKV FVFDWLDSKQ QVFEVILIIT SFILAWGEAW
FLDCRVIPQE RHAQHYFRTM TSNDRTPMEQ PAILIEQERP PQSVTDFYSL MDTARHSDEE
DELDDEYTQM GLDCLRKAYE IIESSDWKVE KVNQKGDTIH STQRDKIGKI YKLTARIKYP
AKALMEDLFY RIEDCPKWNP ALLESKIVRK INSYTDITYQ VSVGGGGGMV KSRDFVNLRS
CRLFYNGQIC DDDETAQLSS DDGNSSLNRS CEGSVSTISD GDSNTPLLPS SVSSCKATFP
TSSKGAAMPF DTLGNSLGAK SLGPIVNFDE EPPPLDQDEF EDAKDKVDGE ANNMTKPNVP
SVGKTKDRVW VTSAVSVQYA AVPPSPKYTR GQNIVSGFAF REIVGKSDSC IVEWVLCLDL
KGYIPRYVLD AALTSSMTDY ISNLRKHVNE LRQKGRGRAP RTH
