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Database: UniProt
Entry: D6WLE2_TRICA
LinkDB: D6WLE2_TRICA
Original site: D6WLE2_TRICA 
ID   D6WLE2_TRICA            Unreviewed;      1260 AA.
AC   D6WLE2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein {ECO:0000256|ARBA:ARBA00019541};
GN   Name=AUGUSTUS-3.0.2_13456 {ECO:0000313|EMBL:EFA03461.2};
GN   ORFNames=TcasGA2_TC013456 {ECO:0000313|EMBL:EFA03461.2};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA03461.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA03461.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03461.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA03461.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03461.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004557}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the WD repeat SCAP family.
CC       {ECO:0000256|ARBA:ARBA00007410}.
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DR   EMBL; KQ971343; EFA03461.2; -; Genomic_DNA.
DR   RefSeq; XP_008193751.1; XM_008195529.2.
DR   RefSeq; XP_015835772.1; XM_015980286.1.
DR   AlphaFoldDB; D6WLE2; -.
DR   STRING; 7070.D6WLE2; -.
DR   EnsemblMetazoa; TC013456_001; TC013456_001; TC013456.
DR   GeneID; 663635; -.
DR   KEGG; tca:663635; -.
DR   eggNOG; KOG1933; Eukaryota.
DR   HOGENOM; CLU_006510_0_0_1; -.
DR   InParanoid; D6WLE2; -.
DR   OMA; IMKQYNV; -.
DR   OrthoDB; 2875749at2759; -.
DR   Proteomes; UP000007266; Linkage group 5.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032936; C:SREBP-SCAP complex; IBA:GO_Central.
DR   GO; GO:0032934; F:sterol binding; IEA:InterPro.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032933; P:SREBP signaling pathway; IEA:InterPro.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR030225; SCAP.
DR   InterPro; IPR000731; SSD.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR46378; STEROL REGULATORY ELEMENT-BINDING PROTEIN CLEAVAGE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR46378:SF1; STEROL REGULATORY ELEMENT-BINDING PROTEIN CLEAVAGE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF12349; Sterol-sensing; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50156; SSD; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
PE   3: Inferred from homology;
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   TRANSMEM        285..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        354..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        522..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        710..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          287..445
FT                   /note="SSD"
FT                   /evidence="ECO:0000259|PROSITE:PS50156"
FT   REPEAT          772..811
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1139..1178
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          828..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1260 AA;  143212 MW;  FE5B682EE1102137 CRC64;
     MNTRGDEPRP RGTFCGKSST LQEKVAQFYY AHGLFCSTYP GALVFVAICA TLLSCYPLLN
     LPLPGNSPLQ TWTSSVNSSS NVPPFCYIQQ VVLKSTVLPW GPELHLGDAF RAPLYEAFKL
     LEAVRNYQDE STKKTLGHVC LHVESIRKSK SNYKNILPEY SCLVLSPANL WQQDVLKFTQ
     DSSLLTTIFN HHNFQKGKTS ITEMMFGMKV FDTGIKRYPL RNRYRIIQYA ITLFFKEYDE
     KFVHGLRRKL QSVYSLHQNL ENGTNANFAT LNDTLIIQYP GEINLVEFIP ITLAFLILFL
     YFYFSFRKIE LIHSKLGMAF TSVLTVCASL TMTYGLCFFF GLTLNLEGKV VFPYLVLLVG
     LENVLCLTKS IVSSPLHLDV KIRIAQGLSK EGWSITKNLL LEITILTFGI FTFVAVIQEF
     CIFAVVGLVT DYFMQMIFFS TVLGIDIRRK ENMVERHNLS FRSSLFQSQV FYDKSFGIRR
     SKSHPRLSSF PANIVAGQVQ GAQEKKIPKR LKLVNIWTRT RFFHRAFMIL MVIWISNIAY
     NSGFIEHFIL NNSYFHEVAE QNSTSLEQNY SSIKLFPLLN TNNSFINKVS YVTHSPLNYN
     QNQTFDLENL KHSDYEPWLK LSPQHWSSIV RKYNLSLSGQ YIAILPNIKL SHVIRPEQAV
     LLRNPNEKYG EKFQWQALVA ALDPIDFNGM ETGTRSAIPQ SEQPFYPTSV FAMILIAILC
     FISVVVLGYT FVVLYRCICS RNYAEWRASW FSEKGEENVE EPVLLEAVPV VLEGHQQEIE
     CTATDGVNLV SASLDGQLKV WDSGTGELIA NVDRKAYFQG CFESNCGTSE CDDNSSDYES
     GSPPSRGESY LFPRLKHRIN TNFSNVKEQC NSYNAKADFL KTYRELYFVR DLPKAKSRKE
     MNRAKENKSI SFSESNQKFC DNGHTKFDSS DAKLSPIWCM DYLENLIVLG CADGRLEFWE
     GSSGRLKCIF EDGTDVGISN LKIVGSRIIA SRLYGTLEMF QLQTYNRGHP VDWNFTCAYR
     RTHVRTGSVG SVPDHTNLIS QNEDEEDFRC LKVFSVKAHQ QPIICLDCEG GRILTGSQDH
     TLKVFRLEDG SPQYTLHGHC GPITCLFIDR ISPATSGSGS QDGMLCVWDL LTGACMYNIQ
     AHDGTITSLT YSASYVISLG SDDRICVWER FQGHLLNTIY VSQTFSSQVL MLAPHLVVTA
     RSGGLVIWDV RSGECVRTII LGRSPYIFIK QLMLLRDAVV CDYGNQLRIV RFPLITHKFD
//
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