ID   SIN1_DROME              Reviewed;         569 AA.
AC   Q9V719; Q53YG4;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Stress-activated map kinase-interacting protein 1;
DE            Short=SAPK-interacting protein 1;
DE            Short=dSin1;
GN   Name=Sin1; ORFNames=CG10105;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
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   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=16919458; DOI=10.1016/j.cub.2006.08.001;
RA   Frias M.A., Thoreen C.C., Jaffe J.D., Schroder W., Sculley T., Carr S.A.,
RA   Sabatini D.M.;
RT   "mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define
RT   three distinct mTORC2s.";
RL   Curr. Biol. 16:1865-1870(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-355; SER-372 AND
RP   SER-504, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Component of a multiprotein complex that phosphorylates Akt1,
CC       a protein that regulates the balance between cell survival and
CC       apoptosis through a cascade that primarily alters the function of
CC       transcription factors that regulate pro- and antiapoptotic genes.
CC       {ECO:0000269|PubMed:16919458}.
CC   -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF58247.1; -; Genomic_DNA.
DR   EMBL; BT003261; AAO25018.1; -; mRNA.
DR   RefSeq; NP_610963.1; NM_137119.4.
DR   AlphaFoldDB; Q9V719; -.
DR   SMR; Q9V719; -.
DR   BioGRID; 62354; 13.
DR   ComplexPortal; CPX-2269; TORC2 complex.
DR   IntAct; Q9V719; 16.
DR   MINT; Q9V719; -.
DR   STRING; 7227.FBpp0086616; -.
DR   iPTMnet; Q9V719; -.
DR   PaxDb; 7227-FBpp0086616; -.
DR   DNASU; 36604; -.
DR   EnsemblMetazoa; FBtr0087487; FBpp0086616; FBgn0033935.
DR   GeneID; 36604; -.
DR   KEGG; dme:Dmel_CG10105; -.
DR   AGR; FB:FBgn0033935; -.
DR   CTD; 36604; -.
DR   FlyBase; FBgn0033935; Sin1.
DR   VEuPathDB; VectorBase:FBgn0033935; -.
DR   eggNOG; KOG3739; Eukaryota.
DR   GeneTree; ENSGT00390000000642; -.
DR   HOGENOM; CLU_514767_0_0_1; -.
DR   InParanoid; Q9V719; -.
DR   OMA; NAKFWPQ; -.
DR   OrthoDB; 49453at2759; -.
DR   PhylomeDB; Q9V719; -.
DR   Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR   BioGRID-ORCS; 36604; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 36604; -.
DR   PRO; PR:Q9V719; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033935; Expressed in cleaving embryo and 22 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031932; C:TORC2 complex; IGI:FlyBase.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:FlyBase.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:FlyBase.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:FlyBase.
DR   GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IMP:FlyBase.
DR   GO; GO:0034063; P:stress granule assembly; IMP:FlyBase.
DR   GO; GO:0038203; P:TORC2 signaling; IGI:FlyBase.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR031567; CRIM_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR008828; Sin1/Avo1.
DR   InterPro; IPR032679; Sin1_N.
DR   InterPro; IPR031313; Sin1_PH_dom.
DR   PANTHER; PTHR13335; TARGET OF RAPAMYCIN COMPLEX 2 SUBUNIT MAPKAP1; 1.
DR   PANTHER; PTHR13335:SF1; TARGET OF RAPAMYCIN COMPLEX 2 SUBUNIT MAPKAP1; 1.
DR   Pfam; PF16978; CRIM; 1.
DR   Pfam; PF05422; SIN1; 1.
DR   Pfam; PF16979; SIN1_PH; 1.
DR   Genevisible; Q9V719; DM.
PE   1: Evidence at protein level;
KW   Apoptosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..569
FT                   /note="Stress-activated map kinase-interacting protein 1"
FT                   /id="PRO_0000218772"
FT   REGION          52..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   569 AA;  64239 MW;  BD18DC6186C4E665 CRC64;
     MATYSNQHWL LSHIRNSFIS TDDTGMCETV MLSDDMPKHY LRKFGNSGAG GDHYHWRRAH
     KTPPTGGGTT PERNTRHPDA PLQEVDFICY PGLDLSDDEE DMSTHSFDIQ MYPEVGAHRF
     RSNTAQKLEK LDIAKRRAAR IKSVNYQEEV QPPESDDFFK RKELPLSKAE RVKNEPKAND
     DDLSDEGVQS QLTEQLAKSP KQAQNRFIEF ARFDGTSQVG MQTKRINVFL NMLPEPDRNY
     PLKICVVATA KIQEVIGFVC YRTSLQYPDV PLKSLQHYAL YMTEDNDDME DFPPLDNREP
     CSKFGFSQLT LAERRPLAPV TRVDYHSQLG SKSMTSVEDK TALSDAAVKA LQNISLNGGT
     SDPGGGGGGG DSPHDNVKEY EKRLLNHNDM LEAPMHRTFR LNIIDKRFFK SDVTLGISGE
     RIEIDQCKNA KFWPQKKPVS TPIDFVAHCE ILERRHLKAL LRIWLKSNSS SPSFSTGCTS
     APINASVTTL NAGSGSGGIA HSPSSPGHSS GLFSSSNIRF KHYDFDTDTH TAEQIHNKLN
     CILEMRSSDL RREFLLQRDR KQEKRQLKL
//