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SAV_DROME
ID   SAV_DROME               Reviewed;         608 AA.
AC   Q9VCR6; Q8MQH6; Q8T9A6; Q9VCR5;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Scaffold protein salvador;
DE   AltName: Full=Shar-pei;
GN   Name=sav; Synonyms=SHRP; ORFNames=CG33193;
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|EMBL:AAL39999.1};
RN   [1] {ECO:0000312|EMBL:AAM97280.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH WTS.
RX   PubMed=12202036; DOI=10.1016/s0092-8674(02)00824-3;
RA   Tapon N., Harvey K.F., Bell D.W., Wahrer D.C.R., Schiripo T.A., Haber D.A.,
RA   Hariharan I.K.;
RT   "Salvador promotes both cell cycle exit and apoptosis in Drosophila and is
RT   mutated in human cancer cell lines.";
RL   Cell 110:467-478(2002).
RN   [2] {ECO:0000305}
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   [3] {ECO:0000305}
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   [4] {ECO:0000305}
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   [5]
RP   FUNCTION.
RX   PubMed=12421711; DOI=10.1242/dev.00168;
RA   Kango-Singh M., Nolo R., Tao C., Verstreken P., Hiesinger P.R.,
RA   Bellen H.J., Halder G.;
RT   "Shar-pei mediates cell proliferation arrest during imaginal disc growth in
RT   Drosophila.";
RL   Development 129:5719-5730(2002).
RN   [6]
RP   FUNCTION WITH HPO.
RX   PubMed=12941274; DOI=10.1016/s0092-8674(03)00557-9;
RA   Harvey K.F., Pfleger C.M., Hariharan I.K.;
RT   "The Drosophila Mst ortholog, hippo, restricts growth and cell
RT   proliferation and promotes apoptosis.";
RL   Cell 114:457-467(2003).
RN   [7]
RP   PHOSPHORYLATION BY HPO.
RX   PubMed=12941273; DOI=10.1016/s0092-8674(03)00549-x;
RA   Wu S., Huang J., Dong J., Pan D.;
RT   "hippo encodes a Ste-20 family protein kinase that restricts cell
RT   proliferation and promotes apoptosis in conjunction with salvador and
RT   warts.";
RL   Cell 114:445-456(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-416, AND
RP   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).
RN   [9]
RP   INTERACTION WITH JUB.
RX   PubMed=20303269; DOI=10.1016/j.cub.2010.02.035;
RA   Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B.,
RA   Longmore G.D.;
RT   "Ajuba LIM proteins are negative regulators of the Hippo signaling
RT   pathway.";
RL   Curr. Biol. 20:657-662(2010).
RN   [10]
RP   INTERACTION WITH KIBRA; MER AND HPO.
RX   PubMed=20159598; DOI=10.1016/j.devcel.2009.12.012;
RA   Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.;
RT   "Kibra functions as a tumor suppressor protein that regulates Hippo
RT   signaling in conjunction with Merlin and Expanded.";
RL   Dev. Cell 18:288-299(2010).
CC   -!- FUNCTION: Plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling
CC       pathway, a signaling pathway that plays a pivotal role in organ size
CC       control and tumor suppression by restricting proliferation and
CC       promoting apoptosis. The core of this pathway is composed of a kinase
CC       cascade wherein Hippo (Hpo), in complex with its regulatory protein
CC       Salvador (Sav), phosphorylates and activates Warts (Wts) in complex
CC       with its regulatory protein Mats, which in turn phosphorylates and
CC       inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling
CC       pathway inhibits the activity of the transcriptional complex formed by
CC       Scalloped (sd) and Yki and the target genes of this pathway include
CC       cyclin-E (cycE), diap1 and bantam. Required for cell cycle exit in eye
CC       imaginal disk and hid-induced apoptotic cell deaths that are part of
CC       normal retinal development. Activation of Drice in eye imaginal disk by
CC       either Hid or Rpr is almost completely blocked by Sav expression.
CC       {ECO:0000269|PubMed:12202036, ECO:0000269|PubMed:12421711,
CC       ECO:0000269|PubMed:12941274}.
CC   -!- SUBUNIT: Interacts with Wts via its WW domains. Interacts (via FBM
CC       motif) with Mer (via FERM domain). Interacts with Kibra. Interacts with
CC       Hpo (via SARAH domain). Interacts with jub.
CC       {ECO:0000269|PubMed:12202036, ECO:0000269|PubMed:20159598,
CC       ECO:0000269|PubMed:20303269}.
CC   -!- INTERACTION:
CC       Q9VCR6; Q8T0S6: hpo; NbExp=3; IntAct=EBI-145004, EBI-101858;
CC       Q9VCR6; Q6NPA6: par-1; NbExp=2; IntAct=EBI-145004, EBI-3415099;
CC   -!- TISSUE SPECIFICITY: Third instar larvae eye disk, expressed in a stripe
CC       in the morphogenetic furrow, decreases in the region of the second
CC       mitotic wave (SMW) and increases once again posterior to the SMW.
CC       {ECO:0000269|PubMed:12202036}.
CC   -!- PTM: Phosphorylated by Hpo. {ECO:0000269|PubMed:12941273,
CC       ECO:0000269|PubMed:18327897}.
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DR   EMBL; AY131211; AAM97280.1; -; mRNA.
DR   EMBL; AE014297; AAF56090.3; -; Genomic_DNA.
DR   EMBL; AY069854; AAL39999.1; -; mRNA.
DR   RefSeq; NP_788721.1; NM_176544.3.
DR   PDB; 6BN1; X-ray; 2.60 A; B=531-600.
DR   PDBsum; 6BN1; -.
DR   AlphaFoldDB; Q9VCR6; -.
DR   SMR; Q9VCR6; -.
DR   BioGRID; 76064; 59.
DR   DIP; DIP-18696N; -.
DR   IntAct; Q9VCR6; 3.
DR   STRING; 7227.FBpp0083749; -.
DR   iPTMnet; Q9VCR6; -.
DR   PaxDb; Q9VCR6; -.
DR   EnsemblMetazoa; FBtr0084356; FBpp0083749; FBgn0053193.
DR   GeneID; 252554; -.
DR   KEGG; dme:Dmel_CG33193; -.
DR   UCSC; CG33193-RA; d. melanogaster.
DR   CTD; 252554; -.
DR   FlyBase; FBgn0053193; sav.
DR   VEuPathDB; VectorBase:FBgn0053193; -.
DR   eggNOG; KOG1891; Eukaryota.
DR   InParanoid; Q9VCR6; -.
DR   OMA; VWTSDQR; -.
DR   OrthoDB; 284488at2759; -.
DR   PhylomeDB; Q9VCR6; -.
DR   Reactome; R-DME-390089; Formation of the Hippo kinase cassette.
DR   Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
DR   Reactome; R-DME-390150; DS ligand bound to FT receptor.
DR   SignaLink; Q9VCR6; -.
DR   BioGRID-ORCS; 252554; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 252554; -.
DR   PRO; PR:Q9VCR6; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0053193; Expressed in saliva-secreting gland and 21 other tissues.
DR   ExpressionAtlas; Q9VCR6; baseline and differential.
DR   Genevisible; Q9VCR6; DM.
DR   GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR   GO; GO:0106037; C:apicomedial cortex; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0060090; F:molecular adaptor activity; IGI:FlyBase.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0035329; P:hippo signaling; IDA:FlyBase.
DR   GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR   GO; GO:0072002; P:Malpighian tubule development; IMP:FlyBase.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:FlyBase.
DR   GO; GO:0046621; P:negative regulation of organ growth; TAS:FlyBase.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR   GO; GO:0045463; P:R8 cell development; IGI:FlyBase.
DR   GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IGI:FlyBase.
DR   GO; GO:0045570; P:regulation of imaginal disc growth; TAS:FlyBase.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:FlyBase.
DR   GO; GO:0046666; P:retinal cell programmed cell death; IMP:FlyBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
DR   GO; GO:0072089; P:stem cell proliferation; IMP:FlyBase.
DR   CDD; cd00201; WW; 1.
DR   InterPro; IPR011524; SARAH_dom.
DR   InterPro; IPR030030; Sav.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR47522; PTHR47522; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF51045; SSF51045; 2.
DR   PROSITE; PS50951; SARAH; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Coiled coil; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..608
FT                   /note="Scaffold protein salvador"
FT                   /id="PRO_0000076062"
FT   DOMAIN          423..456
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224,
FT                   ECO:0000305"
FT   DOMAIN          458..491
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224,
FT                   ECO:0000305"
FT   DOMAIN          552..599
FT                   /note="SARAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT   REGION          17..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          274..294
FT                   /evidence="ECO:0000255"
FT   MOTIF           32..38
FT                   /note="Ferm-binding motif (FBM)"
FT   COMPBIAS        17..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        119
FT                   /note="S -> A (in Ref. 4; AAL39999)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="L -> M (in Ref. 1; AAM97280)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="Missing (in Ref. 4; AAL39999)"
FT                   /evidence="ECO:0000305"
FT   HELIX           537..544
FT                   /evidence="ECO:0007829|PDB:6BN1"
FT   HELIX           555..557
FT                   /evidence="ECO:0007829|PDB:6BN1"
FT   HELIX           560..599
FT                   /evidence="ECO:0007829|PDB:6BN1"
SQ   SEQUENCE   608 AA;  68146 MW;  05DF47686EE3335E CRC64;
     MNYLTILLCN RKPTMLSRRN KEKSQHKEGV VGKYMKKDTP PDISVINVWS DQRAKKKSLQ
     RCASTSPSCE FHPRSSSTSR NTYSCTDSQP DYYHARRAQS QMPLQQHSHS HPHSLPHPSH
     PHVRSHPPLP PHQFRASSNQ LSQNSSNYVN FEQIERMRRQ QSSPLLQTTS SPAPGAGGFQ
     RSYSTTQRQH HPHLGGDSYD ADQGLLSASY ANMLQLPQRP HSPAHYAVPP QQQQHPQIHQ
     QHASTPFGST LRFDRAAMSI RERQPRYQPT SSPMQQQQQQ QQQQQQQLQH TQLAAHLGGS
     YSSDSYPIYE NPSRVISMRA TQSQRSESPI YSNTTASSAT LAVVPQHHHQ GHLAVPSGSG
     GGSLSGSGRG GSSGSVRGAS TSVQSLYVPP RTPPSAVAGA GGSANGSLQK VPSQQSLTEP
     EELPLPPGWA TQYTLHGRKY YIDHNAHTTH WNHPLEREGL PVGWRRVVSK MHGTYYENQY
     TGQSQRQHPC LTSYYVYTTS AEPPKAIRPE ASLYAPPTHT HNALVPANPY LLEEIPKWLA
     VYSEADSSKD HLLQFNMFSL PELEGFDSML VRLFKQELGT IVGFYERYRR ALILEKNRRA
     GQNQNQNQ
 
 
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