位置:首页 > 蛋白库 > SCHI1_DROME
SCHI1_DROME
ID   SCHI1_DROME             Reviewed;         616 AA.
AC   A8DYY6;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Schwannomin-interacting protein 1 homolog {ECO:0000303|PubMed:26954546};
GN   Name=Schip1 {ECO:0000303|PubMed:26954546};
GN   ORFNames=CG5375 {ECO:0000312|FlyBase:FBgn0032221};
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|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   [2] {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   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH EX; MER AND TAO, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=26954546; DOI=10.1016/j.devcel.2016.02.004;
RA   Chung H.L., Augustine G.J., Choi K.W.;
RT   "Drosophila Schip1 links Expanded and Tao-1 to regulate hippo signaling.";
RL   Dev. Cell 36:511-524(2016).
CC   -!- FUNCTION: Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a
CC       signaling pathway that plays a pivotal role in organ size control and
CC       tumor suppression by restricting proliferation and promoting apoptosis.
CC       The core of this pathway is composed of a kinase cascade wherein Hippo
CC       (hpo), in complex with its regulatory protein Salvador (sav),
CC       phosphorylates and activates Warts (wts) in complex with its regulatory
CC       protein Mats, which in turn phosphorylates and inactivates the Yorkie
CC       (yki) oncoprotein. Schip1 promotes kinase activity of Tao and enhances
CC       phosphorylation of hpo by Tao. {ECO:0000269|PubMed:26954546}.
CC   -!- SUBUNIT: Interacts with ex; the interaction results in recruitment of
CC       Schip1 to the apical cell membrane. Interacts with Tao; the interaction
CC       enhances Tao kinase activity. Interacts with Mer.
CC       {ECO:0000269|PubMed:26954546}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000269|PubMed:26954546}. Apical cell membrane
CC       {ECO:0000269|PubMed:26954546}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In eye disks of the third instar larvae, expressed
CC       in all cells (at protein level). {ECO:0000269|PubMed:26954546}.
CC   -!- DISRUPTION PHENOTYPE: Death during embryonic or early larval stages.
CC       Inactivation in adult eyes results in enlarged eyes with irregular
CC       bulging on the surface. {ECO:0000269|PubMed:26954546}.
CC   -!- SIMILARITY: Belongs to the SCHIP1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014134; ABV53662.1; -; Genomic_DNA.
DR   RefSeq; NP_001097139.1; NM_001103669.2.
DR   AlphaFoldDB; A8DYY6; -.
DR   SMR; A8DYY6; -.
DR   STRING; 7227.FBpp0111946; -.
DR   PaxDb; A8DYY6; -.
DR   EnsemblMetazoa; FBtr0113033; FBpp0111946; FBgn0032221.
DR   GeneID; 34393; -.
DR   KEGG; dme:Dmel_CG5375; -.
DR   UCSC; CG5375-RB; d. melanogaster.
DR   CTD; 29970; -.
DR   FlyBase; FBgn0032221; Schip1.
DR   VEuPathDB; VectorBase:FBgn0032221; -.
DR   eggNOG; KOG4847; Eukaryota.
DR   GeneTree; ENSGT00390000011127; -.
DR   HOGENOM; CLU_444300_0_0_1; -.
DR   InParanoid; A8DYY6; -.
DR   OMA; HDERQLP; -.
DR   OrthoDB; 357946at2759; -.
DR   PhylomeDB; A8DYY6; -.
DR   BioGRID-ORCS; 34393; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 34393; -.
DR   PRO; PR:A8DYY6; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032221; Expressed in brain and 7 other tissues.
DR   ExpressionAtlas; A8DYY6; baseline and differential.
DR   Genevisible; A8DYY6; DM.
DR   GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
DR   GO; GO:0035332; P:positive regulation of hippo signaling; IMP:UniProtKB.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR   InterPro; IPR039045; SCHIP_1.
DR   InterPro; IPR015649; SCHIP_1_C.
DR   PANTHER; PTHR13103; PTHR13103; 1.
DR   Pfam; PF10148; SCHIP-1; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Coiled coil; Membrane; Reference proteome.
FT   CHAIN           1..616
FT                   /note="Schwannomin-interacting protein 1 homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436305"
FT   REGION          38..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          550..594
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        57..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  70514 MW;  EF0B944CBFA82C44 CRC64;
     MDIYITKGIT NPNYPGFQKF AHTLSDDYIE YSDMECNESD LTDSDREDDP TFPSKMAKES
     GSETFKNGQD SILSNCDNGN TYISEEESVN RSENIPDIVN ENYSATSENS KRALQKPDLI
     YNLSQNYTTN PEFPSWSCTI NSKYEGQLQG QSPIDIVGDF GGEVEREFEL LLTGYKNKKE
     ADELKGSNLD KICDAELSNG TEALKQTSST RLSGNSTRKN KKKNTPYGHQ IVKTKHPKPS
     HDERQLPPDT FDYKTYSQRK YIICDADQYS SVPEKNKNDS PNLNQAEIPN MSSLEIGGSG
     SQQNLDEDNN KVASRKYSNQ SRWSQYLEDP IKYSKDPCST MVLEQFDAYK IANDMDVETL
     QNHYKKVKQI EKKRRFNRDE IRKRLAIGDK DSLNNDIKKE EFLTGSDNES YSSDSETCPK
     LSSGVLRKQS EFCETKRNKE FENDKIFQKN QINQDKSMNH MNGNPIGTTD YPSDENLFFF
     ANQSKLQIEV RIALAQSKEI AQMKVKARKH GVTPIVDVIR SMLCDVGIKM NSNHRWISRQ
     LLTGIQVPTL QLLVNNLQEY IENLNVTLLE SLKERDDLNS DQDDILHDLE KINNFFVFQQ
     QSGQQVNKIV RHGHLD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024