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KIBRA_DROYA
ID   KIBRA_DROYA             Reviewed;        1288 AA.
AC   B4PSQ2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein kibra;
GN   Name=Kibra; ORFNames=GE26432;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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. Kibra acts synergistically along with Ex and Mer to
CC       regulate the Hippo signaling pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with Mer and Ex. Interacts (via domain WW 1)
CC       with Ex (via RXPPXY motif). Interacts with Mer, Sav, Hpo and Wts (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Apical cell membrane
CC       {ECO:0000250}. Note=Localizes at the apical cortex of epithelial cells
CC       and cytoplasmic, punctate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily. {ECO:0000305}.
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DR   EMBL; CM000160; EDW97548.1; -; Genomic_DNA.
DR   RefSeq; XP_002097836.1; XM_002097800.2.
DR   AlphaFoldDB; B4PSQ2; -.
DR   STRING; 7245.FBpp0271442; -.
DR   EnsemblMetazoa; FBtr0272950; FBpp0271442; FBgn0243454.
DR   GeneID; 6537278; -.
DR   KEGG; dya:Dyak_GE26432; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; KOG3209; Eukaryota.
DR   HOGENOM; CLU_005420_1_0_1; -.
DR   OMA; HHTHIPR; -.
DR   OrthoDB; 364990at2759; -.
DR   PhylomeDB; B4PSQ2; -.
DR   ChiTaRS; kibra; fly.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0106037; C:apicomedial cortex; IEA:EnsemblMetazoa.
DR   GO; GO:0005911; C:cell-cell junction; IEA:EnsemblMetazoa.
DR   GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0036375; C:Kibra-Ex-Mer complex; IEA:EnsemblMetazoa.
DR   GO; GO:0007298; P:border follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:0046621; P:negative regulation of organ growth; IEA:EnsemblMetazoa.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblMetazoa.
DR   GO; GO:0035332; P:positive regulation of hippo signaling; ISS:UniProtKB.
DR   GO; GO:0045463; P:R8 cell development; IEA:EnsemblMetazoa.
DR   GO; GO:0045464; P:R8 cell fate specification; IEA:EnsemblMetazoa.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:EnsemblMetazoa.
DR   CDD; cd08680; C2_Kibra; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037771; C2_WWC.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF51045; SSF51045; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Coiled coil; Cytoplasm; Membrane; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..1288
FT                   /note="Protein kibra"
FT                   /id="PRO_0000392976"
FT   DOMAIN          54..87
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          101..134
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          691..811
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1253..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          201..229
FT                   /evidence="ECO:0000255"
FT   COILED          335..463
FT                   /evidence="ECO:0000255"
FT   COILED          1049..1076
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..870
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..912
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1288 AA;  144094 MW;  0175729B491F02F7 CRC64;
     MPNLQQTASQ SQSQHHLHPH HLRPHQQQHH QQQQQQQQQQ HTHHQQQQQH HSDFPLPDGW
     DIAKDFDGKT YYIDHINKKT TWLDPRDCYT KPQTFEDCVG DELPMGWEES YDPNIGPYYI
     NHLAQSTQLE DPRQEWKTVQ EQMLSDYLSA AQDQLENKRE MFDVKQQRLL WAQEEYNHLK
     LAASRSSLCS SSSSMSRHDP ELLRADLMLA RERVHQLKQE LTHITNDISY TERGMNTLYS
     VGEKINAREN GCYDIAEVQA IREEMLKVHK SLVSGEKVRE ELMRSLVQIK NELGRQQISE
     ENSDLASPFD RVCVASQTDL CGSSGDNLNG GARFAEMAKT KLQYAEWRKH IKKLQQQLAD
     HVERIEPGQL ESDKDRILLI QEKEKLLNDL NSISLKSRSE EEKRVIHQTR HKLEEDLKEA
     YEANNTCVAN RLRFHEEKQL LLDKLQEALK STKLLEERLK SFSSESTFSI SSGSSLGSLS
     TASSKSALSF TDIYIDPFAV DSPIDVVDLR RRSQRLFQQH QQQRLHPVHP VLQQQQSAEV
     TLSPRSSLSM ETPPASPMKY NAGADQTPQA LKEEPTYANA LPAPPAYTAP PPVPISGVRA
     RPYDLDSTVL DCMMLEAKLQ KLNMGTPLNL AAAPLSPISE KPSLLDLPQE MLSRSSSTSN
     TRSVSAAVSN ESVAGDSGVF EASRAHLPRK ELAQVQIGLK YLKQEGVLVV SLERANNLLA
     LWTASADNSQ VYLRAALLPN SLTSIRTKAL GDFQKPVFND TFAVPITLDK LLTKSLQVTV
     VTMTGQKEEI IGTVQISMAE FNPEDSTLKW YNVLSSKFIP SFESLDIPST SAAAAAAAVA
     ASNAPNSGNN REESSDESTI TSSQTSTLTR NQAPCMELQE QIAAELLELG PLNEPECSDD
     DDDDEEEELD DKQLVSDVGL MNSSGMLDAY LQNMKQEFAD KETNTDRAYL PEKSRGQSQL
     MDDRPVKRSQ TFTPSAAVSK NRYNCRLNRS DSDSAMHCGV APHTFQRGAA ERRSLRFHTK
     APKSVTKLHH THIPRTSLDL ELDLQAQHSK LYFLNDQIAK LQNLKEVLQK ACENKDPLVA
     AWAIENEEFQ RLVARADPAK CPEERQLQKL LMKTAKEIHK LRKTKVPKGC PDLVSFKEKI
     TFFTRKGLSV PELPSEFTLP EANPIEEEEE EEDEDEFYNS AETAIAINTA LVASSNRNKN
     LSEHPHRATS GAVPKLPAPV ATPAATPAAT PVATPVATPV ATPAATPVVS PAVQTDAKPA
     AAPIPVASSD AEQQRFDYVV DRNYGVEV
 
 
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