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