KIBRA_DROWI
ID KIBRA_DROWI Reviewed; 1288 AA.
AC B4NAD3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein kibra;
GN Name=Kibra; ORFNames=GK11691;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH964232; EDW80747.1; -; Genomic_DNA.
DR RefSeq; XP_002069761.2; XM_002069725.2.
DR AlphaFoldDB; B4NAD3; -.
DR SMR; B4NAD3; -.
DR STRING; 7260.FBpp0240834; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR HOGENOM; CLU_005420_1_0_1; -.
DR InParanoid; B4NAD3; -.
DR OMA; HHTHIPR; -.
DR OrthoDB; 364990at2759; -.
DR PhylomeDB; B4NAD3; -.
DR ChiTaRS; kibra; fly.
DR Proteomes; UP000007798; Unassembled WGS sequence.
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; 1.
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;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1288
FT /note="Protein kibra"
FT /id="PRO_0000392975"
FT DOMAIN 49..82
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 96..129
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 702..822
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 143..170
FT /evidence="ECO:0000255"
FT COILED 197..232
FT /evidence="ECO:0000255"
FT COILED 333..461
FT /evidence="ECO:0000255"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..934
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 144069 MW; 37E0A6CE4A43051A CRC64;
MSNLPQTQAH HLQPHPQHPQ HLLHHHQQQQ QQQQQQQQQQ HGHHNHSDFP LPDGWDIAKD
FDGKTYYIDH INKKTTWLDP RDRYTKPQSF EDCVGDELPV GWEEAYEPNI GRYYINHIAQ
STQLEDPRQE WKSVQEQMLS DYLSAAQDQL ENKREMYDVK QQRLLLAQEE YNHLNKLAAS
RSSLCSSSSS MSRHDPELLR ADLMLARERV RQLKQELNHI TNDISHTERG MNTLYSVGEK
INARENGCYD IAEVQAIREE MLKVHKSLVS GEKVREELMR SLVQIKNELS RQQMNEENAD
LLNAASPFDR VCVASQTDLC GAGESLNGGA RFAEMAKTKL QYAEWRKHIK KLQQQLADHV
ERIEPGQLES DKDRILLIQE KEKLLNDLNS ISLKSRSLEE TQVIQQTRQK LEDDLKEAYE
ANNTCIANRL RFHEEKQHLL DKLQEALKST KLLEERLKSF SSESTFSISS GSSLGSLSTA
SSKSALSFTD IYVDHFAVDS PIDVVDLQRR SQRFFQQQQQ QQQHRLPPVH GHPVLQQQQS
SEVSLSPRSS LSMETPPASP MKYNAGADQP QLPPAAASLA PPKEEPTYAN ALPAPPAYTA
PPPAPIAAVR APHAYDLDST VLDCMILEAK LKKLNLNSPL NLAAPLSPIS EKPSLLDLPQ
EMLSRSSSTS NTRSVSAAVS NESVAGDSGV FEASRAHLPR RELAQVQIGL KYLKQEGVLV
VSLERANNLL ALWTASSDNS QVYLRAALLP NSLTSIRTKA LGDFQKPVFN DTFAVPISLD
KLLTKSLQVT VVSMTGQKEE IIGTVQISMA EFNPDDSTLK WYNVLSSKFM PSFESLDIPS
TSAAAAAAAV AANNTNAMNS NSNNNREESS DESTITSSQT STLTRNQAPP LELQAQIAEE
LPEHVRLNEQ ECSDDDDDDD DDDDEEEEDE QQLIGTEELT NSSGMLDTYL KIMKQQYADK
ETNTECAFPP EKSRAQSQLL DDRPVKRSQT FTPSAAVSKS RYNCRLNRSD SDSAMHFGVT
PHTFHRGAAE RRSLRFHTKA PKTATKLHHT HIPRTSLDLE LDLQAQHSKL FFLNDQIAKL
QNLKDVLQKG CESKDPLIAA WAIENEEFQR LVARADPAKC PEERQLQKLL MKTAKEIHKL
RKTKVPKGCP DLVSFKEKIT FFTRKGLSVP ELPSEFILAD GDAIEEEEEE DDNAAETAIA
INTALVASSN RNKNLSEHHH RAACNSGAVP KRSATPTPIT AATTADASAS SAPATAAVAP
TTAATVSDDK PDQQRFDYVV DRNYGVEV
