KIBRA_DROAN
ID KIBRA_DROAN Reviewed; 1271 AA.
AC B3LWS4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein kibra;
GN Name=Kibra; ORFNames=GF18133;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV42712.1; -; Genomic_DNA.
DR RefSeq; XP_001954151.1; XM_001954115.2.
DR AlphaFoldDB; B3LWS4; -.
DR SMR; B3LWS4; -.
DR STRING; 7217.FBpp0121325; -.
DR EnsemblMetazoa; FBtr0122833; FBpp0121325; FBgn0095151.
DR GeneID; 6500911; -.
DR KEGG; dan:6500911; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR HOGENOM; CLU_005420_1_0_1; -.
DR InParanoid; B3LWS4; -.
DR OMA; HHTHIPR; -.
DR OrthoDB; 364990at2759; -.
DR PhylomeDB; B3LWS4; -.
DR ChiTaRS; kibra; fly.
DR Proteomes; UP000007801; 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; cd00201; WW; 2.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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..1271
FT /note="Protein kibra"
FT /id="PRO_0000392968"
FT DOMAIN 45..78
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 92..125
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 685..805
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..223
FT /evidence="ECO:0000255"
FT COILED 326..454
FT /evidence="ECO:0000255"
FT COILED 1039..1066
FT /evidence="ECO:0000255"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..896
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 142669 MW; D9EF46FF70F6117D CRC64;
MPNQSQHHLQ PHPHHLRPQQ QQQQQQQQQQ QQHHRQQQQQ NHSDFPLPDG WDIAKDFDGK
TYYIDHINKK TTWLDPRDCY TKPQTFEDCV GDELPMGWEE SYDPNIGLYY INHLAQSTQL
EDPRQEWKSV QEQMLSDYLS AAQDQLENKR EMFDVKQQRL LWAQEEYNHL KLAASRSSLC
SSSSSMSRHD PELLRADLML ARERVHQLKQ ELNHITNDIS YTERGMNTLY SVGEKINARQ
NGCYDIAEVQ AIREEMLKVH KSLVSGEKVR EELMRSLVQI KNELSRQQIS EENSDLASPF
DRVCVASQTD LCGSTGDNLN GGARFAEMAK TKLQYAEWRK HIKKLQQQLA DHVERIEPGQ
LESDKDRILL IQEKEKLLND LNSISLKSRS EEEKRVIQQT RNKLEEDLKE AYEANNTCVA
NRLRFHEEKQ LLLDKLQEAL KSTKLLEERL KSFSSESTFS ISSGSSLGSL STASSKSALS
FTDIYIDPFA VDSPIDVVDL RRRSQRLFQQ HQRLHPVHPG LQQQQQQQQQ SSEVSLSPRS
SLSMETPPAS PMKYNPGADP TTPALKEEPT YANALPAPPA YTAPPPVPVS GVRARPYDLD
STVLDCMMLE AKLQKLNLGT PLNLAAAPLS PISEKPSLLD LPQEMLSRSS STSNTRSVSA
AVSNESVAGD SGVFEASRAH LPRKELAQVQ IGLKYLKLEG VLVVSLERAN NLLALWTASA
DNSQVYLRAA LLPNSLTSIR TKALGDFQKP VFNDTFAVPI TLDKLLTKSL QVTVVTMTGQ
KEEIIGTVQI SMAEFNPEDS TLKWYNVLSS KFIPTFESLD LPSTSAAAAA VAVAASSSAS
NSIREESSDE STITSSQTST LTRNQAPPME LQAQIAEEQP EQDGSDDDDD DDEEEDDNNK
KIIREVAVGL MNSGCMLDTY LQNMKQEFAD KETNTDCAFL PEKSRGQSQM MDDRPVKRSQ
TFTPSAAVSK NRYNCRLNRS DSDSAMHCGV APHTFQRGAA ERRSLRFHTK APKSVTKLHH
THIPRTSLDL ELDLQAQHSK LYFLNDQIAK LQNLKEVLQK ACENKDPLIA AWAIENEEFQ
RLVARADPAK CPEERQLQKL LMKTAKEIHK LRKTKVPKGC PDLVSFKEKI TFFTRKGMSV
PELPSEFTLP EANPIEEEEE EEEEDEDEFY NAAETAIAIN TALVASNNRN KNLTDHLNRV
SNYAAPKPPT IPAPPAASPA APAGSNPPSA TPSTTPATQA TTTAVPVPAD DNNPEQQRYD
YVVDRTYGVE V
