KIBRA_DROVI
ID KIBRA_DROVI Reviewed; 1276 AA.
AC B4M5X4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein kibra;
GN Name=Kibra; ORFNames=GJ10664;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940652; EDW59050.1; -; Genomic_DNA.
DR RefSeq; XP_002055938.1; XM_002055902.2.
DR AlphaFoldDB; B4M5X4; -.
DR SMR; B4M5X4; -.
DR STRING; 7244.FBpp0225081; -.
DR EnsemblMetazoa; FBtr0226589; FBpp0225081; FBgn0197942.
DR GeneID; 6633021; -.
DR KEGG; dvi:6633021; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR HOGENOM; CLU_005420_1_0_1; -.
DR InParanoid; B4M5X4; -.
DR OMA; HHTHIPR; -.
DR OrthoDB; 364990at2759; -.
DR PhylomeDB; B4M5X4; -.
DR ChiTaRS; kibra; fly.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035332; P:positive regulation of hippo signaling; ISS:UniProtKB.
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..1276
FT /note="Protein kibra"
FT /id="PRO_0000392974"
FT DOMAIN 43..76
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 90..123
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 697..817
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 137..219
FT /evidence="ECO:0000255"
FT COILED 266..298
FT /evidence="ECO:0000255"
FT COILED 327..455
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..921
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 143315 MW; AFB6A7F6DAD31873 CRC64;
MSNQQQQQQQ QQQPRQHPQP HPHHHHHHLH HHHQQQPGQH SEFPLPEGWD IARDFDGKTY
YIDHINKKTT WLDPRDRYTK PQSFEDCVGD ELPVGWEEAY DSNIGRYYIN HIAQSTQLED
PRQEWKSVQE QMLSDYLSAA QDQLENKREM YDVKQQRLNL AQEEYNHLNK LAASRSSLCS
SSSSMSRHDP ELLRADLMLA RERVRQLKQE LTHITNDISY TERGMNTLYS VGEKINARKN
GCYDIAEVQA IREEMLKVHK SLVSGEKVRE ELMRSLVQIK NELSRQQINE ENAELMSAAS
PFDRVCVASQ TDLCGAGEHL NGGARFAEMA KTKLQYAEWR KHIKKLQQQL ADHVERIEPG
QLESDKDRIL LIQEKEKLLN DLNSISLKSR SAEEKQVIQQ TRHKLEEDLK EAYEATNTCI
ANRLRFHEEK QLLLDKLQEA LKSTKLLEER LKSFSSESTF SISSGSSLGS LSTASSKSAL
SFTDIYIDPF AVGESPIDVV DLQRRSQRLF QQHQRLPPVH PALQQQQQTQ PLASSEVSLS
PRSSLSMETP PASPMKYNAV ADQPQAQAKL KEEPTYANAL PALPTIPAPP AYAAPPAIPL
ALAAVRAHPY DLDSTVLDCM MLEAKLQKLN LGSPLNLNGP LSPISEKPSL LDLPQEMLSR
SSSTSNTRSV SAAVSNESVA GDSGVFEASR AHLPRKELAQ VQIGLKYLKQ EGVLVVSLER
ANNLSALWTA TTDNSQVYLR AALLPNSLTS IRTKALSDFQ KPVFNDTFAV PISLDKLLTK
SLQVTVVSMT GQKEEIIGTV QISMAEFNPE DSTLKWYNVL SSKFIPSFES LDLPSTSAAA
AAAAVAASNS NNNNSNTNNR EESSDESTIT SSQTSTLTRN QAPPLELQAQ IAEELPEHVR
HNEQQCSDDD DDDDEEEDEQ QLVGTLGLTH SGCMLDAYLE NMKQEYADKE TNTDCAFPPE
KLRSQSQLLD DRPVKRSQTF TPSAAVSKNR YNCRLNRSDS DSAMHFGVTP HTFHRGAVER
RSLRFQPKAT KSVTKLHHNH IPRTSLDLEL DLQAQHSKLF FLNDQISKLQ NLKEVLQKAC
DNKDPLIAAW AIENEEFQRL VARADPAKFP EERLLQKLLM KTTKEIHKLR KTKVPKGAPD
LVSFKEKISF FTRKGMSVPE LPIEFMHPDA DAIEEEEEDD NDDEEDNVVE TAIAINTALV
ASSNRNKNLS EHHHRSTDGA LSKLAATLTP AINPAPVSAP IPVAVSVPVA APLADEAKPE
QQRYDYVVDR NYGVEV