KIBRA_DROMO
ID KIBRA_DROMO Reviewed; 1264 AA.
AC B4K6I9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein kibra;
GN Name=Kibra; ORFNames=GI10447;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW16289.1; -; Genomic_DNA.
DR RefSeq; XP_002000828.1; XM_002000792.2.
DR AlphaFoldDB; B4K6I9; -.
DR STRING; 7230.FBpp0159664; -.
DR PRIDE; B4K6I9; -.
DR EnsemblMetazoa; FBtr0161172; FBpp0159664; FBgn0133211.
DR GeneID; 6574800; -.
DR KEGG; dmo:Dmoj_GI10447; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR HOGENOM; CLU_005420_1_0_1; -.
DR InParanoid; B4K6I9; -.
DR OMA; HHTHIPR; -.
DR OrthoDB; 364990at2759; -.
DR PhylomeDB; B4K6I9; -.
DR ChiTaRS; kibra; fly.
DR Proteomes; UP000009192; 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; 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; 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;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1264
FT /note="Protein kibra"
FT /id="PRO_0000392972"
FT DOMAIN 35..68
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 82..115
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..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..215
FT /evidence="ECO:0000255"
FT COILED 258..288
FT /evidence="ECO:0000255"
FT COILED 319..445
FT /evidence="ECO:0000255"
FT COMPBIAS 1234..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 142031 MW; 7620137734FCA74F CRC64;
MSNQQQQQLP RQLPQPHPHH HHHHHQQQPG QHSEFPLPDG WDIARDFDGK TYYIDHINKK
TTWLDPRDRY TKPQSFEDCV GDELPVGWEE AYDSNIGRYY INHIAQTTQL EDPRQEWKSV
QEQMLSDYLS AAQDQLENKR EMYDVKQQRL NLAQEEYNHL NKLAASRSSL CSSSSSMSRH
DPELLRADLM LARERVRQLK QELNHITNDI SYTERGMNTL YSVGEKINAR QNGCYDIAEV
QAIREEMLKV HKSLVSGEKV REELMRSLVQ IKNELSRQQI NEENAELLSA TSPFDRVCVA
SQTDLCGAGE HLNGGARFAE MAKTKLQYAE WRKHIKKLQQ QLADHVERIE PGQLESDKDR
ILLIQEKEKL LNDLNSISLK SRSAEEKLVI QQTRHKLEED LKEAYEATNT CVANRLRFHE
EKQLLLAKLQ EALKSTNLLE ERLKSFSSES TFSISSGSSL GSLSTASSKS ALSFTDIYID
PFAVGESPID VVDLQRRSQR LFQQHQRLPP VHPAVQLQQQ HQLQQQTQPQ PASEVSLSPR
SSLSIETPPA SPMKYNAIAD QPQAQAQAAL KEEPTYANAM PAPPAYTAPP SVPMALAAVR
THPYDLDSTV LDCMMLEAKL QKLNLSSPLN LNGPLSPISE KPSLLDLPQE MLSRSSSTSN
TRSVSAAVSN ESVAGDSGVF EASRAHLPRK ELAQVQIGLK YLKQEGVLVV SLERANNLSA
LWTATTDNSQ VYLRAALLPN SLTSIRTKAL GDFQKPVFND TFAVPISLDK LLTKSLQVTV
VTMTGQKEEI IGTVQISMAE FNPDDSTLKW YNVLSSKFIP TFESLDLPST SAAAAAAAVA
ASNNIINNNN NNNNNNIREE SSDESTITSS QTSTLTRNQA PPLELQAQIA EELPEHVRLN
EQQCSDDDDD DDEEEDEQQL VGTLGLTHSG CMLDAYLENM KQEYADKETN TDCAFPPEKL
RSQTQLLDDR PVKRSQTFTP SAAVSKNRYN CRLNRSDSDS AMHFGVTPHT FHRGAVERRS
LRFQPKATKS VTKLHHTHIP RTSLDLELDL QAQHSKLYFL NDQISKLQNL KEVLQKACDN
KDPLIAAWAI ENEEFQRLVA RADPTKCPEE RLLQKLLMKT TKEIHKLRKT KVPKGCPDLV
SFKEKMFFFT RKGMSVPELP NDFLLPDAQA IEEEEEDDDE DNVAETAIAI NTALVASSNR
NKNLSEHHHR STGGAVSKLT ATPTPAINPA PVATPVPATS NANEANGEQQ RYDYVVDRNY
GVEV
