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Database: UniProt
Entry: B3LWS4
LinkDB: B3LWS4
Original site: B3LWS4 
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   29-OCT-2014, entry version 36.
DE   RecName: Full=Protein kibra;
GN   Name=Kibra; ORFNames=GF18133;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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
CC       pathway, a signaling pathway that plays a pivotal role in organ
CC       size control and tumor suppression by restricting proliferation
CC       and promoting apoptosis. The core of this pathway is composed of a
CC       kinase cascade wherein Hippo (Hpo), in complex with its regulatory
CC       protein Salvador (Sav), phosphorylates and activates Warts (Wts)
CC       in complex with its regulatory protein Mats, which in turn
CC       phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Kibra
CC       acts synergistically along with Ex and Mer to regulate the Hippo
CC       signaling pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with Mer and Ex. Interacts (via domain WW
CC       1) with Ex (via RXPPXY motif). Interacts with Mer, Sav, Hpo and
CC       Wts (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Apical cell
CC       membrane {ECO:0000250}. Note=Localizes at the apical cortex of
CC       epithelial cells and cytoplasmic, punctate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 WW domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00224}.
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DR   EMBL; CH902617; EDV42712.1; -; Genomic_DNA.
DR   RefSeq; XP_001954151.1; XM_001954115.1.
DR   ProteinModelPortal; B3LWS4; -.
DR   STRING; 7217.FBpp0121325; -.
DR   EnsemblMetazoa; FBtr0122833; FBpp0121325; FBgn0095151.
DR   GeneID; 6500911; -.
DR   KEGG; dan:Dana_GF18133; -.
DR   FlyBase; FBgn0095151; Dana\GF18133.
DR   eggNOG; COG5021; -.
DR   InParanoid; B3LWS4; -.
DR   KO; K16685; -.
DR   OrthoDB; EOG7RZ5P8; -.
DR   PhylomeDB; B3LWS4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035330; P:regulation of hippo signaling; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR001202; WW_dom.
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; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1271       Protein kibra.
FT                                /FTId=PRO_0000392968.
FT   DOMAIN       45     78       WW 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN       92    125       WW 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN      687    789       C2.
FT   COILED      192    223       {ECO:0000255}.
FT   COILED      326    454       {ECO:0000255}.
FT   COILED     1039   1066       {ECO:0000255}.
FT   COMPBIAS      4     40       Gln-rich.
FT   COMPBIAS    181    187       Poly-Ser.
FT   COMPBIAS    505    530       Gln-rich.
FT   COMPBIAS    826    835       Poly-Ala.
FT   COMPBIAS    886    892       Poly-Asp.
FT   COMPBIAS   1156   1168       Poly-Glu.
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
//
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