KIBRA_DROSE
ID KIBRA_DROSE Reviewed; 1295 AA.
AC B4HEJ6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein kibra;
GN Name=Kibra; ORFNames=GM25831;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480815; EDW42153.1; -; Genomic_DNA.
DR RefSeq; XP_002031167.1; XM_002031131.1.
DR AlphaFoldDB; B4HEJ6; -.
DR SMR; B4HEJ6; -.
DR STRING; 7238.B4HEJ6; -.
DR EnsemblMetazoa; FBtr0208816; FBpp0207308; FBgn0180687.
DR HOGENOM; CLU_005420_1_0_1; -.
DR OMA; HHTHIPR; -.
DR PhylomeDB; B4HEJ6; -.
DR ChiTaRS; kibra; fly.
DR Proteomes; UP000001292; 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; 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..1295
FT /note="Protein kibra"
FT /id="PRO_0000392973"
FT DOMAIN 53..86
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 100..133
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 690..810
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..228
FT /evidence="ECO:0000255"
FT COILED 334..460
FT /evidence="ECO:0000255"
FT COILED 1048..1075
FT /evidence="ECO:0000255"
FT COMPBIAS 21..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..911
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 144908 MW; 8148BB9C88E68FBF CRC64;
MPNLQQTASQ SQHHLHPHHL RPQQQQQQQQ HHHQQQRQQQ QHTHHQQQHH SDFPLPDGWD
IAKDFDGKTY YIDHINKKTT WLDPRDCYTK PQTFEDCVGD ELPMGWEESY DPNIGPYYIN
HLAQSTQLED PRQEWKSVQE QMLSDYLSAA QDQLENKREM FDVKQQRLLW AQEEYNHLKL
AASRSSLCSS SSSMSRHDPE LLRADLMLAR ERVHQLKQEL THITNDISYT ERGMNTLYSV
GEKINARENG CYDIAEVQAI HEEMLKVHKS LVSGEKVREE LMRSLVQIKN ELGRQQISEE
NSDLASPFDR VCVASQTDLC GSSGDNLNEG ARFAEMAKTT LQYAEWRKHI KKLQQQLADH
VERIEPGQLE SDKDRILLIQ EKEKLLNDLN SISLKSRSEE EKRVIHQTRH KLEEDLKEAY
EANNTCVANR LRFHEEKQLL LDKLQEALKS TKLLEERLKT FSSESTFSIS SGSSLGSLVH
GQHKSALSFT DIYIDPFAVD SPIDVVDLRR RSQRLFQQHQ QQRLHPVHPV LQQQQSAEVT
LSPRSSLSME TPPASPMKYN AGADQTPQAL KEEPTYANAL HAPPAYTAPP PVPISGVRAR
PYDLDSTVLD CMMLEAKLQK LNMGTPLNLA VAPLSPISEK PSLLDLPQEM LSRSSSTSNT
RSVSAAVSNE SVAGDSGVFE ASRAHLPRKE LAQVQIGLKY LKQEGVLVVS LERANNLLAL
WTASADNSQV YLRAALLPNS LTSIRTKALG DFQKPVFNDT FAVPITLDKL LTKSLQVTVV
TMTGQKEEII GTVQISMAEF NPEDSTLKWY NVLSSKFIPS FESLDIPSTS AAAAAAAVAA
SNAPNPGNNR EESSDESTIT SSQTSTLTRN QAPCMELQEQ IAAELMGLGP LNEPECSDDD
DDDEEEELED KQLVSDVGLM NSSSMLHAYL QNMKQEFADK ETNTDRAYLP EKSRGQSQLM
DDRPVKRSQT FTPSAAVSKN RYNCRLNRSD SDSAMHCGVA PHTFQRGAAE RRSLRYLSKA
PKSVTKLHHT HIPRTSLDLE LDLQAQHSKL YFLNDQIAKL QNLKEVLQKA CDNKDPLVAA
WAIENEEFQR LVARADPAKC PEERQLQKLL MKTAKEIHKL RKTKVPKGCP DLVSFKEKIT
FFTRKGLSVP ELPSEFTLPE ANPIEEEEEE EDEDEFYNSP ETAIAINTAL VASSNRNKNL
SEHLHRATSG AVPKIPAPVV TPAVTPAAAP AATPAATPAA TPAATSAATP AATPVVSPAA
QPDAKAADAP IPVASNDAEQ QRFDYVVDRN YGVEV
