ID B0XHJ0_CULQU Unreviewed; 1116 AA.
AC B0XHJ0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Protein kibra {ECO:0000256|ARBA:ARBA00013712};
GN Name=6052939 {ECO:0000313|EnsemblMetazoa:CPIJ018899-PA};
GN ORFNames=CpipJ_CPIJ018899 {ECO:0000313|EMBL:EDS28441.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS28441.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS28441.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ018899-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ018899-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00024960}.
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.
CC {ECO:0000256|ARBA:ARBA00025969}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily.
CC {ECO:0000256|ARBA:ARBA00010585}.
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DR EMBL; DS233162; EDS28441.1; -; Genomic_DNA.
DR RefSeq; XP_001869112.1; XM_001869077.1.
DR AlphaFoldDB; B0XHJ0; -.
DR STRING; 7176.B0XHJ0; -.
DR EnsemblMetazoa; CPIJ018899-RA; CPIJ018899-PA; CPIJ018899.
DR KEGG; cqu:CpipJ_CPIJ018899; -.
DR VEuPathDB; VectorBase:CPIJ018899; -.
DR VEuPathDB; VectorBase:CQUJHB004225; -.
DR eggNOG; KOG3209; Eukaryota.
DR HOGENOM; CLU_005420_1_0_1; -.
DR InParanoid; B0XHJ0; -.
DR OMA; QVTVVSM; -.
DR OrthoDB; 1334597at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd08680; C2_Kibra; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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 PANTHER; PTHR14791; BOMB/KIRA PROTEINS; 1.
DR PANTHER; PTHR14791:SF29; PROTEIN KIBRA; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT DOMAIN 19..52
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 571..690
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 750..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 254..288
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 313..382
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 929..966
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 750..771
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 125142 MW; F6125AC2660E3126 CRC64;
MIFWHPLTKP ETFADCVGNE LPFGWEEVYD PQIGTYYVNH NTQSTQLEDP RLEWKSKQEE
MLREYLCSAQ DTLEAKKEIF NVKTQRLHLA QEEYNHLNAL AASRTICSST SSCSTKFDPE
LLRADLALAK ERVFRLKKEL SRIQKEMHNT QKGVDTLSGV EQKLNSHING CYNITEAQAI
LEEVKKIQKS LITGEREKKE LMKSLAQVKD DLTRLQLRQE SPDASTFNLA QDRVCAASQT
DLSSENFPMG AREMAKMRQR YDEWRKRVKE IQEKLAALEE KIRPGEVESD QDRLLLFQEK
KQLLLEYRSI TPKSRSQTEM KRIQSVCKQL EADLNMAYEE SNQCIANRLK LHEEKQALLQ
KLLEALKEFT HLENQLKSLS ASTLSISSSS SLGSLSTASS KGSLSGLSFT DIYGDPLSTE
PQIDMVDINR RVQRLFHPSS EVSLSPRSSL SLETPPASPM KLEWNGGTEG PPYKPSAPYN
VPAPSYSSDY NLDKQKLEEQ LQDLKIRQLG IAPLSPIYEK PSYLDIPPAV ILSRSSSTSN
TRSVSTTVSD ESVAGDSGVF EASRALLTSK ECAQIQISIR YTATDSTLCI TIERGRNLAA
LCLPEGCQLF VRAILLPGTA TPFIRTNAVT DFVKPVFKTM LVAQMPLEKV YTKSLHVKVM
IIVGQREDWV GSAQISLAEF NAADASNKWY NIISRKSMTE LDGLEGCSNI REESSDESTI
ISSQTSTLTR NQGQEELQAV LEMVYDELAN DDEDEEDEED DDEEEEEVDE EAKNQAATQL
MLEEYMNSVK GTIATEDELD ETAAAAAIPV EKADKETNTE CAFLPEKGRR RLNDPAIRAG
GASSTIEENS VVDDRLVKRS QTFSPSAVAS KARYICRLNR SDSDSAMHFN NPVTPHPFRR
GAVERRSLRY SSRTPKVYHK MHPAVPRTSL DLELDLQAQQ TKLETLTDEI SRLRDLKKRL
ELARDNNNVK VAAWALENED FLKLIKGAGS ATTTEEKHMA KLLHKTSKEI YKLRKTKAGK
GKLDLISFKE KMAFFTRRGV SVPELPADIL QLDADCGDCG EQLSACNSPT KCPEEPVAGP
SKPFDPSEPS TSRAGQGSAK LEFSYNEVDR TYGVEV
//
