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Database: UniProt
Entry: E0VV15_PEDHC
LinkDB: E0VV15_PEDHC
Original site: E0VV15_PEDHC 
ID   E0VV15_PEDHC            Unreviewed;      1256 AA.
AC   E0VV15;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Protein kibra {ECO:0000256|ARBA:ARBA00013712};
GN   Name=8230669 {ECO:0000313|EnsemblMetazoa:PHUM457750-PA};
GN   ORFNames=Phum_PHUM457750 {ECO:0000313|EMBL:EEB17221.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB17221.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB17221.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB17221.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB17221.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM457750-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM457750-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; AAZO01005566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235800; EEB17221.1; -; Genomic_DNA.
DR   RefSeq; XP_002429959.1; XM_002429914.1.
DR   AlphaFoldDB; E0VV15; -.
DR   STRING; 121224.E0VV15; -.
DR   EnsemblMetazoa; PHUM457750-RA; PHUM457750-PA; PHUM457750.
DR   GeneID; 8230669; -.
DR   KEGG; phu:Phum_PHUM457750; -.
DR   CTD; 8230669; -.
DR   VEuPathDB; VectorBase:PHUM457750; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; KOG3209; Eukaryota.
DR   HOGENOM; CLU_005420_1_0_1; -.
DR   InParanoid; E0VV15; -.
DR   OMA; DTDYQYK; -.
DR   OrthoDB; 1334597at2759; -.
DR   Proteomes; UP000009046; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
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; SM00239; C2; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF51045; WW domain; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046}.
FT   DOMAIN          9..42
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          56..89
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          691..811
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          424..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..193
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          230..257
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          295..322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          354..396
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1013..1043
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        843..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1147..1169
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1256 AA;  140965 MW;  9003A2487CFFC8CB CRC64;
     MPRRRNGELP LPEGWEYATD DDGKVYFIDH VTKKTTWIDP RDRFTKPQTF ADCIGNELPL
     GWEEAYDAQI GVYYINHVNQ CTQLEDPRLE WRAIQEAMLR DYLQTAQDAL EAKKEIFDVK
     QQRLYLAEDE YNHLNNALTT LNKSRSSLCS NVSSTKYDPD LLKSDVALAR NRVSRLKREL
     EQIKTEMTCT QRGVETLASV EQKLSGQGGY YNLSEAQAIV TELKNIQMSL SSGEKEKAEL
     MQSLAKLKDD LTRLQLSESS PDVSTLSLPQ EKLSTASQTD LSGELVPIGT RLAEMARTRL
     QYDEARKRVQ LVQRKLADLE EKVTPGQAES DKDRLLLFQE KEQLLRELRS MTPRSRSAQE
     MTDIQLEVKR LERDLNQALE LNNRAIADRV RLHEEKQILL QELCEALRTM TSLESQLKSL
     SASTSSVSSS SSLGSLSTSS SKGSLSSGLS FTDIYDVNWP GSSVDMIDLH KRVERLLRSS
     NDAISPQPSL SPRSSLSSVS PPVSPQLHKV PSKVSNYTFE SNNSIIYDKF QMSESNIQTV
     TGNNPTTLVN SKYNDSADPL YQNIGINLVC LPPRYDDVER QRQLERSGKL LDNVKNKLLM
     YDHNLENVRL CEDERAYPQS RISQTRQQLE PPLSPISETP QDQNFELIQV SSTPSSGSNT
     RSVSAAVSDE SVAGDSGVFE AANRLQHCNL DTAQIQIKLR YAVSEGLLHV GIERARNLSA
     LLIPQQSQVF IKTVLLPSGP GSGSCCTKTV TDLKKPIFGE NFPLSVALNK LSSKTLQINV
     LCLTNSIEEC VGYAQVSLAD FSPESVSSKW YNILGSEFMQ LKSPTNKTLR NSSINVKNEG
     NNKSEVNETR REESSDESTI ISSQASTLTR PAVVESCAST FCLAEEEEED VLEQVFPLED
     ETCIDKETNT ECVFVLEKGN RGENKQMGII KRSQTFSPSA AQHQYTCRLN RSDSDSSMPL
     YRRGAPFQRN SVERRSLRWK PSSGLTVVKV NSHRRSGRVP AVARTSLDLE LDRRAQLSRL
     QAQQDELEKL RNLTTKLESV RARGDAELAA LVLEDQQFQT LIAQAETSLQ PQSQDDKRVE
     KMFKKTAKEI YKLRKSKAGK GKPDVISFKE KMAFFTRVHL NIPNLPGEEI RSESSTLTRG
     ESLLNPELED DDADDADADD DDNDNDNDDN DNKLELNESN EEGLSVIVSE TINESTGETL
     RNVEGEEKKV VMENSEINIR SVDKDSRTVE GSEGIQSGKE NQRFEYVVDR ILGVEV
//
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