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KIBRA_DROER
ID   KIBRA_DROER             Reviewed;        1283 AA.
AC   B3P3M8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Protein kibra;
GN   Name=Kibra; ORFNames=GG21121;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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; CH954181; EDV48916.1; -; Genomic_DNA.
DR   RefSeq; XP_001979958.1; XM_001979922.2.
DR   AlphaFoldDB; B3P3M8; -.
DR   SMR; B3P3M8; -.
DR   STRING; 7220.FBpp0139667; -.
DR   EnsemblMetazoa; FBtr0141175; FBpp0139667; FBgn0113304.
DR   GeneID; 6552773; -.
DR   KEGG; der:6552773; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; KOG3209; Eukaryota.
DR   HOGENOM; CLU_005420_1_0_1; -.
DR   OMA; HHTHIPR; -.
DR   OrthoDB; 364990at2759; -.
DR   PhylomeDB; B3P3M8; -.
DR   ChiTaRS; kibra; fly.
DR   Proteomes; UP000008711; 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; 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; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..1283
FT                   /note="Protein kibra"
FT                   /id="PRO_0000392970"
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          537..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          887..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          941..969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          200..228
FT                   /evidence="ECO:0000255"
FT   COILED          334..462
FT                   /evidence="ECO:0000255"
FT   COILED          1048..1075
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        31..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..910
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1283 AA;  143670 MW;  A2128BC76FC54E37 CRC64;
     MPNLQQTASQ SQHHLYPPHL RPHHHHQQQQ HHQQQQQQQH THHQQQQQHH SDFPLPDGWD
     IAKDFDGKTY YIDHINKKTT WLDPRDCYTK PQTFEDCVGD ELPMGWEESY DPNIGPYYIN
     HLAQSTQLED PRQEWKTVQE QMLSDYLSAA QDQLENKREM LDVKQQRLLW AQEEYNHLKL
     AASRSSLCSS SSSMSRHDPE LLRADLMLAR ERVHQLKQEL THITNDISYT ERGMNTLYSV
     GEKINARENG CYDIAEVQAI REEMLKVHKS LVSGEKVREE LMRSLVQIKN ELGRQQISEE
     NSDLASPFDR VCVASQTDLC GSSGDNLNGG ARFAEMAKTK LQYAEWRKHI KKLQQQLADH
     VERIEPGQLE SDKDRILLIQ EKEKLLNDLN SISLKSRSEE EKRVIHQTRH KLEEDLKEAY
     EANNTCVANR LRFHEEKQLL LDKLQEALKS TKLLEERLKS FSSESTFSIS SGSSLGSLST
     ASSKSALSFT DIYIDPFAVD SPIDVVDLRR RSQRLFQQHQ QQRLLPVHPV LQQQQSAEVT
     LSPRSSLSME TPPASPMKYN AGADQTPQAL KEEPTYANAL PAPPAYTAPP PVPISGVRAR
     PYDLDSTVLD CMMLEAKLQK LNMGTPLNLA AAPLSPISEK PSLLDLPQEM LSRSSSTSNT
     RSVSAAVSNE SVAGDSGVFE ASRAHLPRKE LAQVQIGLKY LKQEGVLVVS LERANNLLAL
     WTASADNSQV YLRAALLPNS LTSIRTKALG DFQKPFFNDT FAVPITLDKL LTKSLQVTVV
     TMTGQKEEII GTVQISMAEF NPEDSTLKWY NVLSSKFIPS FESLDIPSTS AAAAAAAVAA
     SNAPSSGNNR EESSDESTIT SSQTSTLTRN QAPCMELQEQ ITAELLELGP LNEPECSDDD
     DEDEEEELDD KQLVSDVGLM NSSGMLDAYL QNMKQEFADK ETNTDRAYLP EKSRGQSQLM
     DDRPVKRSQT FTPSAAVSKN RYNCRLNRSD SDSAMHCGVA PHTFQRGAAE RRSLRFHTKA
     PKSVTKLHHT HIPRTSLDLE LDLQAQHSKL YFLNDQIAKL QNLKEVLQKA CENKDPLVAA
     WAIENEEFQR LVARADPAKC PEERQLQKLL MKTAKEIHKL RKTKVPKGCP DLVSFKEKIT
     FFTRKGLSVP ELPSEFTLPE ANPIEEEEEE EDEDEFYNSP ETAIAINTAL VASSNRNKNL
     SEHPHRSTSG AVPKLPAPVA TPAATPAATP AATPVATPAA TPVVATAAQP EAKPAAAPIP
     VASNDAEQQR FDYVVDRNYG VEV
 
 
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