ID Q7QEI4_ANOGA Unreviewed; 1013 AA.
AC Q7QEI4;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 5.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Protein kibra {ECO:0000256|ARBA:ARBA00013712};
GN Name=KIBRLG {ECO:0000313|EMBL:EAA06758.5};
GN Synonyms=1272272 {ECO:0000313|EnsemblMetazoa:AGAP000002-PA};
GN ORFNames=AgaP_AGAP000002 {ECO:0000313|EMBL:EAA06758.5};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA06758.5};
RN [1] {ECO:0000313|EMBL:EAA06758.5, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA06758.5,
RC ECO:0000313|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA06758.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA06758.5};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA06758.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA06758.5};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA06758.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA06758.5};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA06758.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA06758.5};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP000002-PA}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP000002-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; AAAB01008846; EAA06758.5; -; Genomic_DNA.
DR RefSeq; XP_311158.5; XM_311158.5.
DR AlphaFoldDB; Q7QEI4; -.
DR STRING; 7165.Q7QEI4; -.
DR PaxDb; 7165-AGAP000002-PA; -.
DR EnsemblMetazoa; AGAP000002-RA; AGAP000002-PA; AGAP000002.
DR EnsemblMetazoa; AGAP000002-RB; AGAP000002-PB; AGAP000002.
DR GeneID; 1272272; -.
DR KEGG; aga:AgaP_AGAP000002; -.
DR CTD; 1272272; -.
DR VEuPathDB; VectorBase:AGAP000002; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR HOGENOM; CLU_005420_1_0_1; -.
DR InParanoid; Q7QEI4; -.
DR OMA; THTHQNT; -.
DR OrthoDB; 1334597at2759; -.
DR Proteomes; UP000007062; Chromosome X.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0046621; P:negative regulation of organ growth; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0035330; P:regulation of hippo signaling; IBA:GO_Central.
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; PF00397; WW; 2.
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:UP000007062}.
FT DOMAIN 8..41
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 55..88
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 660..781
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..325
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..405
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 476..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..866
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 112402 MW; B0AFA89921130064 CRC64;
MPKSSSNADL PLGWEINTDY DGKVYFIDHI NKKTTWIDPR DKHTKPETFA DCIGNELPFG
WEESYDPQIG TYYINHNTQT TQLEDPRLQW KSKQDEMLRE YLCSAQDTLE AKKEILSVKT
QRLHLAQEEY NHLNALAASR TSLCSSTSSC STKFDPELLR ADLAIAKERV FRLKKELSRI
QKEMHSTQKG VDTLASVEQK LNAHVNGCYN ISEAQAIMEE VKKIQKSLIT GEREKKELMK
SLAQVKDDLT RLQLRQESPD ASTFNLAQDR ICAASQTDLS SEHFPMGARE MAKMRQRYDE
WRRRVKEIQE QLAALEEKIR PGELESDQDR LLLFQEKKQL LLEYRSITPK SRSPTEMRRI
QSVCRQLEED LNMAYEESNQ CIANRLKLHE EKQALLQQLL EALKEFTHLE HQLKSLSAST
LSISSSSSLG SLSTASSKGS LSGLSFTDIY GDPLSAEPQI DMVDMNRRVQ RLFHPSSEVT
SLSPRSSLST ETPPVSPMKM DWVAVVTAAA AVAGGSDSPS ANPASVHAAI NTTAKLASAA
SGPSYATPGT SQPVVPSYAV ATGVASSASS TTTSTEYNLD RQRLEEQLQE LKIRQLGIAG
GPLSPIYEKP SYLEPAALLS RSSSTSNTRS VSTTVSDESV AGDSGVFEAS RGPPPLLARE
CAQVQIGLRY VAADGVLCIT IERGSNFGAL GPPAGCQLFI RAMLLPTPSG PGLVRTGTVT
DLVRPTFKTM LVVPLSLDKV YAKSLHVKVM VLVGQREDWI GSTQISLAEF NAGDATTSRW
YNIVSRKSMN ESDLLDGGAR EESSDESTII SSQTSTLTRN QGQDELQAVL ELVYDELSND
DEDDDEEEDE EQGDEDDEEE EEEENGEELL YKKAVDDAGE PVARMMGRRR GKDLQRIVNS
VEEEDECEEQ QEQEGCASSE ATEMMIQEYM NSVKEQCGDA GDVGEDGEVD RTVPQPSSVQ
RVDKETNTEC AFLPERSRRR FPDPNGPARS STIEEGSVVD DRLVKRSQTF SPR
//
