ID A0A077Z8K4_TRITR Unreviewed; 1201 AA.
AC A0A077Z8K4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein kibra {ECO:0000256|ARBA:ARBA00013712};
GN ORFNames=TTRE_0000436301 {ECO:0000313|EMBL:CDW56089.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56089.1};
RN [1] {ECO:0000313|EMBL:CDW56089.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW56089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily.
CC {ECO:0000256|ARBA:ARBA00010585}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG806007; CDW56089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z8K4; -.
DR STRING; 36087.A0A077Z8K4; -.
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; PF00397; WW; 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|SAM:Coils}.
FT DOMAIN 59..92
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 106..139
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 655..781
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 598..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 233..260
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 369..396
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 598..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 131921 MW; 483E8885EAC0D2C9 CRC64;
MHSNGLTNGC CSQNAAQLPE SADDSSTLVA PVSLAPTTLS LPSVSACSRS QHSTASSDLP
LPEGWEIKVD NDGRPYFIDH RSKITTWIDP RDRLTKPSAF SDCVGNELPF GWEQAYDNNV
GVYFINHLSA TNQLEDPRVQ WRALQDAMIR EYLQAAQEQM RAKELILKVK KDRRILAEQE
FQQLCDVLNK VEDSTTTTTI SRGINSVSRS NLGSSSTLTS SSRHDPDLLR SEIRIARQRL
ARLRREERQV ECELKHKQRG YDTLAEIKDR VSSNPEGYTA SETYALAREK EHLRVSLAAV
DQRKNKLVQD LLRLKSDLQQ SATVPESACS SSSIVSNSVG CLAEPPTSNS RCVHSPADRI
PKGLPVADIA RARLQYQETR HRLHNLQERL ALIEEQISPV QMETDRDQIT LIQEKEQLLH
ELRMVCYGEK KPPPEQQAML EEKMHALEED LRQALRLTHQ EMIERFSLHD ERLKIRREIM
SIGRVLASLE QYVQTLSAST LSSSSLSTGS SHASSASNLN QDAYWLQYGN GIEVQELVDL
RQRIERLAVG CSVPAPPCSS AEPRVEIEKG GSQPAISAAE LAHRLSSFST TADTVCRPLS
SAEDNSGTNT RSVSAAVSDE SVAGDSGVYD GRKPASTNLG DGLTSAWPTS PIVAVTAQLM
VGFDYLIDEN KLIVSIERAR NLHSLPCVNS ITALCVQGTI LPCATGDSVD FVTKWSRDVD
KPAFKQAFAI SISLPEVCNR ILQLYLWGLS GASSSRMAVC LGGVQVNFAE FSAQMIRCQW
LNVLSSSFFP HSDRLKPPSP EFNSEHDGET TASRSDAKNV VFGPAKLQCS PLEEDAKVSC
VDVRESVFNK DNVRQNPREE SSDESTIISS RNSTLTSLRG RALGALVDGQ NRADEQKANH
EAPEVSAEVT SSSRALAAEP KLRLTICSDF DGSAIAESPT GAATSGFSEL SRSSSTLSTK
VEKETAVGRL VPPAASAAAG RGCQQRSVRL NRSGSDSSVP STNRTEPFRR NIPERRSLRW
KRLGPCRRRA GAKLPYEASS SRRGGLQDVG FCTSLDIDVD LQATRIKLER EEELVDQLQN
VVDSLGSWKS GGNKGLPSWI ADDETVQSIL DRYYTTENPV ADSAGRAIDP SDLYQQTARK
IVRQSAHRVR RLMAAKGQLP PASNFKSKLN CLLATTAISI LPPSEETDAQ SLRLNISSEP
A
//
