YAP1_DANRE
ID YAP1_DANRE Reviewed; 442 AA.
AC Q1L8J7; A1L1U5;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transcriptional coactivator YAP1;
DE Short=Yes-associated protein 1;
DE Short=zYAP {ECO:0000303|PubMed:21687713};
DE AltName: Full=Protein yorkie homolog;
DE AltName: Full=Yes-associated protein YAP65 homolog;
GN Name=yap1; ORFNames=CH211-181P1.5-001 {ECO:0000312|EMBL:CAK04259.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19393221; DOI=10.1016/j.bbrc.2009.04.070;
RA Jiang Q., Liu D., Gong Y., Wang Y., Sun S., Gui Y., Song H.;
RT "yap is required for the development of brain, eyes, and neural crest in
RT zebrafish.";
RL Biochem. Biophys. Res. Commun. 384:114-119(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21687713; DOI=10.1371/journal.pone.0020309;
RA Gee S.T., Milgram S.L., Kramer K.L., Conlon F.L., Moody S.A.;
RT "Yes-associated protein 65 (YAP) expands neural progenitors and regulates
RT Pax3 expression in the neural plate border zone.";
RL PLoS ONE 6:E20309-E20309(2011).
RN [5]
RP FUNCTION.
RX PubMed=25778702; DOI=10.1038/nature14215;
RA Porazinski S., Wang H., Asaoka Y., Behrndt M., Miyamoto T., Morita H.,
RA Hata S., Sasaki T., Krens S.F., Osada Y., Asaka S., Momoi A., Linton S.,
RA Miesfeld J.B., Link B.A., Senga T., Castillo-Morales A., Urrutia A.O.,
RA Shimizu N., Nagase H., Matsuura S., Bagby S., Kondoh H., Nishina H.,
RA Heisenberg C.P., Furutani-Seiki M.;
RT "YAP is essential for tissue tension to ensure vertebrate 3D body shape.";
RL Nature 521:217-221(2015).
CC -!- FUNCTION: Transcriptional regulator which can act both as a coactivator
CC and a corepressor and is the critical downstream regulatory target in
CC the Hippo signaling pathway that plays a pivotal role in organ size
CC control and tumor suppression by restricting proliferation and
CC promoting apoptosis (By similarity). Required for expansion of the
CC neural plate and neural plate border zone progenitor pools. Acts as a
CC direct regulator of pax3 expression via interaction with tead1
CC (PubMed:21687713). Plays a key role in tissue tension and 3D tissue
CC shape by regulating cortical actomyosin network formation
CC (PubMed:25778702). {ECO:0000250|UniProtKB:P46937,
CC ECO:0000269|PubMed:21687713}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46937}. Nucleus
CC {ECO:0000250|UniProtKB:P46937}. Note=Both phosphorylation and cell
CC density can regulate its subcellular localization. Phosphorylation
CC sequesters it in the cytoplasm by inhibiting its translocation into the
CC nucleus. At low density, predominantly nuclear and is translocated to
CC the cytoplasm at high density. {ECO:0000250|UniProtKB:P46937}.
CC -!- TISSUE SPECIFICITY: Expressed in the notochord, brain, eyes, branchial
CC arches and pectoral fins. {ECO:0000269|PubMed:19393221}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed in the embryo: maternal
CC expression is ubiquitous. {ECO:0000269|PubMed:19393221}.
CC -!- PTM: Phosphorylated by lats1 and lats2; leading to cytoplasmic
CC translocation and inactivation. {ECO:0000250|UniProtKB:P46937}.
CC -!- DISRUPTION PHENOTYPE: Embryos display a small head with smaller eyes
CC than normal and fewer cartilages in the branchial arches. Marked
CC increase in cell death in brain (PubMed:19393221). Incomplete epiboly
CC at gastrulation, characterized by blastopore closure defects and
CC impaired axis formation (PubMed:21687713).
CC {ECO:0000269|PubMed:19393221, ECO:0000269|PubMed:21687713}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shaping life - Issue 175 of
CC January 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/175/";
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; CR762425; CAK04259.2; -; Genomic_DNA.
DR EMBL; CT573116; CAK04259.2; JOINED; Genomic_DNA.
DR EMBL; BC129216; AAI29217.1; -; mRNA.
DR RefSeq; NP_001132952.1; NM_001139480.1.
DR AlphaFoldDB; Q1L8J7; -.
DR SMR; Q1L8J7; -.
DR STRING; 7955.ENSDARP00000089684; -.
DR iPTMnet; Q1L8J7; -.
DR PaxDb; Q1L8J7; -.
DR Ensembl; ENSDART00000098914; ENSDARP00000089684; ENSDARG00000068401.
DR Ensembl; ENSDART00000188193; ENSDARP00000152736; ENSDARG00000112952.
DR GeneID; 561411; -.
DR KEGG; dre:561411; -.
DR CTD; 10413; -.
DR ZFIN; ZDB-GENE-030131-9710; yap1.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00510000046760; -.
DR HOGENOM; CLU_041917_0_1_1; -.
DR InParanoid; Q1L8J7; -.
DR OMA; YYLNHIT; -.
DR OrthoDB; 1006566at2759; -.
DR PhylomeDB; Q1L8J7; -.
DR TreeFam; TF326941; -.
DR Reactome; R-DRE-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DRE-2028269; Signaling by Hippo.
DR Reactome; R-DRE-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-DRE-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-DRE-8951671; RUNX3 regulates YAP1-mediated transcription.
DR PRO; PR:Q1L8J7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000068401; Expressed in swim bladder and 25 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:ZFIN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:ZFIN.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:CACAO.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:ZFIN.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:CACAO.
DR GO; GO:0007492; P:endoderm development; IMP:ZFIN.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0042593; P:glucose homeostasis; IMP:ZFIN.
DR GO; GO:0060914; P:heart formation; IMP:CACAO.
DR GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IMP:ZFIN.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0031016; P:pancreas development; IMP:ZFIN.
DR GO; GO:1905480; P:positive regulation of glutamate-ammonia ligase activity; IMP:ZFIN.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048916; P:posterior lateral line development; IMP:ZFIN.
DR GO; GO:0039022; P:pronephric duct development; IMP:ZFIN.
DR GO; GO:0010468; P:regulation of gene expression; IMP:ZFIN.
DR GO; GO:0046620; P:regulation of organ growth; IMP:ZFIN.
DR GO; GO:0003406; P:retinal pigment epithelium development; IMP:ZFIN.
DR GO; GO:0003139; P:secondary heart field specification; IMP:ZFIN.
DR GO; GO:0001944; P:vasculature development; IMP:ZFIN.
DR GO; GO:0001570; P:vasculogenesis; IMP:ZFIN.
DR GO; GO:0003173; P:ventriculo bulbo valve development; IMP:ZFIN.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 2: Evidence at transcript level;
KW Activator; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..442
FT /note="Transcriptional coactivator YAP1"
FT /id="PRO_0000433905"
FT DOMAIN 126..159
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 186..219
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 51..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..442
FT /note="Transactivation domain"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT REGION 286..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..279
FT /evidence="ECO:0000255"
FT COMPBIAS 60..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 69
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 87
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 119
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT CONFLICT 370
FT /note="G -> S (in Ref. 2; AAI29217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 48362 MW; F1B0FC36035C535C CRC64;
MDPNQHNPPA GHQIVHVRGD SETDLEALFN AVMNPKNTIV PPSVPMRLRK LPDSFFTPPE
PKSHSRQAST DAGTAGTVTP HHVRAHSSPA SLQLGAVSPG ALTSMGPANA PPQHLRQSSY
EIPDDMPLPP GWEMAKTPSG QRYFLNHNDQ TTTWQDPRKA LLQMNQAAPA SPVPVQQQNI
MNPASGPLPD GWEQAITSEG EIYYINHKNK TTSWLDPRLD PRFAMNQQRI SQSAPVKQGS
QLPSSPQSGV MSGNNPIRLQ QIHIEKERLR IKQELLRQRP QELALRNQLP TSMEQDGGTQ
NPVSSPGMGQ DARNMTTNSS DPFLNSGTYH SRDESTDSGL SMSSYSVPRT PDDFLNSVDE
METGDTLGPG SMATQPSRFP DYLDAIPGTD VDLGTLEGES MAVEGEELMP SLQEALSSDI
LNDMESVLAA TKIDKENFLT WL