YAP1_ORYLA
ID YAP1_ORYLA Reviewed; 459 AA.
AC H2LBU8;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Transcriptional coactivator YAP1 {ECO:0000250|UniProtKB:P46937};
DE Short=Yes-associated protein 1 {ECO:0000250|UniProtKB:P46937};
DE AltName: Full=Protein hirame {ECO:0000303|PubMed:25778702};
DE AltName: Full=Protein yorkie homolog {ECO:0000250|UniProtKB:P46937};
DE AltName: Full=Yes-associated protein YAP65 homolog {ECO:0000250|UniProtKB:P46937};
GN Name=yap1 {ECO:0000250|UniProtKB:P46937};
GN Synonyms=hir {ECO:0000303|PubMed:25778702};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR;
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, PHOSPHORYLATION AT
RP SER-21; SER-69; SER-87 AND SER-119, AND MUTAGENESIS OF SER-21; SER-69;
RP SER-87 AND SER-119.
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). Plays a key role in tissue tension
CC and 3D tissue shape by regulating cortical actomyosin network formation
CC (PubMed:25778702). {ECO:0000250|UniProtKB:P46937,
CC ECO:0000269|PubMed:25778702}.
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: Ubiquitously expressed throughout development.
CC {ECO:0000269|PubMed:25778702}.
CC -!- PTM: Phosphorylated by lats1 and lats2; leading to cytoplasmic
CC translocation and inactivation. {ECO:0000305|PubMed:25778702}.
CC -!- DISRUPTION PHENOTYPE: Embryos are sensitive to deformation by gravity
CC and display a markedly flattened body. Mutants show delayed blastopore
CC closure and progressive body collapse from mid-neurulation, surviving
CC until just before hatching (6 days post-fertilization, dpf). During
CC body collapse, tissues and organs including neural tube and somites
CC become gradually flattened and improperly aligned.
CC {ECO:0000269|PubMed:25778702}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
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DR AlphaFoldDB; H2LBU8; -.
DR SMR; H2LBU8; -.
DR STRING; 8090.ENSORLP00000003377; -.
DR iPTMnet; H2LBU8; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_041917_0_1_1; -.
DR InParanoid; H2LBU8; -.
DR TreeFam; TF326941; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0035329; P:hippo signaling; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Activator; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..459
FT /note="Transcriptional coactivator YAP1"
FT /id="PRO_0000433906"
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..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..459
FT /note="Transactivation domain"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT REGION 307..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
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:0000305|PubMed:25778702"
FT MOD_RES 69
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000305|PubMed:25778702"
FT MOD_RES 87
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000305|PubMed:25778702"
FT MOD_RES 119
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000305|PubMed:25778702"
FT MUTAGEN 21
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-69; A-87 and A-119."
FT /evidence="ECO:0000269|PubMed:25778702"
FT MUTAGEN 69
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-21; A-87 and A-119."
FT /evidence="ECO:0000269|PubMed:25778702"
FT MUTAGEN 87
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-21; A-87 and A-119."
FT /evidence="ECO:0000269|PubMed:25778702"
FT MUTAGEN 119
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-21; A-69 and A-87."
FT /evidence="ECO:0000269|PubMed:25778702"
SQ SEQUENCE 459 AA; 50053 MW; B9C11A29AD51D512 CRC64;
MDPSQHNPPV GHQIVHVRGD SETDLEALFN AVMNPKGAVV PQSVPMRMRK LPDSFFKPPE
PKSHSRQAST DAGSGGVLTP HHVRAHSSPA SLQLGAVSGG SLSGMASAGA SPQHLRQSSY
EIPDDVPLPP GWEMAKTSSG QRYFLNHIDQ TTTWQDPRKA LLQLNQATPP STVPVQQQNL
LSPASGPLPE GWEQAITPEG EIYYINHKNK TTSWLDPRLE TRYALNQQRI TQSAPVKQGG
PLPPNPHGGV MGGNNQMRLQ QMEKERIRLK QQELLRQSQR PQIDLQPSTA NQDAEHCDEL
ALRNQLPTSM DQDGSSNPVS SPMAQDARTM TANSNDPFLN SVSSGTYHSR DESTDSGLSM
SSYSVPRTPD DFLNSVDEMD TGDPLAPSMA TQPSRFPDYL DTIPGTDVDL GTLEGESMAV
EGEELMPSLQ EALSSDILND MESVLAATKI DKESFLTWL
