YAP1_CHICK
ID YAP1_CHICK Reviewed; 448 AA.
AC P46936;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Transcriptional coactivator YAP1;
DE Short=Yes-associated protein 1;
DE AltName: Full=65 kDa Yes-associated protein {ECO:0000303|PubMed:8035999};
DE Short=YAP65 {ECO:0000303|PubMed:8035999};
DE AltName: Full=Protein yorkie homolog;
GN Name=YAP1; Synonyms=YAP65;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=8035999;
RA Sudol M.;
RT "Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds
RT to the SH3 domain of the Yes proto-oncogene product.";
RL Oncogene 9:2145-2152(1994).
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 (By similarity). {ECO:0000250|UniProtKB:H2LBU8,
CC ECO:0000250|UniProtKB:P46937}.
CC -!- INTERACTION:
CC P46936; Q13625-2: TP53BP2; Xeno; NbExp=6; IntAct=EBI-7804091, EBI-287091;
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 -!- PTM: Phosphorylated by LATS1 and LATS2; leading to cytoplasmic
CC translocation and inactivation. {ECO:0000250|UniProtKB:H2LBU8}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
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DR EMBL; X76483; CAA54021.1; -; mRNA.
DR PIR; I50730; I50730.
DR RefSeq; NP_990574.1; NM_205243.1.
DR AlphaFoldDB; P46936; -.
DR SMR; P46936; -.
DR BioGRID; 676433; 1.
DR IntAct; P46936; 1.
DR MINT; P46936; -.
DR STRING; 9031.ENSGALP00000027721; -.
DR GeneID; 396171; -.
DR KEGG; gga:396171; -.
DR CTD; 10413; -.
DR VEuPathDB; HostDB:geneid_396171; -.
DR eggNOG; KOG0940; Eukaryota.
DR InParanoid; P46936; -.
DR OrthoDB; 1006566at2759; -.
DR PhylomeDB; P46936; -.
DR PRO; PR:P46936; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; 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:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; ISS:UniProtKB.
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; 1.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Cytoplasm; Nucleus; Proto-oncogene;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..448
FT /note="Transcriptional coactivator YAP1"
FT /id="PRO_0000076073"
FT DOMAIN 169..202
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..448
FT /note="Transactivation domain"
FT REGION 293..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..99
FT /evidence="ECO:0000250"
FT COILED 258..303
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 47822 MW; 719CC8D0F879A38D CRC64;
MDPGQPQPQQ PPQAAQPPAP QQAAPQPPGA GSGAPGGAAQ PPGAGPPPAG HQIVHVRGDS
ETDLEALFNA VMNPKGANVP HTLPMRLRKL PDSFFKPPEP KAHSRQASTD AGTAGALTPQ
HVRAHSSPAS LQLGAVSPGT LTPSGVVTGP GAPSSQHLRQ SSFEIPDDVP LPPGWEMAKT
PSGQRYFLNH IDQTTTWQDP RKAMLSQMNV TAPTSPPVQQ NLMNSASAMN QRISQSAPVK
QPPPLAPQSP QGGVMGGSSS NQQQQMRLQQ LQMEKERLRL KHQELLRQEL ALRSQLPTME
QDGGSQNPVS SPGMSQELRT MTTNSSDPFL NSGTYHSRDE STDSGLSMSS YSVPRTPDDF
LNSVDEMDTG DSISQSNIPS HQNRFPDYLE AIPGTNVDLG TLEGDGMNIE GEELMPSLQE
ALSSDILNDM ESVLAATKPD KESFLTWL
