YAP1A_XENLA
ID YAP1A_XENLA Reviewed; 459 AA.
AC D6C652;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Transcriptional coactivator YAP1-A;
DE Short=Yes-associated protein 1-A;
DE Short=xYAP {ECO:0000303|PubMed:21687713};
DE AltName: Full=Protein yorkie homolog-A;
DE AltName: Full=Yes-associated protein YAP65 homolog A;
GN Name=yap1-a {ECO:0000305}; Synonyms=yap {ECO:0000303|PubMed:21687713};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION
RP WITH TEAD1.
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).
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). Required for expansion of the neural plate and neural
CC plate border zone progenitor pools. Acts as a direct regulator of pax3
CC expression via interaction with tead1 (PubMed:21687713).
CC {ECO:0000250|UniProtKB:H2LBU8, ECO:0000250|UniProtKB:P46937,
CC ECO:0000269|PubMed:21687713}.
CC -!- SUBUNIT: Interacts with tead1. {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 -!- PTM: Phosphorylated by lats1 and lats2; leading to cytoplasmic
CC translocation and inactivation. {ECO:0000250|UniProtKB:P46937}.
CC -!- DISRUPTION PHENOTYPE: Incomplete epiboly at gastrulation, characterized
CC by blastopore closure defects and impaired axis formation.
CC {ECO:0000269|PubMed:21687713}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
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DR EMBL; FJ979828; ADC43261.1; -; mRNA.
DR RefSeq; NP_001233236.1; NM_001246307.1.
DR AlphaFoldDB; D6C652; -.
DR SMR; D6C652; -.
DR IntAct; D6C652; 1.
DR GeneID; 100653494; -.
DR CTD; 100653494; -.
DR Xenbase; XB-GENE-17333137; yap1.L.
DR OrthoDB; 1006566at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 100653494; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..459
FT /note="Transcriptional coactivator YAP1-A"
FT /id="PRO_0000433907"
FT DOMAIN 141..174
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 199..232
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..459
FT /note="Transactivation domain"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT REGION 344..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 269..297
FT /evidence="ECO:0000255"
FT COMPBIAS 69..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 80
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 98
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 134
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
SQ SEQUENCE 459 AA; 50275 MW; 8564CEF501FCAC3C CRC64;
MEPGSQQQPS APAQQPPPVG HQVVHVRTDS ETDLEALFNA VMNPKNANLP QTLPMRMRKL
PDSFFKQPQP EAKSHSRQAS TDGGSAGALT PQHVRAHSSP ASLQLAAVSP GALSPQGVVT
GLAPPSAPHL RQSSYEIPDD VPLPPGWEMA KTPSGQRYFL NHIDQTTTWQ DPRKAMLSQI
NVTAPTSPPV QQNIMTPTGP LPDGWEQALT PEGEAYFINH KNKSTSWLDP RLDPRFAMNQ
QRLSQNAPVK APPALPPPSP QTGVLGSGGN QQMRLQQLQM EKERLRLKHQ ELLRQVRPQE
LALRSQIPPM EQDGGTQNPV CTTGISQELR TMTMNSSDPF LNSGTYHSRD ESTESGLSMS
SYSVPRTPDD FLNSVDEMDT GEAITQSTIP TQQNRFPDYL ETLPGTNVDL GTLEGEAMNV
EGEELMPSLQ EALSSDILND METVLAATKL DKESFLTWL
