YAP1_CAEEL
ID YAP1_CAEEL Reviewed; 442 AA.
AC Q19404;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Yes-associated protein homolog 1 {ECO:0000305|PubMed:23396260};
GN Name=yap-1 {ECO:0000312|WormBase:F13E6.4};
GN ORFNames=F13E6.4 {ECO:0000312|WormBase:F13E6.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH WTS-1 AND EGL-44, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-104, AND
RP PHOSPHORYLATION AT SER-104.
RX PubMed=23396260; DOI=10.1016/j.yexcr.2013.01.020;
RA Iwasa H., Maimaiti S., Kuroyanagi H., Kawano S., Inami K., Timalsina S.,
RA Ikeda M., Nakagawa K., Hata Y.;
RT "Yes-associated protein homolog, YAP-1, is involved in the thermotolerance
RT and aging in the nematode Caenorhabditis elegans.";
RL Exp. Cell Res. 319:931-945(2013).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=27930654; DOI=10.1371/journal.pgen.1006469;
RA Jensen V.L., Carter S., Sanders A.A., Li C., Kennedy J., Timbers T.A.,
RA Cai J., Scheidel N., Kennedy B.N., Morin R.D., Leroux M.R., Blacque O.E.;
RT "Whole-organism developmental expression profiling identifies rab-28 as a
RT novel ciliary GTPase associated with the BBSome and intraflagellar
RT transport.";
RL PLoS Genet. 12:E1006469-E1006469(2016).
CC -!- FUNCTION: Plays a role in thermal stress response and in aging.
CC {ECO:0000269|PubMed:23396260}.
CC -!- SUBUNIT: Interacts (via WW domain) with wts-1 (via N-terminus).
CC Interacts (via WW domain) with egl-44; the interaction may regulate
CC transcription. {ECO:0000269|PubMed:23396260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23396260}. Nucleus
CC {ECO:0000269|PubMed:23396260}. Cell projection, cilium
CC {ECO:0000269|PubMed:27930654}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:27930654}. Note=Cytoplasmic localization is
CC regulated by wts-1 and ftt-2 (PubMed:23396260). Localizes in the
CC cytoplasm when phosphorylated at Ser-104 (PubMed:23396260). Transient
CC nuclear localization in hypodermal cells upon heat shock treatment
CC (PubMed:23396260). Nuclear export after heat shock treatment is
CC regulated by wts-1, ftt-2, hsf-1 and daf-21 (PubMed:23396260). During
CC the embryonic development of dorsal epithelial cells, localizes
CC transiently in the nucleus (PubMed:23396260). Mainly cytoplasmic during
CC embryo elongation (PubMed:23396260). Localizes to the base of the
CC cilium (PubMed:27930654). {ECO:0000269|PubMed:23396260,
CC ECO:0000269|PubMed:27930654}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelia, hypodermis, muscles,
CC pharynx, intestine, gonadal sheath cells, vulva, spermatheca and in
CC excretory tissue. {ECO:0000269|PubMed:23396260}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at L1 stage results in
CC vulva protrusion and rupture of internal tissues resulting in premature
CC death. RNAi-mediated knockdown in middle-aged adults extends their
CC lifespan. {ECO:0000269|PubMed:23396260}.
CC -!- SIMILARITY: Belongs to the YAP1 family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; Z68105; CAA92121.2; -; Genomic_DNA.
DR PIR; G89632; G89632.
DR RefSeq; NP_509789.2; NM_077388.4.
DR AlphaFoldDB; Q19404; -.
DR DIP; DIP-25866N; -.
DR IntAct; Q19404; 2.
DR STRING; 6239.F13E6.4; -.
DR iPTMnet; Q19404; -.
DR EPD; Q19404; -.
DR PaxDb; Q19404; -.
DR PeptideAtlas; Q19404; -.
DR EnsemblMetazoa; F13E6.4.1; F13E6.4.1; WBGene00008748.
DR UCSC; F13E6.4; c. elegans.
DR WormBase; F13E6.4; CE37348; WBGene00008748; yap-1.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00510000046760; -.
DR HOGENOM; CLU_630441_0_0_1; -.
DR InParanoid; Q19404; -.
DR OMA; DINPHEF; -.
DR OrthoDB; 1326944at2759; -.
DR Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-CEL-2028269; Signaling by Hippo.
DR Reactome; R-CEL-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-CEL-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-CEL-8951671; RUNX3 regulates YAP1-mediated transcription.
DR PRO; PR:Q19404; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008748; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0003713; F:transcription coactivator 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; IGI:WormBase.
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 Cell projection; Cilium; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..442
FT /note="Yes-associated protein homolog 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432474"
FT DOMAIN 203..236
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23396260"
FT MUTAGEN 104
FT /note="S->A: Cytoplasmic localization. No significant
FT effect on nucleocytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:23396260"
SQ SEQUENCE 442 AA; 50692 MW; DE2E0F058C57E190 CRC64;
MASKSIHKKH QENSQQDKNQ FSVHHYLDPN QSIHALISCS EKKYEKNQNQ KKNPLPSSYY
HQKRNPGSSA HSPYGSVDES SRTAVSPAMD MVSNQAPIHT RQVSAPNLHT SVNNGQSSAT
VPHPSHHNVH HQHSKSVSAL PMTIGYSPVP SHVKSVSHEA NYSYAGLSEI PQQQGMMQQN
REKSLSLDPM RRPFMTPQDV EQLPMPQGWE MCYDSDGVRY FKDHNSKTTT WDDPRLKQQE
QTGFGLGENI GQNRYNNCYD NGHSSRSLPS IHQHQQMIPN HPQPQYSSQQ QMDYIQQLQN
ERMMIQEKNA QLINSGLVDS PQPPYQAISP MSSTMMHSHD PNFMYQQQQQ AQNSQQQQTP
HTLHQIPNQY QNSQMNDDSA MEVDYSMVSH PQQLQHQHQP HMHNNMPSNY VIDDINPHEF
DQYLQISNDN NRGVGSMVHH YQ
