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TEAD4_CHICK
ID   TEAD4_CHICK             Reviewed;         438 AA.
AC   P48984;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Transcriptional enhancer factor TEF-3;
DE   AltName: Full=M-CAT-binding factor;
DE   AltName: Full=RTEF-1;
DE   AltName: Full=TEA domain family member 4;
DE            Short=TEAD-4;
DE   AltName: Full=TEF-1;
GN   Name=TEAD4; Synonyms=TEF-1, TEF3;
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] (ISOFORMS A; B; C AND D).
RC   TISSUE=Heart;
RX   PubMed=8106348; DOI=10.1016/s0021-9258(17)41840-0;
RA   Stewart A.F.R., Larkin S.B., Farrance I.K.G., Mar J.H., Hall D.E.,
RA   Ordahl C.P.;
RT   "Muscle-enriched TEF-1 isoforms bind M-CAT elements from muscle-specific
RT   promoters and differentially activate transcription.";
RL   J. Biol. Chem. 269:3147-3150(1994).
CC   -!- FUNCTION: Transcription factor which plays a key role in the Hippo
CC       signaling pathway, a pathway involved in organ size control and tumor
CC       suppression by restricting proliferation and promoting apoptosis. The
CC       core of this pathway is composed of a kinase cascade wherein MST1/MST2,
CC       in complex with its regulatory protein SAV1, phosphorylates and
CC       activates LATS1/2 in complex with its regulatory protein MOB1, which in
CC       turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (By
CC       similarity). Binds m-cat elements from muscle-specific promoters and
CC       differentially activate transcription. {ECO:0000250}.
CC   -!- FUNCTION: Isoform B has probably a transactivation capacity that is
CC       lacking in the other isoforms. Isoform D may be defective in DNA
CC       binding.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=B;
CC         IsoId=P48984-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=P48984-2; Sequence=VSP_006391;
CC       Name=C;
CC         IsoId=P48984-3; Sequence=VSP_006391, VSP_006392;
CC       Name=D;
CC         IsoId=P48984-4; Sequence=VSP_006393;
CC   -!- TISSUE SPECIFICITY: Enriched in cardiac and skeletal muscle.
CC   -!- CAUTION: Was originally called TEF-1, but is the ortholog of mammalian
CC       TEF-3. {ECO:0000305|PubMed:8106348}.
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DR   EMBL; U04834; AAC59646.2; -; mRNA.
DR   EMBL; U06848; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U06849; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U06850; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U06851; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A53042; A53042.
DR   PIR; B53042; B53042.
DR   PIR; C53042; C53042.
DR   RefSeq; NP_001001337.1; NM_001001337.1.
DR   RefSeq; NP_001001340.1; NM_001001340.1. [P48984-4]
DR   RefSeq; NP_001001341.1; NM_001001341.1.
DR   RefSeq; NP_990102.1; NM_204771.1.
DR   AlphaFoldDB; P48984; -.
DR   SMR; P48984; -.
DR   STRING; 9031.ENSGALP00000029867; -.
DR   PaxDb; P48984; -.
DR   Ensembl; ENSGALT00000087584; ENSGALP00000062355; ENSGALG00000014342. [P48984-4]
DR   GeneID; 395542; -.
DR   KEGG; gga:395542; -.
DR   CTD; 7004; -.
DR   VEuPathDB; HostDB:geneid_395542; -.
DR   eggNOG; KOG3841; Eukaryota.
DR   GeneTree; ENSGT00950000182956; -.
DR   InParanoid; P48984; -.
DR   OrthoDB; 823827at2759; -.
DR   PhylomeDB; P48984; -.
DR   Reactome; R-GGA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR   Reactome; R-GGA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR   PRO; PR:P48984; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000014342; Expressed in skeletal muscle tissue and 11 other tissues.
DR   ExpressionAtlas; P48984; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR   GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 6.10.20.40; -; 1.
DR   InterPro; IPR000818; TEA/ATTS_dom.
DR   InterPro; IPR038096; TEA/ATTS_sf.
DR   InterPro; IPR027255; TEF-3.
DR   InterPro; IPR016361; TEF_metazoa.
DR   InterPro; IPR041086; YBD.
DR   Pfam; PF01285; TEA; 1.
DR   Pfam; PF17725; YBD; 1.
DR   PIRSF; PIRSF002603; TEF; 1.
DR   PIRSF; PIRSF500722; TEF-3; 1.
DR   PRINTS; PR00065; TEADOMAIN.
DR   SMART; SM00426; TEA; 1.
DR   PROSITE; PS00554; TEA_1; 1.
DR   PROSITE; PS51088; TEA_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..438
FT                   /note="Transcriptional enhancer factor TEF-3"
FT                   /id="PRO_0000205939"
FT   DNA_BIND        28..104
FT                   /note="TEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..131
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000303|PubMed:8106348"
FT                   /id="VSP_006393"
FT   VAR_SEQ         111..123
FT                   /note="Missing (in isoform A and isoform C)"
FT                   /evidence="ECO:0000303|PubMed:8106348"
FT                   /id="VSP_006391"
FT   VAR_SEQ         201
FT                   /note="P -> PVCL (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:8106348"
FT                   /id="VSP_006392"
FT   CONFLICT        1
FT                   /note="M -> LELLAGTI (in Ref. 1; AAC59646)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   438 AA;  49443 MW;  B2B580273EB0D1BC CRC64;
     MTSEWSSPAS PEGSNDSGGS EALDKPIDND AEGVWSPDIE QSFQEALAIY PPCGRRKIIL
     SDEGKMYGRN ELIARYIKLR TGKTRTRKQV SSHIQVLARR KAREIQAKLK KTQVDKYDFS
     SEKDQTAKDK AMQSIATMSS AQIISATAFH SKMALPGLPR SAYPAVSGFW QGALPGQAGS
     SQDVKPFTQQ PYALQPSLPL PGFDSPTGLP PSSSTPAWQG RRVASSKLWM LEFSAFLEQQ
     QDQDTYNKHL FVHIGQSNPS YSDPYLEAVD IRQIYDKFPE KKGGLKELFE RGPANAFFLV
     KFWADLNTNI EDESRSFYGV SSQYESPENM VITCSTKVCS FGKQVVEKVE TEYAHYENGH
     YAYRIHRSPL CEYMINFIHK LKHLPEKYMM NSVLENFTIL QVVTNRDTQE TLLCIAYVFE
     VSASDHGAQH HIYRLVKD
 
 
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