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EGL27_CAEEL
ID   EGL27_CAEEL             Reviewed;        1129 AA.
AC   Q09228; J7RNK9; Q09229; Q86LT4; Q8MQF3; Q9XYD0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Egg-laying defective protein 27;
GN   Name=egl-27 {ECO:0000312|WormBase:C04A2.3a};
GN   ORFNames=C04A2.3 {ECO:0000312|WormBase:C04A2.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2;
RX   PubMed=9927605; DOI=10.1242/dev.126.5.1055;
RA   Herman M.A., Ch'ng Q., Hettenbach S.M., Ratliff T.M., Kenyon C.,
RA   Herman R.K.;
RT   "EGL-27 is similar to a metastasis-associated factor and controls cell
RT   polarity and cell migration in C. elegans.";
RL   Development 126:1055-1064(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2;
RX   PubMed=10226007; DOI=10.1242/dev.126.11.2483;
RA   Solari F., Bateman A., Ahringer J.;
RT   "The Caenorhabditis elegans genes egl-27 and egr-1 are similar to MTA1, a
RT   member of a chromatin regulatory complex, and are redundantly required for
RT   embryonic patterning.";
RL   Development 126:2483-2494(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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   [4]
RP   FUNCTION, INTERACTION WITH CEH-6; SEM-4 AND SOX-2, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=22493276; DOI=10.1073/pnas.1117031109;
RA   Kagias K., Ahier A., Fischer N., Jarriault S.;
RT   "Members of the NODE (Nanog and Oct4-associated deacetylase) complex and
RT   SOX-2 promote the initiation of a natural cellular reprogramming event in
RT   vivo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:6596-6601(2012).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23271974; DOI=10.1371/journal.pgen.1003108;
RA   Xu X., Kim S.K.;
RT   "The GATA transcription factor egl-27 delays aging by promoting stress
RT   resistance in Caenorhabditis elegans.";
RL   PLoS Genet. 8:E1003108-E1003108(2012).
RN   [6]
RP   INTERACTION WITH WDR-5.1.
RX   PubMed=25124442; DOI=10.1126/science.1255885;
RA   Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
RA   Jarriault S.;
RT   "Sequential histone-modifying activities determine the robustness of
RT   transdifferentiation.";
RL   Science 345:826-829(2014).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25446273; DOI=10.1016/j.ydbio.2014.10.014;
RA   Krueger A.V., Jelier R., Dzyubachyk O., Zimmerman T., Meijering E.,
RA   Lehner B.;
RT   "Comprehensive single cell-resolution analysis of the role of chromatin
RT   regulators in early C. elegans embryogenesis.";
RL   Dev. Biol. 398:153-162(2015).
CC   -!- FUNCTION: Transcription factor which promotes stress survival and
CC       delays aging. Required for cell cycle progression and development of
CC       the mesodermal and endodermal embryonic lineages (PubMed:25446273).
CC       Required for normal T-cell polarity, for correct migration of QL
CC       neuroblast descendants and other cells, for embryonic patterning and
CC       for the embryonic expression of hlh-8. Also required for the
CC       transdifferentiation of the Y rectal epithelial cell to the PDA motor
CC       neuron during larval development. {ECO:0000269|PubMed:10226007,
CC       ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:23271974,
CC       ECO:0000269|PubMed:25446273, ECO:0000269|PubMed:9927605}.
CC   -!- SUBUNIT: Interacts with ceh-6, sem-4 and sox-2 (PubMed:22493276).
CC       Interacts with wdr-5.1 (PubMed:25124442). {ECO:0000269|PubMed:22493276,
CC       ECO:0000269|PubMed:25124442}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC       ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10226007,
CC       ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:9927605}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=a {ECO:0000312|WormBase:C04A2.3a};
CC         IsoId=Q09228-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:C04A2.3b};
CC         IsoId=Q09228-2; Sequence=VSP_047939, VSP_001608;
CC       Name=c {ECO:0000312|WormBase:C04A2.3c};
CC         IsoId=Q09228-3; Sequence=VSP_019864, VSP_001609;
CC       Name=d {ECO:0000312|WormBase:C04A2.3d};
CC         IsoId=Q09228-4; Sequence=VSP_047940, VSP_001608;
CC   -!- TISSUE SPECIFICITY: Expression detected in anterior intestine and head
CC       region. {ECO:0000269|PubMed:23271974}.
CC   -!- DEVELOPMENTAL STAGE: Expression detected from the 50-cell stage of
CC       embryogenesis through to adulthood. In the adult, expression increases
CC       two-fold between day 4 and day 14. {ECO:0000269|PubMed:10226007,
CC       ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:23271974,
CC       ECO:0000269|PubMed:9927605}.
CC   -!- INDUCTION: By starvation, heat stress, oxidative stress, and UV stress.
CC       {ECO:0000269|PubMed:23271974}.
CC   -!- DOMAIN: The SANT domain and GATA-type zinc finger are required for
CC       conversion of the Y rectal cell to the PDA neuron.
CC       {ECO:0000269|PubMed:22493276}.
CC   -!- DISRUPTION PHENOTYPE: Shortened lifespan and reduced survival in
CC       response to heat stress. Impaired differentiation of the Y rectal cell
CC       to the PDA neuron with the Y cell remaining undifferentiated in its
CC       original rectal location. Double RNAi-mediated knockdown with lin-40
CC       results in delayed cell cycle progression in mesodermal and endodermal
CC       embryonic lineages, but accelerated cell cycle progression in a subset
CC       of embryonic lineages (PubMed:25446273). {ECO:0000269|PubMed:22493276,
CC       ECO:0000269|PubMed:23271974, ECO:0000269|PubMed:25446273}.
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DR   EMBL; AF096618; AAD27790.1; -; mRNA.
DR   EMBL; BX284602; CCD62843.1; -; Genomic_DNA.
DR   EMBL; BX284602; CCD62844.2; -; Genomic_DNA.
DR   EMBL; BX284602; CCD62845.1; -; Genomic_DNA.
DR   EMBL; BX284602; CCM09405.1; -; Genomic_DNA.
DR   PIR; T43674; T43674.
DR   RefSeq; NP_001021911.2; NM_001026740.4.
DR   RefSeq; NP_001021912.1; NM_001026741.2.
DR   RefSeq; NP_001263660.1; NM_001276731.1. [Q09228-4]
DR   RefSeq; NP_741012.1; NM_171011.3. [Q09228-1]
DR   AlphaFoldDB; Q09228; -.
DR   BioGRID; 39459; 20.
DR   DIP; DIP-61372N; -.
DR   IntAct; Q09228; 7.
DR   STRING; 6239.C04A2.3a; -.
DR   iPTMnet; Q09228; -.
DR   EPD; Q09228; -.
DR   PaxDb; Q09228; -.
DR   PeptideAtlas; Q09228; -.
DR   PRIDE; Q09228; -.
DR   EnsemblMetazoa; C04A2.3a.1; C04A2.3a.1; WBGene00001194. [Q09228-1]
DR   EnsemblMetazoa; C04A2.3b.1; C04A2.3b.1; WBGene00001194. [Q09228-2]
DR   EnsemblMetazoa; C04A2.3c.1; C04A2.3c.1; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3c.2; C04A2.3c.2; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3c.3; C04A2.3c.3; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3c.4; C04A2.3c.4; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3c.5; C04A2.3c.5; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3c.6; C04A2.3c.6; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3c.7; C04A2.3c.7; WBGene00001194. [Q09228-3]
DR   EnsemblMetazoa; C04A2.3d.1; C04A2.3d.1; WBGene00001194. [Q09228-4]
DR   GeneID; 174121; -.
DR   KEGG; cel:CELE_C04A2.3; -.
DR   UCSC; C04A2.3a; c. elegans. [Q09228-1]
DR   CTD; 174121; -.
DR   WormBase; C04A2.3a; CE31287; WBGene00001194; egl-27. [Q09228-1]
DR   WormBase; C04A2.3b; CE47754; WBGene00001194; egl-27. [Q09228-2]
DR   WormBase; C04A2.3c; CE33268; WBGene00001194; egl-27. [Q09228-3]
DR   WormBase; C04A2.3d; CE47784; WBGene00001194; egl-27. [Q09228-4]
DR   eggNOG; KOG2133; Eukaryota.
DR   GeneTree; ENSGT00940000153615; -.
DR   HOGENOM; CLU_012470_0_0_1; -.
DR   InParanoid; Q09228; -.
DR   OMA; HHANGLL; -.
DR   OrthoDB; 315192at2759; -.
DR   SignaLink; Q09228; -.
DR   PRO; PR:Q09228; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00001194; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q09228; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; ISS:WormBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:WormBase.
DR   GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR   GO; GO:0007155; P:cell adhesion; IMP:WormBase.
DR   GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0008544; P:epidermis development; IMP:WormBase.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR   GO; GO:0031581; P:hemidesmosome assembly; IGI:WormBase.
DR   GO; GO:0007498; P:mesoderm development; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR   GO; GO:0018991; P:oviposition; IMP:WormBase.
DR   GO; GO:0009786; P:regulation of asymmetric cell division; IMP:WormBase.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:WormBase.
DR   GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:WormBase.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR000679; Znf_GATA.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00320; GATA; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM01189; ELM2; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1129
FT                   /note="Egg-laying defective protein 27"
FT                   /id="PRO_0000083511"
FT   DOMAIN          87..223
FT                   /note="BAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          224..327
FT                   /note="ELM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT   DOMAIN          332..384
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   ZN_FING         439..485
FT                   /note="GATA-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..628
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..950
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..515
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_019864"
FT   VAR_SEQ         1..238
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047940"
FT   VAR_SEQ         1..141
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:10226007"
FT                   /id="VSP_047939"
FT   VAR_SEQ         294..296
FT                   /note="Missing (in isoform b and isoform d)"
FT                   /evidence="ECO:0000303|PubMed:10226007"
FT                   /id="VSP_001608"
FT   VAR_SEQ         886..887
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001609"
FT   CONFLICT        671
FT                   /note="P -> L (in Ref. 1; AAD27790)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1129 AA;  128359 MW;  6E0F88BBC0AF43E8 CRC64;
     MSRFDSQCSS EDVNKEDECV PSSSEDSQDG VSSPMENDDE PEFSQKHYDI EPCYYSLTGK
     SDRNCRGIVY RYRQDSDLKG FQSHDGTLYR LRDSVFVEVS QNEPYVIAAI CGFKYTKRDH
     VVVKLTRYFR ADDIPEISLN LMKQERAELE INPHLCPQSL NRELFNSELQ ITQPVSCLRG
     KCIVEYVKDV RHARTVADFS LDNDTFFFCL HYNQDSTKLA STHYAIRVGT SFQATLPPMA
     ECSVGDDSDR DELLYRPNSI ESGEEEDYIK LARCYRTYTL SGNHMLDSQK NARSLQVSDL
     LMDEAIIQLH RSGYKIDDAL SELNANDIIL TTDVDNMTQD DAKKFAKGIK QLGKNFSRIH
     RELLPHHSRE QLVSYYYLWK KTPEATKPKQ AARRVNPTSI KRPTKEKVKA SRPTSTEYLD
     FDSASESDVE NNGPSGRACH HCYGAESKDW HHANGLLLCT DCRLHYKKYG QLRQIANRPS
     QVPACLFKRS NSDEEESGVR TRAGKKEQRR RTPSSMSETP DRRSPSTVSN GAPNLTAEET
     PTKKLNGSVK RAPKRPLHNG VINNVEKSNS SEEPASPTTP PPTLTNGLTN GHGPESSTPN
     GETISKRMKV EPSYDDDDDE EEGKMTIDEG DDDPMPVLNG FKKEESVEEI KLELNGTIKK
     ENGVETDPTT PTCSMEAENE VCETPAVVSV EIRDETNGET NSDLKDDENV EPDSPEDTFE
     LGSNVEFETK NAMFVRSIVR SCGPRCARTD LIFKIKVGGV WEKSIKEKEE RKKVHLQNQR
     IQDSEKVAIQ QNQIKKEQQQ SQPTPQQIHQ QQAQQNAQHL QQLQQAVMLG HLPPEVLRQM
     MPPQFGVDPT AILMQQMMAG QQSQGVNAAF QHQMALQQQL EAHQVQFQLM MAHQHQQKMI
     AEQQQQQRHA AAQQLREREQ REQRERERER QHQQQAQQAL HQQQQQHAAA AANQLNPAMM
     QMMALMANSA ASQQDIARLM EMAAQQQQQQ QQAAQAQAQR DQERERRERE AREREAARER
     EREQAAREAA ARDQAAREHA QAVQAAAAAA QQAQALTPDM QHMHLLQQLM LNPALMMQLQ
     QAQAQQQQQQ PQVTNPLQML QHGMAAQSAN QAEMMRRIHP EPAMRPQHQ
 
 
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