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ZTF11_CAEEL
ID   ZTF11_CAEEL             Reviewed;         539 AA.
AC   O02274; H2L2J7;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 3.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Zinc finger protein ztf-11 {ECO:0000305};
GN   Name=ztf-11 {ECO:0000312|WormBase:F52F12.6a};
GN   Synonyms=ekl-2 {ECO:0000312|WormBase:F52F12.6a};
GN   ORFNames=F52F12.6 {ECO:0000312|WormBase:F52F12.6a};
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 LIN-9; LIN-52; RBA-1 AND SIN-3, SUBCELLULAR
RP   LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=31386623; DOI=10.7554/elife.46703;
RA   Lee J., Taylor C.A., Barnes K.M., Shen A., Stewart E.V., Chen A.,
RA   Xiang Y.K., Bao Z., Shen K.;
RT   "A Myt1 family transcription factor defines neuronal fate by repressing
RT   non-neuronal genes.";
RL   Elife 8:0-0(2019).
CC   -!- FUNCTION: Transcriptional repressor which promotes neuronal
CC       differentiation during embryonic and postembryonic neurogenesis
CC       (PubMed:31386623). Together with components of the MuvB corepressor
CC       complex, negatively regulates the expression of non-neuronal genes
CC       during neurogenesis (PubMed:31386623). Required for the generation of
CC       postembryonic neurons from epidermal cells (PubMed:31386623).
CC       {ECO:0000269|PubMed:31386623}.
CC   -!- SUBUNIT: Interacts with MuvB corepressor complex components lin-9, lin-
CC       52 and rba-1; the interaction is required to suppress the activation of
CC       non-neuronal genes in neurons (PubMed:31386623). Interacts with sin-3;
CC       the interaction is weak (PubMed:31386623).
CC       {ECO:0000269|PubMed:31386623}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31386623}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:F52F12.6a};
CC         IsoId=O02274-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F52F12.6b};
CC         IsoId=O02274-2; Sequence=VSP_060462;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development, but
CC       rarely expressed in lineages that do not produce neurons
CC       (PubMed:31386623). First expressed in neural precursors at the mid-
CC       gastrula stage of embryogenesis (PubMed:31386623). Highly expressed
CC       during the late gastrula to lima-bean embryonic stages, but weakly
CC       expressed in subsequent embryonic stages (PubMed:31386623). Post
CC       hatching, expressed in few neuronal nuclei and transiently expressed in
CC       postembryonic neuroectoblasts (PubMed:31386623). Not expressed in
CC       postmitotic neurons (PubMed:31386623). In L1 larvae, expressed in
CC       neurons and glia, but not in non-neuronal precursors (PubMed:31386623).
CC       In L2 stage larvae, expressed in the rectal epithelial Y cell
CC       (PubMed:31386623). {ECO:0000269|PubMed:31386623}.
CC   -!- DISRUPTION PHENOTYPE: Knockout in the rectal epithelial Y cell results
CC       in impaired formation of the PDA motor neuron (PubMed:31386623).
CC       Knockout in Pn lineages (the precursor cells of the ventral epidermis
CC       of newly hatched animals) results in the defective formation of ventral
CC       cord motor neurons (PubMed:31386623). {ECO:0000269|PubMed:31386623}.
CC   -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
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DR   EMBL; BX284601; CAB05737.2; -; Genomic_DNA.
DR   EMBL; BX284601; CCE71678.1; -; Genomic_DNA.
DR   PIR; T22514; T22514.
DR   RefSeq; NP_001251245.1; NM_001264316.1. [O02274-1]
DR   RefSeq; NP_001251246.1; NM_001264317.1. [O02274-2]
DR   AlphaFoldDB; O02274; -.
DR   SMR; O02274; -.
DR   STRING; 6239.F52F12.6a; -.
DR   EPD; O02274; -.
DR   PaxDb; O02274; -.
DR   EnsemblMetazoa; F52F12.6a.1; F52F12.6a.1; WBGene00009939. [O02274-1]
DR   EnsemblMetazoa; F52F12.6b.1; F52F12.6b.1; WBGene00009939. [O02274-2]
DR   GeneID; 172845; -.
DR   KEGG; cel:CELE_F52F12.6; -.
DR   UCSC; F52F12.6; c. elegans. [O02274-1]
DR   CTD; 172845; -.
DR   WormBase; F52F12.6a; CE24995; WBGene00009939; ztf-11. [O02274-1]
DR   WormBase; F52F12.6b; CE46793; WBGene00009939; ztf-11. [O02274-2]
DR   eggNOG; KOG3803; Eukaryota.
DR   GeneTree; ENSGT00940000170173; -.
DR   HOGENOM; CLU_493673_0_0_1; -.
DR   InParanoid; O02274; -.
DR   OMA; LMLAQFQ; -.
DR   OrthoDB; 1250194at2759; -.
DR   PRO; PR:O02274; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00009939; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR   GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR   GO; GO:0048664; P:neuron fate determination; IMP:UniProtKB.
DR   GO; GO:0048665; P:neuron fate specification; IMP:UniProtKB.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
DR   GO; GO:1903620; P:positive regulation of transdifferentiation; IMP:UniProtKB.
DR   InterPro; IPR002515; Znf_C2H2C.
DR   InterPro; IPR036060; Znf_C2H2C_sf.
DR   Pfam; PF01530; zf-C2HC; 2.
DR   SUPFAM; SSF103637; SSF103637; 2.
DR   PROSITE; PS51802; ZF_CCHHC; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..539
FT                   /note="Zinc finger protein ztf-11"
FT                   /id="PRO_0000448889"
FT   ZN_FING         256..299
FT                   /note="CCHHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   ZN_FING         302..345
FT                   /note="CCHHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   REGION          24..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   VAR_SEQ         1..97
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060462"
SQ   SEQUENCE   539 AA;  57069 MW;  C8D04C5F3244F1BE CRC64;
     MSSISNNPDF SSIDPAVLMS LLMKSSGSLP TPPDTHSDGS ESPDSTASDS SDKKRRRKPE
     SKDIVRVAEE AEAAAATCSS IPSSSDTKEN ETEEDQNMTC DTTTNNAQKP TEQTATSADV
     VTSSVPSGLE GVPSFLFSQF MAPSFQKQLE IFTSGNMMSA THSDTSPSDV DSVLDGGVVT
     AEETSSSKSP MMTSSDTPKT PLTASSPPHS SGSESRVMSP ITHTNISDEL SISTTPTVAF
     TPNGSIPSPG TGYSWSIRRE GKLACPTPGC DGSGHQTGLY THHRSLSGCP RRPDKTVIQM
     LALRQDTVLR CTTAGCSGKG HVNGNRTSHR SLSGCPIAHQ EKLARKGIKT TPQRTKTPIK
     GISISDECPL DLTLSGLPAG LSAQQLLAAA QAGLIPSSQM MDALFQQFSQ TQPLATLEEE
     SKKENEMEVD VETTSDDIPT LIKEEEEVKC ESPVPSVIPE IQSTPSRPVA APVAPGSAEK
     SSPTSQMLLQ MPGFSEALLK MTAPQVPFPQ YSPQAALFGN QSALLAQIML TQLQMQQGF
 
 
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