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LSY27_CAEEL
ID   LSY27_CAEEL             Reviewed;         250 AA.
AC   O45526; H9G332;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Zinc finger protein lsy-27 {ECO:0000305};
GN   Name=lsy-27 {ECO:0000312|WormBase:F47H4.1a};
GN   ORFNames=F47H4.1 {ECO:0000312|WormBase:F47H4.1a};
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, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-148.
RX   PubMed=21555395; DOI=10.1534/genetics.111.129064;
RA   Zhang F., O'Meara M.M., Hobert O.;
RT   "A left/right asymmetric neuronal differentiation program is controlled by
RT   the Caenorhabditis elegans lsy-27 zinc-finger transcription factor.";
RL   Genetics 188:753-759(2011).
CC   -!- FUNCTION: Involved in regulating left/right asymmetric differentiation
CC       of the gustatory ASE neurons (PubMed:21555395). Plays a role in
CC       modulating expression of LIM/homeobox protein lim-6 (PubMed:21555395).
CC       {ECO:0000269|PubMed:21555395}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:F47H4.1a};
CC         IsoId=O45526-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F47H4.1b};
CC         IsoId=O45526-2; Sequence=VSP_061399;
CC   -!- DEVELOPMENTAL STAGE: Expressed very broadly throughout the embryo, from
CC       the one-cell stage until the comma stage, when expression diminishes,
CC       and is not observed after hatching in larvae or in adults
CC       (PubMed:21555395). Expressed in both ASE neurons in the comma-stage
CC       embryo (PubMed:21555395). {ECO:0000269|PubMed:21555395}.
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DR   EMBL; BX284605; CAB07203.1; -; Genomic_DNA.
DR   EMBL; BX284605; CCG28095.1; -; Genomic_DNA.
DR   PIR; T22368; T22368.
DR   RefSeq; NP_001256739.1; NM_001269810.1.
DR   RefSeq; NP_001256740.1; NM_001269811.1.
DR   AlphaFoldDB; O45526; -.
DR   DIP; DIP-26919N; -.
DR   IntAct; O45526; 1.
DR   STRING; 6239.F47H4.1a; -.
DR   EPD; O45526; -.
DR   PaxDb; O45526; -.
DR   EnsemblMetazoa; F47H4.1a.1; F47H4.1a.1; WBGene00009834. [O45526-1]
DR   EnsemblMetazoa; F47H4.1b.1; F47H4.1b.1; WBGene00009834. [O45526-2]
DR   GeneID; 180149; -.
DR   KEGG; cel:CELE_F47H4.1; -.
DR   UCSC; F47H4.1; c. elegans. [O45526-1]
DR   CTD; 180149; -.
DR   WormBase; F47H4.1a; CE16062; WBGene00009834; lsy-27.
DR   WormBase; F47H4.1b; CE47185; WBGene00009834; lsy-27.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00970000195965; -.
DR   HOGENOM; CLU_098769_0_0_1; -.
DR   InParanoid; O45526; -.
DR   OMA; NEDIHIH; -.
DR   OrthoDB; 1600969at2759; -.
DR   PhylomeDB; O45526; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00009834; Expressed in embryo and 4 other tissues.
DR   ExpressionAtlas; O45526; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..250
FT                   /note="Zinc finger protein lsy-27"
FT                   /id="PRO_0000454831"
FT   ZN_FING         25..48
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         52..75
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         81..104
FT                   /note="C2H2-type 3; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          126..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..46
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061399"
FT   MUTAGEN         148
FT                   /note="S->L: In ot108; defects in left/right asymmetry in
FT                   the gustatory ASE neurons. Significantly reduced expression
FT                   of LIM homeobox protein lim-6."
FT                   /evidence="ECO:0000269|PubMed:21555395"
SQ   SEQUENCE   250 AA;  27806 MW;  C80CADD677421807 CRC64;
     MTSIHSPVTR KEDTELKRPD LRGKFVCSSC SQNFQHSASL NRHRQLMHSN EHTCMMCERA
     LNQKETIREH MRNEHNLAQV FTCGCCNWTF ASKRQLTEHT KCIQGTGAPG DTIPIAKSIN
     APGSLIQSTI QGTPPVVKTG RKRPMGGSLS PSSSVSTSIS SRDASGSPPP TEEEAERKVL
     FDNAVDTILQ SKFFTYQQIT EVDTWVKIIE SANTLADTLQ RIKKSQKVKA EGPAVESKMI
     PEKHVKQEIE
 
 
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