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NFYB1_CAEEL
ID   NFYB1_CAEEL             Reviewed;         403 AA.
AC   O17286; A0A0M7RFF4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Nuclear transcription factor Y subunit nfyb-1 {ECO:0000305};
DE   AltName: Full=CAAT box DNA-binding protein subunit nfyb-1 {ECO:0000305};
GN   Name=nfyb-1 {ECO:0000312|WormBase:W10D9.4a};
GN   ORFNames=W10D9.4 {ECO:0000312|WormBase:W10D9.4a};
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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15704008; DOI=10.1007/s10735-004-6017-6;
RA   Franchini A., Imbriano C., Peruzzi E., Mantovani R., Ottaviani E.;
RT   "Expression of the CCAAT-binding factor NF-Y in Caenorhabditis elegans.";
RL   J. Mol. Histol. 36:139-145(2005).
RN   [3] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN NF-Y COMPLEX, INTERACTION WITH NFYC-1; NFYA-1
RP   AND NFYA-2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17574230; DOI=10.1016/j.ydbio.2007.05.021;
RA   Deng H., Sun Y., Zhang Y., Luo X., Hou W., Yan L., Chen Y., Tian E.,
RA   Han J., Zhang H.;
RT   "Transcription factor NFY globally represses the expression of the C.
RT   elegans Hox gene Abdominal-B homolog egl-5.";
RL   Dev. Biol. 308:583-592(2007).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23933492; DOI=10.1016/j.ydbio.2013.08.001;
RA   Milton A.C., Packard A.V., Clary L., Okkema P.G.;
RT   "The NF-Y complex negatively regulates Caenorhabditis elegans tbx-2
RT   expression.";
RL   Dev. Biol. 382:38-47(2013).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=25873636; DOI=10.1534/g3.115.018101;
RA   Milton A.C., Okkema P.G.;
RT   "Caenorhabditis elegans TBX-2 Directly Regulates Its Own Expression in a
RT   Negative Autoregulatory Loop.";
RL   G3 (Bethesda) 5:1177-1186(2015).
CC   -!- FUNCTION: Component of sequence-specific heterotrimeric transcription
CC       factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically
CC       recognize a 5'-CCAAT-3' box motif found in the promoters of its target
CC       genes to regulate their expression and control cellular identity in
CC       particular tissue types (PubMed:17574230). In association with the
CC       components in the NF-Y complexes, represses the expression of the T-box
CC       transcription factor tbx-2 throughout larval development, which most
CC       likely restricts its expression to certain tissues (PubMed:23933492,
CC       PubMed:25873636). May act to repress txb-2 expression in conjunction
CC       with tbx-2 itself, which has an autoregulatory role (PubMed:25873636).
CC       In association with the components in the nfya-1-NF-Y complex,
CC       negatively regulates the expression of the homeobox protein egl-5 to
CC       spatially restrict its expression in tissues such as the head
CC       (PubMed:17574230). May regulate spatial egl-5 expression in association
CC       with the mes-2-mes-3-mes-6 complex (PubMed:17574230).
CC       {ECO:0000269|PubMed:17574230, ECO:0000269|PubMed:23933492,
CC       ECO:0000269|PubMed:25873636}.
CC   -!- SUBUNIT: Forms two NF-Y heterotrimeric transcription factor complexes:
CC       the nfya-1-NF-Y complex is composed of nfya-1, nfyb-1 and nfyc-1, and
CC       the nfya-2-NF-Y complex is composed of nfya-2, nfyb-1 and nfyc-1
CC       (PubMed:17574230). Interacts with nfyc-1; the interaction is direct and
CC       is required for the interaction with either nfya-1 or nfya-2, and
CC       subsequent binding of the complex to the 5'-CCAAT-3' box motif in DNA
CC       (PubMed:17574230). {ECO:0000269|PubMed:17574230}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17574230}. Cytoplasm
CC       {ECO:0000269|PubMed:15704008, ECO:0000269|PubMed:17574230}. Perikaryon
CC       {ECO:0000269|PubMed:15704008}. Note=Localizes to the cytoplasm of
CC       secretory cells and cell bodies of the small ganglia surrounding the
CC       pharynx. {ECO:0000269|PubMed:15704008}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:W10D9.4a};
CC         IsoId=O17286-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:W10D9.4b};
CC         IsoId=O17286-2; Sequence=VSP_060606;
CC   -!- TISSUE SPECIFICITY: Expressed in certain parts of the gonads with high
CC       expression in fertilized oocytes in the uterus and mature oocytes from
CC       the distal to the proximal arm of the gonad, but weak expression in the
CC       syncytial ovaries and immature oocytes at the beginning of the proximal
CC       arm of the gonad (PubMed:15704008). Expressed in secretory cells in the
CC       pharyngeal terminal bulb wall, in the small ganglia surrounding the
CC       pharynx and in the neurons running anteriorly to the sensory organs in
CC       the head (PubMed:15704008). Not expressed in the intestine, the
CC       hypodermis or body wall muscle surrounding the pseudocoelomic space
CC       (PubMed:15704008). {ECO:0000269|PubMed:15704008}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cells of the developing embryo
CC       (PubMed:15704008, PubMed:17574230). At the larval stages, weakly
CC       expressed in neurons and pharyngeal secretory cells (PubMed:15704008,
CC       PubMed:17574230). At larval stages also expressed in the developing
CC       hermaphrodite vulva and male tail (PubMed:17574230). Not expressed in
CC       the gonads in larval stages (PubMed:15704008).
CC       {ECO:0000269|PubMed:15704008, ECO:0000269|PubMed:17574230}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in ectopic
CC       expression of the homeobox protein egl-5 in the head region
CC       (PubMed:17574230). RNAi-mediated knockdown results in ectopic
CC       expression of tbx-2 in the gut and seam cells of L4 stage larvae and
CC       adults (PubMed:23933492). RNAi-mediated knockdown enhances the larval
CC       lethality phenotype of the tbx-2 bx59 mutant (PubMed:23933492).
CC       {ECO:0000269|PubMed:17574230, ECO:0000269|PubMed:23933492}.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR   EMBL; BX284602; CCD65581.1; -; Genomic_DNA.
DR   EMBL; BX284602; CUR29996.1; -; Genomic_DNA.
DR   PIR; E88021; E88021.
DR   RefSeq; NP_001303801.1; NM_001316872.1. [O17286-2]
DR   RefSeq; NP_493740.1; NM_061339.4. [O17286-1]
DR   AlphaFoldDB; O17286; -.
DR   SMR; O17286; -.
DR   ComplexPortal; CPX-5666; CCAAT-binding factor complex, nfya-1 variant.
DR   ComplexPortal; CPX-5667; CCAAT-binding factor complex, nfya-2 variant.
DR   DIP; DIP-25261N; -.
DR   IntAct; O17286; 14.
DR   STRING; 6239.W10D9.4; -.
DR   EPD; O17286; -.
DR   PaxDb; O17286; -.
DR   PeptideAtlas; O17286; -.
DR   EnsemblMetazoa; W10D9.4a.1; W10D9.4a.1; WBGene00021132. [O17286-1]
DR   EnsemblMetazoa; W10D9.4b.1; W10D9.4b.1; WBGene00021132. [O17286-2]
DR   GeneID; 173435; -.
DR   KEGG; cel:CELE_W10D9.4; -.
DR   UCSC; W10D9.4; c. elegans. [O17286-1]
DR   CTD; 173435; -.
DR   WormBase; W10D9.4a; CE14792; WBGene00021132; nfyb-1. [O17286-1]
DR   WormBase; W10D9.4b; CE51090; WBGene00021132; nfyb-1. [O17286-2]
DR   eggNOG; KOG0869; Eukaryota.
DR   GeneTree; ENSGT00940000165114; -.
DR   HOGENOM; CLU_683769_0_0_1; -.
DR   InParanoid; O17286; -.
DR   OrthoDB; 1529111at2759; -.
DR   PRO; PR:O17286; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00021132; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; O17286; baseline and differential.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IPI:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009888; P:tissue development; IMP:UniProtKB.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR   PANTHER; PTHR11064; PTHR11064; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..403
FT                   /note="Nuclear transcription factor Y subunit nfyb-1"
FT                   /id="PRO_0000450334"
FT   REGION          318..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..376
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060606"
SQ   SEQUENCE   403 AA;  46062 MW;  72724FFCD9DA89FF CRC64;
     MDPKPINEGM LLEDHDHGMP EEEEITEDDM NGIHNIEEDT RTISEIAMEL HHPNKSQVLL
     DQERFLPIAN VVRIMKTQMD PQAKLAKDAK ECAQECVSEF ISFIASEAAE ICNITKRKTI
     TADDLLTAME ATGFDNYAEP MRIFLQKYRQ AHKITGPIHR THPDYVRPPQ FQMDPFVRPL
     FFDTEQGRRC TETQYVINGS EIVKNAPLGE EWNEQTGTLN TRADGYYMEE PMEPMPMEEV
     EIEEHEEIIE QDSLGAIALE QQGQMQIYVD PKTKQHFAAK ETPNGMELYP LIIQDTPLQL
     ENVSGPNQFV MNMPDGRAIP HGMGQEEPQP VSSSSVMRKI GQNPSSYAQQ HHHVSHVEQH
     DDVEYEEEEE VDQVEEDTVP VPIAPRPAAT RVQPKRTPTK RKK
 
 
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