ZFP1_CAEEL
ID ZFP1_CAEEL Reviewed; 867 AA.
AC P34447; G8JYB8; P34448; P34449;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc finger protein zfp-1 {ECO:0000312|WormBase:F54F2.2a};
DE AltName: Full=Protein AF-10 homolog {ECO:0000305};
GN Name=zfp-1 {ECO:0000312|WormBase:F54F2.2a};
GN ORFNames=F54F2.2 {ECO:0000312|WormBase:F54F2.2a};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16507136; DOI=10.1186/gb-2006-7-1-r4;
RA Lehner B., Calixto A., Crombie C., Tischler J., Fortunato A., Chalfie M.,
RA Fraser A.G.;
RT "Loss of LIN-35, the Caenorhabditis elegans ortholog of the tumor
RT suppressor p105Rb, results in enhanced RNA interference.";
RL Genome Biol. 7:R4.1-R4.10(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16710447; DOI=10.1371/journal.pgen.0020074;
RA Cui M., Kim E.B., Han M.;
RT "Diverse chromatin remodeling genes antagonize the Rb-involved SynMuv
RT pathways in C. elegans.";
RL PLoS Genet. 2:E74-E74(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21980302; DOI=10.1371/journal.pgen.1002299;
RA Mansisidor A.R., Cecere G., Hoersch S., Jensen M.B., Kawli T.,
RA Kennedy L.M., Chavez V., Tan M.W., Lieb J.D., Grishok A.;
RT "A conserved PHD finger protein and endogenous RNAi modulate insulin
RT signaling in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002299-E1002299(2011).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH DOT-1.1, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=23806335; DOI=10.1016/j.molcel.2013.06.002;
RA Cecere G., Hoersch S., Jensen M.B., Dixit S., Grishok A.;
RT "The ZFP-1(AF10)/DOT-1 complex opposes H2B ubiquitination to reduce Pol II
RT transcription.";
RL Mol. Cell 50:894-907(2013).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY (ISOFORMS A AND C),
RP DEVELOPMENTAL STAGE (ISOFORMS A AND C), DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF MET-4.
RX PubMed=23263989; DOI=10.1128/mcb.01462-12;
RA Avgousti D.C., Cecere G., Grishok A.;
RT "The conserved PHD1-PHD2 domain of ZFP-1/AF10 is a discrete functional
RT module essential for viability in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 33:999-1015(2013).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF 601-TRP--LYS-867.
RX PubMed=24066155; DOI=10.1371/journal.pone.0074908;
RA Gysi S., Rhiner C., Flibotte S., Moerman D.G., Hengartner M.O.;
RT "A network of HSPG core proteins and HS modifying enzymes regulates netrin-
RT dependent guidance of D-type motor neurons in Caenorhabditis elegans.";
RL PLoS ONE 8:E74908-E74908(2013).
RN [9]
RP FUNCTION (ISOFORM A).
RX PubMed=24558261; DOI=10.1534/genetics.114.162917;
RA Kennedy L.M., Grishok A.;
RT "Neuronal migration is regulated by endogenous RNAi and chromatin-binding
RT factor ZFP-1/AF10 in Caenorhabditis elegans.";
RL Genetics 197:207-220(2014).
RN [10]
RP FUNCTION.
RX PubMed=25422944; DOI=10.1371/journal.pone.0113060;
RA Tehrani N., Del Rosario J., Dominguez M., Kalb R., Mano I.;
RT "The insulin/IGF signaling regulators cytohesin/GRP-1 and PIP5K/PPK-1
RT modulate susceptibility to excitotoxicity in C. elegans.";
RL PLoS ONE 9:E113060-E113060(2014).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY (ISOFORMS A AND C), AND DISRUPTION PHENOTYPE.
RX PubMed=27039057; DOI=10.1111/acel.12477;
RA Singh A., Kumar N., Matai L., Jain V., Garg A., Mukhopadhyay A.;
RT "A chromatin modifier integrates insulin/IGF-1 signalling and dietary
RT restriction to regulate longevity.";
RL Aging Cell 15:694-705(2016).
CC -!- FUNCTION: Recruits the histone methyltransferase dot-1.1 to chromatin
CC to methylate 'Lys-79' of histone H3 and activate transcription
CC (PubMed:23806335). Recognizes and binds histone H3 methylated at 'Lys-
CC 4' (H3K4me) at the promoters of target genes (PubMed:23263989). During
CC stress, the zfp-1-dot-1.1 complex also plays a role in the
CC deubiquitination of histone H2B sites, which negatively modulates the
CC RNA polymerase II-induced transcription of highly expressed genes
CC (PubMed:23806335). In response to stress, binds to the pdk-1 promoter
CC to negatively regulate pdk-1 expression, which negatively modulates
CC daf-16/FOXO-mediated gene expression (PubMed:21980302). Thus, most
CC likely via this mechanism, in response to stress, it confers a
CC protective role against neuronal necrosis (PubMed:25422944). Plays a
CC role in Insulin/IGF-1-like signaling (IIS)- and diet restriction-
CC mediated lifespan extension by controlling daf-16/FOXO and pha-4/FOXA
CC recruitment to target promoters (PubMed:27039057). May negatively
CC regulate the expression of genes required for vulval development
CC (PubMed:16507136, PubMed:16710447). May play a role in axon guidance in
CC D-type motor neurons (PubMed:24066155). May suppress sensitivity to
CC RNAi (PubMed:16507136). {ECO:0000269|PubMed:16507136,
CC ECO:0000269|PubMed:16710447, ECO:0000269|PubMed:21980302,
CC ECO:0000269|PubMed:23263989, ECO:0000269|PubMed:23806335,
CC ECO:0000269|PubMed:24066155, ECO:0000269|PubMed:25422944,
CC ECO:0000269|PubMed:27039057}.
CC -!- FUNCTION: [Isoform a]: Required for migration of HSN motor neurons
CC during embryogenesis. {ECO:0000269|PubMed:24558261}.
CC -!- SUBUNIT: Multimer; in vitro (PubMed:23806335). Interacts (via C-
CC terminus) with dot-1.1 to form a heterodimer known as the zfp-1-dot-1.1
CC complex or DotCom complex (PubMed:23806335).
CC {ECO:0000269|PubMed:23806335}.
CC -!- INTERACTION:
CC P34447; Q6AW06: dot-1.1; NbExp=3; IntAct=EBI-6740300, EBI-21195283;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23263989,
CC ECO:0000305|PubMed:21980302, ECO:0000305|PubMed:23806335}. Chromosome
CC {ECO:0000269|PubMed:23263989, ECO:0000305|PubMed:23806335}.
CC Note=Localizes to all six condensed chromosomes (PubMed:23263989). zfp-
CC 1 and dot-1.1 colocalize to promoters of highly expressed genes
CC (PubMed:23806335). {ECO:0000269|PubMed:23263989,
CC ECO:0000269|PubMed:23806335}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F54F2.2a}; Synonyms=Long
CC {ECO:0000303|PubMed:23263989};
CC IsoId=P34447-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F54F2.2b};
CC IsoId=P34447-2; Sequence=VSP_060338, VSP_060339;
CC Name=c {ECO:0000312|WormBase:F54F2.2c}; Synonyms=Short
CC {ECO:0000303|PubMed:23263989};
CC IsoId=P34447-3; Sequence=VSP_060337;
CC -!- TISSUE SPECIFICITY: Isoform a: Expressed at high levels in maturing
CC oocytes, but at low levels in the rest of the germ line (at protein
CC level) (PubMed:23263989). Isoform a: Not expressed in the pharynx, germ
CC line and tail (PubMed:27039057). Isoform c: Not expressed in the germ
CC line (at protein level) (PubMed:23263989). Isoform c: Uniformly
CC expressed (PubMed:27039057). {ECO:0000269|PubMed:23263989,
CC ECO:0000269|PubMed:27039057}.
CC -!- DEVELOPMENTAL STAGE: Expressed in somatic cells throughout development
CC (at protein level) (PubMed:23263989). Isoform a: Predominantly
CC expressed in embryos and adults (at protein level) (PubMed:23263989).
CC Isoform c: Abundant at larval stages (at protein level)
CC (PubMed:23263989). {ECO:0000269|PubMed:23263989}.
CC -!- DOMAIN: The PHD-type zinc finger 1 most likely mediates nuclear
CC localization. {ECO:0000305|PubMed:23263989,
CC ECO:0000305|PubMed:23806335}.
CC -!- DOMAIN: The ePHD2 domain folds as an integrated structural module
CC comprizing the C2HC pre-PHD-type 2 zinc finger and the PHD-type 2 zinc
CC finger. It mediates non-specific binding to dsDNA, but does not bind
CC histones in contrast to many PHD-type zinc fingers.
CC {ECO:0000305|PubMed:23263989, ECO:0000305|PubMed:23806335}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in developmental
CC defects such as slow growth, protruding vulva, and a reduced brood size
CC (PubMed:16710447). RNAi-mediated knockdown results in germ line
CC defects, resulting in no embryos or impaired oogenesis
CC (PubMed:23263989). RNAi-mediated knockdown suppresses the multivulval
CC phenotype of the lin-15A-lin15B n765 mutant (PubMed:16507136,
CC PubMed:16710447). RNAi-mediated knockdown shortens the lifespan of daf-
CC 2 e1370 mutants (PubMed:27039057). {ECO:0000269|PubMed:16507136,
CC ECO:0000269|PubMed:16710447, ECO:0000269|PubMed:23263989,
CC ECO:0000269|PubMed:27039057}.
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DR EMBL; BX284603; CCD71235.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD71236.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD71237.1; -; Genomic_DNA.
DR PIR; S44827; S44827.
DR PIR; S44829; S44829.
DR RefSeq; NP_001022610.1; NM_001027439.1. [P34447-2]
DR RefSeq; NP_001022611.1; NM_001027440.3.
DR RefSeq; NP_498943.2; NM_066542.7.
DR AlphaFoldDB; P34447; -.
DR SMR; P34447; -.
DR BioGRID; 41439; 21.
DR ComplexPortal; CPX-4127; ZFP-1(AF10)/DOT-1 complex.
DR IntAct; P34447; 14.
DR STRING; 6239.F54F2.2a.2; -.
DR iPTMnet; P34447; -.
DR EPD; P34447; -.
DR PaxDb; P34447; -.
DR PeptideAtlas; P34447; -.
DR EnsemblMetazoa; F54F2.2a.1; F54F2.2a.1; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2a.2; F54F2.2a.2; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2a.3; F54F2.2a.3; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2a.4; F54F2.2a.4; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2a.5; F54F2.2a.5; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2a.6; F54F2.2a.6; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2a.7; F54F2.2a.7; WBGene00006975. [P34447-1]
DR EnsemblMetazoa; F54F2.2b.1; F54F2.2b.1; WBGene00006975. [P34447-2]
DR EnsemblMetazoa; F54F2.2c.1; F54F2.2c.1; WBGene00006975. [P34447-3]
DR EnsemblMetazoa; F54F2.2c.2; F54F2.2c.2; WBGene00006975. [P34447-3]
DR GeneID; 176237; -.
DR KEGG; cel:CELE_F54F2.2; -.
DR CTD; 176237; -.
DR WormBase; F54F2.2a; CE25003; WBGene00006975; zfp-1. [P34447-1]
DR WormBase; F54F2.2b; CE26933; WBGene00006975; zfp-1. [P34447-2]
DR WormBase; F54F2.2c; CE33653; WBGene00006975; zfp-1. [P34447-3]
DR eggNOG; KOG0956; Eukaryota.
DR GeneTree; ENSGT00940000174200; -.
DR HOGENOM; CLU_014639_0_0_1; -.
DR InParanoid; P34447; -.
DR OMA; AKKGACM; -.
DR OrthoDB; 566217at2759; -.
DR PhylomeDB; P34447; -.
DR PRO; PR:P34447; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006975; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:WormBase.
DR GO; GO:0005694; C:chromosome; IC:ComplexPortal.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003682; F:chromatin binding; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:WormBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034729; P:histone H3-K79 methylation; IC:ComplexPortal.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Chromatin regulator;
KW Chromosome; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..867
FT /note="Zinc finger protein zfp-1"
FT /id="PRO_0000065361"
FT ZN_FING 5..57
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 69..102
FT /note="C2HC pre-PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 125..186
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 69..186
FT /note="Extended PHD2 domain (ePHD2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 267..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 4
FT /note="Required for binding to histone H3 methylated at
FT 'Lys-4' in vitro"
FT /evidence="ECO:0000269|PubMed:23263989"
FT VAR_SEQ 1..232
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060337"
FT VAR_SEQ 1..211
FT /note="MKEMVGGCCVCADENGWTDNPLIYCDGENCEVAVHQGCYGIQEVPEGEWFCA
FT KCTKASAMMPGSINEATFCCQLCPFDYGALKKTDRNGWAHVICALYIPEVRFGNVHSME
FT PVILNDVPTDKFNKLCYICNEERPNDAKKGACMSCNKSTCKRSFHVTCAQRKGLLCEEG
FT AISRNVKYCGYCENHLKKAINDPAIKVIPACPPVQRLSKEQ -> MGKRSVSMFLIDIS
FT LFLLLGTLIVACTVKKEKIKERHNHNRTLLKRTVGGKRKDTGHRHRTSTIPPRDKSSLH
FT APTVKNGNSLSAVEPNGRIKIGYRLSPSVKKGEIVAPKATVTPAVNTRKPINEAISEGI
FT ILDPTYFKNGGNLDSKSPKNQKLAEELQQFIDNPGLGSNETSTLTDDNDVPRVVAVPSQ
FT CKMFETTNQPTNSQLLLNSE (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060338"
FT VAR_SEQ 212..867
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060339"
FT MUTAGEN 4
FT /note="M->D: Preferentially binds to the unmethylated 'Lys
FT 4' residue of histone H3."
FT /evidence="ECO:0000269|PubMed:23263989"
FT MUTAGEN 601..867
FT /note="Missing: In op481; defects in axon guidance in D-
FT type motor neurons in a sdn-1 (zh20) mutant background."
FT /evidence="ECO:0000269|PubMed:24066155"
SQ SEQUENCE 867 AA; 92190 MW; 7E582DC2529CFEAD CRC64;
MKEMVGGCCV CADENGWTDN PLIYCDGENC EVAVHQGCYG IQEVPEGEWF CAKCTKASAM
MPGSINEATF CCQLCPFDYG ALKKTDRNGW AHVICALYIP EVRFGNVHSM EPVILNDVPT
DKFNKLCYIC NEERPNDAKK GACMSCNKST CKRSFHVTCA QRKGLLCEEG AISRNVKYCG
YCENHLKKAI NDPAIKVIPA CPPVQRLSKE QDKKKTVLLT SLPLPPPAPR LHMLADPLPI
KSNKVNNVLG LGSAINAVSL EERPASGSTV NSGIFVPPPT AFSPPLTTSS RSSVAQDPSP
PLTINKNSLS SSGPLIPSTA HLSATTASAT PIMANGSTLP PSSETTVGTH CLQQLQIQSA
AAAAITQNQI GPSELNGYPA ASQLSSFMHE IPARNTTSVA SLLPPGAAEY HLNGSGDEEK
TVKAVLTAPL TKAKRIRDSK NDMMDKTHKR PRANARPPAV LGSMSSGSSG GTVGKSPSMQ
RLQNLVAPIV SETVTDFQRD RVADRTAAER RAAAAQSQPS TSTNGGPNVT IPAVVEVHTN
STNSTNHQNN GLTQNAPAST SMQAGTSSND GVISQNGTSS TSQSNRLNLP SFMEQLLERQ
WDQGSSLLMA NAHFDVAQLL SCLFQLKSEN FRLEENLSGL RKRRDHLFAL NSRLAEVNTL
DVSKRQRSDG LLLQQQIAHH LDPTSIVPKA EVHKQEPLSA PTSVPLPANH SSSLFEDIKA
PKATYSRKTP SNIPLTVPLS TAATALTTTT AASSGAPVNS NIQNHRATPS TAGAPMAATP
IMTAVTSANE LAALSPERAQ ALLNMYRMPL DANVAAQLSM ITNFPGQVNP SLFSRLLAVN
MMNGGLQPNG QPLSALPPPT SATPNGK
