PZF1_CAEEL
ID PZF1_CAEEL Reviewed; 504 AA.
AC G5EGQ2; G5EGG3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Paired zinc finger protein 1 {ECO:0000303|PubMed:17096596, ECO:0000312|WormBase:T05G11.1a};
GN Name=pzf-1 {ECO:0000312|WormBase:T05G11.1a};
GN ORFNames=T05G11.1 {ECO:0000312|WormBase:T05G11.1a};
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17096596; DOI=10.1371/journal.pgen.0020174;
RA Leacock S.W., Reinke V.;
RT "Expression profiling of MAP kinase-mediated meiotic progression in
RT Caenorhabditis elegans.";
RL PLoS Genet. 2:e174-e174(2006).
CC -!- FUNCTION: Possible transcriptional regulator (Probable). Involved in
CC promoting segregation of chromosomes during meiosis, perhaps acting
CC downstream of the let-60 RAS / mpk-1 MAPK signaling pathway
CC (PubMed:17096596). {ECO:0000269|PubMed:17096596,
CC ECO:0000305|PubMed:17096596}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T05G11.1a};
CC IsoId=G5EGQ2-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T05G11.1b};
CC IsoId=G5EGQ2-2; Sequence=VSP_061536;
CC -!- TISSUE SPECIFICITY: Expressed in proximal gonad.
CC {ECO:0000269|PubMed:17096596}.
CC -!- DISRUPTION PHENOTYPE: Superficially wild-type, with a normal brood
CC size, but drastic reduction in brood size when grown at a permissive
CC temperature of 20 degrees Celsius in an mpk-1 mutant background. Double
CC mutant mpk-1;pzf-1 shows meiotic chromosome non-disjunction, increased
CC embryonic lethality and also an abnormal male:hermaphrodite ratio, at
CC 23 degrees Celsius. {ECO:0000269|PubMed:17096596}.
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DR EMBL; BX284605; CAA19434.2; -; Genomic_DNA.
DR EMBL; BX284605; CBW48438.1; -; Genomic_DNA.
DR RefSeq; NP_001256688.1; NM_001269759.1.
DR RefSeq; NP_001256689.1; NM_001269760.1.
DR IntAct; G5EGQ2; 1.
DR STRING; 6239.T05G11.1a; -.
DR PaxDb; G5EGQ2; -.
DR EnsemblMetazoa; T05G11.1a.1; T05G11.1a.1; WBGene00011505.
DR GeneID; 188142; -.
DR KEGG; cel:CELE_T05G11.1; -.
DR CTD; 188142; -.
DR WormBase; T05G11.1a; CE42296; WBGene00011505; pzf-1.
DR WormBase; T05G11.1b; CE45365; WBGene00011505; pzf-1.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_541043_0_0_1; -.
DR InParanoid; G5EGQ2; -.
DR OMA; HFSRMGN; -.
DR OrthoDB; 1600969at2759; -.
DR PhylomeDB; G5EGQ2; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011505; Expressed in germ line (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EGQ2; 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:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IGI:WormBase.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IGI:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001781; Znf_LIM.
DR SMART; SM00355; ZnF_C2H2; 8.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; LIM domain; Metal-binding; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..504
FT /note="Paired zinc finger protein 1"
FT /id="PRO_0000455833"
FT ZN_FING 12..35
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 39..62
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 68..91
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 179..202
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 206..229
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..258
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..332
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..389
FT /note="C2H2-type 8; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061536"
SQ SEQUENCE 504 AA; 57123 MW; F8B4DB3E285A3A14 CRC64;
MDYVNRNLDD KLLCGICGKY FSDDESLREH RRQRHMTCHM CLLCNRRIPE NETLREHMKN
KHNIWKLFIC VCCNWSFGTE IYLKCHEECM KSTGRPGLLK PLAMPMTAPA REASALNTDP
QNGSDDVPHS SPSPVPMIAE NSIIQASSLK MEPIESADRS SASTSTPRTL VSGTPREKIP
CGFCGKDFFH EGSLREHRRR FHMTGHTCLL CNRQIPENET VRDHMKSQHN IKKVYNCLCC
NWTFLNQVHL ISHKTCLKQT GKPCCRPGHM EPLAIPRTAS IRQFFTLKTE TQSGDDDSAA
GSQLFSARLS CKSCGKFFYS ERSLSKHHRQ IHMSGHVCVL CNHQMPKTVT VQEHMEKEHN
IRLVFNCRCC NWSFATRRCL MSHVECLKKA GDARNVKPVA IPRMAADSIL QSLKESEAQE
YPDFSAASTT SSGPASTLKT PRMDFKKNLK ICTDAVQILV GNGLFSNEQL AQTETWVMIF
SNANKLFHSM NSFGEPSVSR DIPM
