ZTF16_CAEEL
ID ZTF16_CAEEL Reviewed; 480 AA.
AC H2L008; Q5WRS1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Zinc finger protein ztf-16 {ECO:0000305};
GN Name=ztf-16 {ECO:0000303|PubMed:20026024, ECO:0000312|WormBase:R08E3.4b};
GN ORFNames=R08E3.4 {ECO:0000312|WormBase:R08E3.4b};
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20026024; DOI=10.1016/j.ydbio.2009.12.013;
RA Large E.E., Mathies L.D.;
RT "hunchback and Ikaros-like zinc finger genes control reproductive system
RT development in Caenorhabditis elegans.";
RL Dev. Biol. 339:51-64(2010).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 131-GLN--ALA-480 AND 236-ARG--ALA-480.
RX PubMed=22298710; DOI=10.1534/genetics.111.137786;
RA Procko C., Lu Y., Shaham S.;
RT "Sensory organ remodeling in Caenorhabditis elegans requires the zinc-
RT finger protein ZTF-16.";
RL Genetics 190:1405-1415(2012).
CC -!- FUNCTION: Positively regulates the expression of ver-1 in the amphid
CC sheath glia of amphid sensory neurons (PubMed:22298710). Together with
CC ehn-3, plays a role in somatic gonad development and is required for
CC proper gonadal primordium assembly and somatic gonad precursor cell
CC morphology (PubMed:20026024). {ECO:0000269|PubMed:20026024,
CC ECO:0000269|PubMed:22298710}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22298710}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:R08E3.4b};
CC IsoId=H2L008-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:R08E3.4a};
CC IsoId=H2L008-2; Sequence=VSP_060358, VSP_060359;
CC -!- TISSUE SPECIFICITY: Expressed in the somatic gonad, hypodermis and
CC cells in the head and tail (PubMed:20026024). Expressed in amphid and
CC phasmid sheath glia, amphid and phasmid socket glia, and in neurons in
CC the head (PubMed:22298710). {ECO:0000269|PubMed:20026024,
CC ECO:0000269|PubMed:22298710}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryos to adults
CC (PubMed:20026024). First expressed in somatic gonadal precursor cells
CC during embryogenesis (PubMed:20026024). In the L2 larval stage of
CC development, expressed in Z1.pa and Z4.ap distal tip cells and their
CC descendants (PubMed:20026024). {ECO:0000269|PubMed:20026024}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not cause defects in
CC somatic gonad development (PubMed:20026024). RNAi-mediated knockdown in
CC a ehn-3 rd2 mutant background enhances the defects in gonadal
CC development in the ehn-3 single mutant (PubMed:20026024).
CC {ECO:0000269|PubMed:20026024}.
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BX284606; CCD70858.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD70859.1; -; Genomic_DNA.
DR RefSeq; NP_001024850.1; NM_001029679.3. [H2L008-2]
DR RefSeq; NP_001024851.1; NM_001029680.3. [H2L008-1]
DR AlphaFoldDB; H2L008; -.
DR SMR; H2L008; -.
DR IntAct; H2L008; 50.
DR STRING; 6239.R08E3.4b; -.
DR EPD; H2L008; -.
DR PaxDb; H2L008; -.
DR PeptideAtlas; H2L008; -.
DR EnsemblMetazoa; R08E3.4a.1; R08E3.4a.1; WBGene00019960. [H2L008-2]
DR EnsemblMetazoa; R08E3.4b.1; R08E3.4b.1; WBGene00019960. [H2L008-1]
DR GeneID; 180756; -.
DR KEGG; cel:CELE_R08E3.4; -.
DR UCSC; R08E3.4b; c. elegans.
DR CTD; 180756; -.
DR WormBase; R08E3.4a; CE37662; WBGene00019960; ztf-16. [H2L008-2]
DR WormBase; R08E3.4b; CE37663; WBGene00019960; ztf-16. [H2L008-1]
DR eggNOG; KOG1601; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00720000109290; -.
DR HOGENOM; CLU_016943_1_0_1; -.
DR InParanoid; H2L008; -.
DR OMA; NICKRAF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; H2L008; -.
DR SignaLink; H2L008; -.
DR PRO; PR:H2L008; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00019960; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008406; P:gonad development; IGI:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..480
FT /note="Zinc finger protein ztf-16"
FT /id="PRO_0000448221"
FT ZN_FING 5..27
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 103..125
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 133..155
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 161..183
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 190..215
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 223..246
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 420..442
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..472
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 25..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 421..447
FT /note="ECCHCGMMFYDNTMYLLHKSLHSDGDP -> VCVIANNNLLLKMSPFCLPFF
FT EVQLEL (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060358"
FT VAR_SEQ 448..480
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060359"
FT MUTAGEN 131..480
FT /note="Missing: In ns169; reduces expression of ver-1 in
FT amphid sheath glia."
FT /evidence="ECO:0000269|PubMed:22298710"
FT MUTAGEN 236..480
FT /note="Missing: In ns178 and ns171; defective amphid glia
FT remodeling. Reduces expression of ver-1 in amphid sheath
FT glia."
FT /evidence="ECO:0000269|PubMed:22298710"
SQ SEQUENCE 480 AA; 54081 MW; D3D32ECE232B4450 CRC64;
MDELNACTEC GFTTTVFSEF QGHIEKHENE HSRSSSGEMS NSQTIEWGDG IQSSTPSPRS
TPPSDPTPSP DSDEHLEHHI SITEITNTLI KKEPGTKGQK TVHVCPHCNF TTCMSQHMKS
HLEAHERHQG QMYQCDICKM QFSQKANMHR HRMRHSGVKP YECRFCKKRF FRKDQMQEHS
MTHIKTGFGF DCPVSQCNMQ FSQHNALRAH LEETHTISST NPASCKRCNL MFANSRRLLL
HFQTRHDDSE SSPKKENTPK RKKLSNGNAL PMDPANMSIT EQLQRMVKSE FSPPNTDTSD
NSTSSEFDKI PPSFPMANPD ILLMCLNQMN QFNGFGENIP RPMLNIPNIP LPALHNIPAV
AAIVKQDQVQ LWSEQTSSSV SVSAPSPSEQ SHSPPANESS LSLTEKEKSP TPEKEDEENV
ECCHCGMMFY DNTMYLLHKS LHSDGDPFKC ALCGTQCGEK YMFTTHVIFA DHSTQATTSA
