ZC3HE_CAEEL
ID ZC3HE_CAEEL Reviewed; 740 AA.
AC Q95XU6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14;
DE AltName: Full=Suppressor of tau pathology protein 2;
GN Name=sut-2; ORFNames=Y61A9LA.8;
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=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]
RP SUBCELLULAR LOCATION.
RX PubMed=19273536; DOI=10.1093/hmg/ddp099;
RA Guthrie C.R., Schellenberg G.D., Kraemer B.C.;
RT "SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 18:1825-1838(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19273536}. Cytoplasm
CC {ECO:0000269|PubMed:19273536}. Note=Mainly nuclear. Small amounts are
CC found in the cytoplasm.
CC -!- SIMILARITY: Belongs to the ZC3H14 family. {ECO:0000305}.
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DR EMBL; FO081464; CCD71770.1; -; Genomic_DNA.
DR RefSeq; NP_504239.2; NM_071838.5.
DR AlphaFoldDB; Q95XU6; -.
DR SMR; Q95XU6; -.
DR BioGRID; 43899; 3.
DR STRING; 6239.Y61A9LA.8; -.
DR EPD; Q95XU6; -.
DR PaxDb; Q95XU6; -.
DR PeptideAtlas; Q95XU6; -.
DR EnsemblMetazoa; Y61A9LA.8a.1; Y61A9LA.8a.1; WBGene00022019.
DR GeneID; 178847; -.
DR KEGG; cel:CELE_Y61A9LA.8; -.
DR UCSC; Y61A9LA.8; c. elegans.
DR CTD; 178847; -.
DR WormBase; Y61A9LA.8a; CE31123; WBGene00022019; sut-2.
DR eggNOG; KOG3702; Eukaryota.
DR GeneTree; ENSGT00440000038430; -.
DR HOGENOM; CLU_022605_0_0_1; -.
DR InParanoid; Q95XU6; -.
DR OMA; FCEYYHP; -.
DR OrthoDB; 893844at2759; -.
DR PhylomeDB; Q95XU6; -.
DR PRO; PR:Q95XU6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00022019; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q95XU6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR Gene3D; 1.10.340.40; -; 1.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR043094; Nab2/ZC3H14_N_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; PTHR14738; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..740
FT /note="Zinc finger CCCH domain-containing protein 14"
FT /id="PRO_0000405583"
FT ZN_FING 499..522
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 523..543
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 668..691
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 674..691
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 693..709
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 82..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 82854 MW; F3B8A5C873C58A6D CRC64;
MNTQTGTGTS EVSKKLKAAI RAKLEELGVY VDDELPDYIM VMIANKKEKV QMKDDLNLFI
GKSTAKFVDW LFDLFDRLQN ASNKQGETSK KEEDKRKELE ATAAAKEHEE KRRKEKEEHE
KELQKEKERE KERQRERDRE KRAEEEKRRE EKRKEIQRSK RRRTRSRSNT YSDEEEHVRA
RGEKHDRHHH KDHRRGRSHE RKIITSTIVR QASASPDKKL HSTVTVKRNI RPTGDQNIKG
RGTMFLRAMN EASVSAGYGS SSKRSETHHE DDMSDVEALP SKPASTKSPK KSIRDRMSRI
SKTSEPPIEE DDAVVLEDFA QTGGGPQMIL KLSGGREAIK KTRIQDRIVV DDGLRRGLLK
RKIETASGAS AGAATSEEPK SKHDRIIFDI TPSRDSTPTD DSPTMQKWNG QIEIGDDSEE
SEDDEEAEID AFVAEARGIA RRESFRDEED ELPPTHQLSG GPYAYHHSTA APTYIPTPLS
VLSEQQNQMG GGAAKEDHHV KERCIFWPKC TKGDTCAFMH PTTNCKNFPN CTFGIRCLFI
HPPCRFDRFC TKKHCPFTHH GTGGQQPGGA QLTSEFKNPL TSSRMLTVPS PFIAATAAAV
EELPKPAARG ALGSLAEKLA ASIKKKPAPG AESEKKEEKS DENESKAEEP KAEVAPVQPK
PLPDIAPLHS MVLCRYAGAC RNPICHFKHP KECRFGANCR NPSCYFYHKP AGAAPTPVAA
PIAAESAGAA KYKWTSATAN
