ID H0WRX8_OTOGA Unreviewed; 736 AA.
AC H0WRX8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14 {ECO:0000256|ARBA:ARBA00015071, ECO:0000256|RuleBase:RU369058};
GN Name=ZC3H14 {ECO:0000313|Ensembl:ENSOGAP00000004809.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000004809.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000004809.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in poly(A) tail length control in neuronal cells.
CC Binds the polyadenosine RNA oligonucleotides.
CC {ECO:0000256|ARBA:ARBA00003177, ECO:0000256|RuleBase:RU369058}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|RuleBase:RU369058}.
CC Note=Colocalizes with poly(A) RNA in nuclear speckles.
CC {ECO:0000256|RuleBase:RU369058}.
CC -!- SIMILARITY: Belongs to the ZC3H14 family.
CC {ECO:0000256|ARBA:ARBA00008423, ECO:0000256|RuleBase:RU369058}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAQR03045982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03045983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WRX8; -.
DR STRING; 30611.ENSOGAP00000004809; -.
DR Ensembl; ENSOGAT00000005378.2; ENSOGAP00000004809.2; ENSOGAG00000005373.2.
DR eggNOG; KOG3702; Eukaryota.
DR GeneTree; ENSGT00440000038430; -.
DR HOGENOM; CLU_022605_0_0_1; -.
DR InParanoid; H0WRX8; -.
DR OMA; HPKCKFG; -.
DR TreeFam; TF329509; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:1904115; C:axon cytoplasm; IEA:Ensembl.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008143; F:poly(A) binding; IEA:UniProtKB-UniRule.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:UniProtKB-UniRule.
DR Gene3D; 4.10.1000.30; -; 1.
DR Gene3D; 4.10.1000.40; -; 1.
DR Gene3D; 1.20.1390.10; PWI domain; 1.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1.
DR PANTHER; PTHR14738:SF29; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1.
DR Pfam; PF14608; zf-CCCH_2; 5.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369058};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369058};
KW RNA-binding {ECO:0000256|RuleBase:RU369058};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 595..620
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 595..620
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 77..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 82986 MW; B108864B595406A8 CRC64;
MEIGTEISRK IRSAIKGKLQ ELGAYIDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
RFTVWLHGVL DKLRSVTTEP SSLKSSDTNI FDSSVPSNKS NFSRGDERRH EAAVPPLTIS
NSRPEKRNSR VSTSSQEQKT TNVRQTYDDG AATRLMSTVK PLREPAPSED VIDIKPEPDD
LIDEDLNFVQ ENSLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADCGVHLN RMQFQQQQNS
IHAAKQLDIQ NSRVYEAGHL CEPEMLNSLE ETYSPFFRNN SEKMSIEDEN FRKRKLPVVS
SVVKVKKFNH DGEEEEEDDD YGSRTGGVSS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
EAQESVTKTT NYSTVPQKQT LPVAPRTRTS QEDLLAEVVQ GQSRTPRISP PIKEEETKGD
NIEKNQGTQQ RQLLSRLQID PVMAETLQIS QDYYDMESMV HADTRSFILK KPKLSEEVVV
TPTQESGMKT ADTLRVLSGH LIHTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEDMC
FEGMKPVNQT AASNKGLRGL LHPQQLQLLS RQLEDPNGSF SNAEISELSV TQKPEKLLER
CKYWPACKNG DECAYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKP DCPFTHMSRR
IPVLPPKPAV TAPPTPSSSQ LCRYFPACKK MECPFYHPKH CRFNTQCTRP DCTFYHPTIT
VPPRHALKWI RPQTSK
//
