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Database: UniProt
Entry: A0A2U4A1K9_TURTR
LinkDB: A0A2U4A1K9_TURTR
Original site: A0A2U4A1K9_TURTR 
ID   A0A2U4A1K9_TURTR        Unreviewed;       677 AA.
AC   A0A2U4A1K9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 14 {ECO:0000256|ARBA:ARBA00015071, ECO:0000256|RuleBase:RU369058};
GN   Name=ZC3H14 {ECO:0000313|RefSeq:XP_019774882.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019774882.1};
RN   [1] {ECO:0000313|RefSeq:XP_019774882.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019774882.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_019774882.1; XM_019919323.2.
DR   AlphaFoldDB; A0A2U4A1K9; -.
DR   GeneID; 101327980; -.
DR   OrthoDB; 5400456at2759; -.
DR   Proteomes; UP000245320; Chromosome 2.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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   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:UP000245320};
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          536..561
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         536..561
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  76063 MW;  B50E83B2836343BA CRC64;
     MLQRSRLHGV LDKLRSVTTD PSSLKSSDTN IFDSNVPSNK SSFSRGDERR HEAAVPPLAV
     SSTRPEKRES RVSTSSQEQK ATNVRQTYDD GAATRLMSTV KPLREPAPSE DVIDIKPEPD
     DLIDEDLNFV QENPLSQKKP TVTLTYGSSR PSIEIYRPPA SRNADSGAHL NRLQFQQQQN
     SIHAAKQLDI QTSRIYETGR LCEPEVLNSL EETYSPFFRN SSEKMSIEEE NFRKRKLPVV
     SSVVKVKKFN HDGEEEEEDD DCGSRTGSIS SSVSVPAKPE RRPSLPPSKQ ANKNLILKAI
     SEAQESVTKT TNYSAVSQKQ TLPVAPRTRT SQEELLAEMV QGQSRAPRMS SPIKEEETKG
     DNIDKSQGTQ QRQLLSRLQI DPVMAETLQI SQDYYDMESM VHADTRSFIL KKPKLSEEIV
     VAPNQESGMK TADTLRVLSG HLMQTRDLVQ PDKPASPKFI VTLDGVPSPP GYMSDQEEDM
     SFEGMRPAHH TAASHEGLAG LLHPQQLHLL SRQLEDPDGS FTNAEMSELS VAQKPEKLLE
     RCKYWPACKN GDECAYHHPV SPCKAFPNCK FAEKCLFVHP NCKYDAKCTK PECPFTHMSR
     RIPVLPPKPA VTTPAPPSSS QLCRYFPACK KMECPFYHPK HCRFNTQCTR PDCTFYHPTI
     TVPPRHALKW IRPQTSE
//
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