ZC3HE_BOVIN
ID ZC3HE_BOVIN Reviewed; 735 AA.
AC Q3ZC82;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14;
GN Name=ZC3H14;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in poly(A) tail length control in neuronal cells.
CC Binds the polyadenosine RNA oligonucleotides.
CC {ECO:0000250|UniProtKB:Q6PJT7}.
CC -!- SUBUNIT: Interacts with HOOK2. Interacts with ZFC3H1 in a RNase-
CC sensitive manner. {ECO:0000250|UniProtKB:Q6PJT7}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q8BJ05}.
CC Note=Colocalizes with poly(A) RNA in nuclear speckles.
CC {ECO:0000250|UniProtKB:Q8BJ05}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3ZC82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3ZC82-2; Sequence=VSP_033161;
CC -!- SIMILARITY: Belongs to the ZC3H14 family. {ECO:0000305}.
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DR EMBL; AAFC03026649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC102847; AAI02848.1; -; mRNA.
DR RefSeq; NP_001029578.1; NM_001034406.2. [Q3ZC82-2]
DR RefSeq; NP_001159774.1; NM_001166302.1.
DR AlphaFoldDB; Q3ZC82; -.
DR STRING; 9913.ENSBTAP00000040586; -.
DR iPTMnet; Q3ZC82; -.
DR PaxDb; Q3ZC82; -.
DR PRIDE; Q3ZC82; -.
DR Ensembl; ENSBTAT00000086942; ENSBTAP00000064177; ENSBTAG00000030453. [Q3ZC82-1]
DR GeneID; 511473; -.
DR KEGG; bta:511473; -.
DR CTD; 79882; -.
DR VEuPathDB; HostDB:ENSBTAG00000030453; -.
DR eggNOG; KOG3702; Eukaryota.
DR GeneTree; ENSGT00440000038430; -.
DR InParanoid; Q3ZC82; -.
DR OMA; TFYHPTV; -.
DR OrthoDB; 893844at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000030453; Expressed in spermatid and 103 other tissues.
DR ExpressionAtlas; Q3ZC82; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; PTHR14738; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..735
FT /note="Zinc finger CCCH domain-containing protein 14"
FT /id="PRO_0000331310"
FT ZN_FING 595..620
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 621..640
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 641..656
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 681..698
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 700..718
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 79..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ05"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ05"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 357
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ05"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT VAR_SEQ 452..582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033161"
SQ SEQUENCE 735 AA; 82023 MW; 16BD94BA28B2EA0A CRC64;
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
RFTVWLHGVL DKLRSVTTDP ASLKSSDTNL FDGNVPSNKS SFSRGDERRH EAAVPPLAVS
STRPEKRESR VSTSSQEQKA TNVRQTYDDG AATRLMSTVK PLRELAPSED VIDIKPEPDD
LIDEDLNFVQ ENPLSQKKTT VTLTYGSSRP SIEIYRPPAT RNTDSGAHLN RLQFQQQQNS
IHAAKQLDIQ SSRVYETGRL CEPEVLNSLE ETYSPFFRSN AEKMSIEEEN FRKRKLPVVS
SVVKVKKFSH DGEEEEEDDD CGSRTGSISS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
EAQESVTKTT NYSTVSQKQT LPVAPRTRTS QEDLLAEVAQ GHGRVPRISS PVKEEEAQGG
SVDERQGTQQ RQLLSRLQID PVMAETLQIS QDYYDMESMV HADTRSFILK KPKLCEELVV
AASQASGMET ADALQARSGH LVQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEDMC
SEGMRPAQHP AASHGGLAGL LHPQRSRVLS RQLEDPDGSF ANAEMSELSV AQKPEKLLER
CKYWPACKNG DECAYHHPVS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKP DCPFTHMSRR
TPGLPPKPVT APAPPSSSQL CRYFPACKKM ECPFYHPKHC RFNTQCTRPD CAFYHPTITV
PPRHALKWIR PQTSD
