ZC3HE_RAT
ID ZC3HE_RAT Reviewed; 736 AA.
AC Q7TMD5; Q7TSK6; Q99NC1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14;
DE AltName: Full=Nuclear protein UKp83/UKp68;
GN Name=Zc3h14; Synonyms=Npuk68;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Hara M., Watabe S., Igarashi J., Yamashita K., Yokosuka M., Iigo M.,
RA Ohtani-Kaneko R., Hirata K.;
RT "Antigens recognized by antibody against isolated chromatin fraction from
RT rat liver cells.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=21734151; DOI=10.1073/pnas.1107103108;
RA Pak C., Garshasbi M., Kahrizi K., Gross C., Apponi L.H., Noto J.J.,
RA Kelly S.M., Leung S.W., Tzschach A., Behjati F., Abedini S.S., Mohseni M.,
RA Jensen L.R., Hu H., Huang B., Stahley S.N., Liu G., Williams K.R.,
RA Burdick S., Feng Y., Sanyal S., Bassell G.J., Ropers H.H., Najmabadi H.,
RA Corbett A.H., Moberg K.H., Kuss A.W.;
RT "Mutation of the conserved polyadenosine RNA binding protein, ZC3H14/dNab2,
RT impairs neural function in Drosophila and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12390-12395(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:21734151}.
CC Note=Colocalizes with poly(A) RNA in nuclear speckles.
CC {ECO:0000269|PubMed:21734151}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=UKp83;
CC IsoId=Q7TMD5-1; Sequence=Displayed;
CC Name=2; Synonyms=UKp68;
CC IsoId=Q7TMD5-2; Sequence=VSP_033181;
CC -!- SIMILARITY: Belongs to the ZC3H14 family. {ECO:0000305}.
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DR EMBL; AB032932; BAB40453.1; -; mRNA.
DR EMBL; AB097075; BAC76890.1; -; mRNA.
DR EMBL; AB097076; BAC76891.1; -; mRNA.
DR EMBL; AB097077; BAC76892.1; -; mRNA.
DR EMBL; BC087712; AAH87712.1; -; mRNA.
DR RefSeq; NP_001029123.1; NM_001033951.1. [Q7TMD5-1]
DR RefSeq; NP_620275.1; NM_138920.1. [Q7TMD5-2]
DR AlphaFoldDB; Q7TMD5; -.
DR BioGRID; 251412; 1.
DR STRING; 10116.ENSRNOP00000047580; -.
DR iPTMnet; Q7TMD5; -.
DR PhosphoSitePlus; Q7TMD5; -.
DR jPOST; Q7TMD5; -.
DR PRIDE; Q7TMD5; -.
DR GeneID; 192359; -.
DR KEGG; rno:192359; -.
DR UCSC; RGD:621850; rat. [Q7TMD5-1]
DR CTD; 79882; -.
DR RGD; 621850; Zc3h14.
DR eggNOG; KOG3702; Eukaryota.
DR InParanoid; Q7TMD5; -.
DR OrthoDB; 893844at2759; -.
DR PhylomeDB; Q7TMD5; -.
DR PRO; PR:Q7TMD5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1904115; C:axon cytoplasm; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
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 PROSITE; PS50103; ZF_C3H1; 3.
PE 1: Evidence at protein 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..736
FT /note="Zinc finger CCCH domain-containing protein 14"
FT /id="PRO_0000331314"
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 682..699
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 701..719
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 77..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..420
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 135..153
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:0007744|PubMed:22673903"
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 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 CROSSLNK 489
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|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_033181"
FT CONFLICT 681
FT /note="F -> L (in Ref. 1; BAC76891 and 2; AAH87712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 82632 MW; 35A0F305E2B0C7D1 CRC64;
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
RFTVWLHGVL DKLRSVTTEP SSLKSPDTSI FDSNVPSNKS SFSRGDERRH EAAIPPLAVS
SSRPEKRDSR VSTSSQEHKS TNVRHSYDDG ASTRLMSTVK PLREPAPSED VIDIKPEPDD
LIDEDLNFVQ ENSLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADTGTHLN RPQLQQQQSS
THTAKQLDGQ SSQVYEAGRL CEPEVLGSVE DTYSPFFRNN LDKMNIEEEN FRKRKLPVVS
SVVKVKRFSH DGEEEEEDED YGTRVGSLSS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
EAQESVTKTT NYPAVPQKQT LPVAPRTRTS QEEVLAEMVQ GQNRAPRISP PVKEEEAKGD
NAEKIEGTQQ RQLLSRLQID PVTVDTMELS QDYYDMESMV HADTRSFILK KPKLSEEIVV
TPNQDSGMKT ADALRVLSGH LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEEMC
FEGMKPVNQT SASNKGLRGL LHPQQLHLLS RQLEDPDGSF SNAEMTDLSV AQKPEKLLER
CKYWPACKNG DECVYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKA DCPFTHMSRR
GPVLTPKPAV SSPAPSSNGQ FCRYFPACKK MECPFYHPKH CRFNTQCTRP DCTFYHPTIT
VPPRHALKWI RPQTSE
