ZC3HE_MACFA
ID ZC3HE_MACFA Reviewed; 736 AA.
AC Q4R6F6; Q4R6K3; Q95LZ4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14;
GN Name=ZC3H14; ORFNames=QtsA-17814, QtsA-18125, QtsA-19123;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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:Q6PJT7}.
CC Note=Colocalizes with poly(A) RNA in nuclear speckles.
CC {ECO:0000250|UniProtKB:Q7TMD5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q4R6F6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R6F6-2; Sequence=VSP_033175;
CC Name=3;
CC IsoId=Q4R6F6-3; Sequence=VSP_033173, VSP_033175, VSP_033176;
CC Name=4;
CC IsoId=Q4R6F6-4; Sequence=VSP_033172, VSP_033174;
CC -!- SIMILARITY: Belongs to the ZC3H14 family. {ECO:0000305}.
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DR EMBL; AB071047; BAB64440.1; -; mRNA.
DR EMBL; AB169180; BAE01272.1; -; mRNA.
DR EMBL; AB169227; BAE01319.1; -; mRNA.
DR EMBL; AB169336; BAE01421.1; -; mRNA.
DR RefSeq; XP_005562047.1; XM_005561990.2. [Q4R6F6-1]
DR RefSeq; XP_005562052.1; XM_005561995.2. [Q4R6F6-2]
DR AlphaFoldDB; Q4R6F6; -.
DR STRING; 9541.XP_005562047.1; -.
DR GeneID; 101865337; -.
DR KEGG; mcf:101865337; -.
DR CTD; 79882; -.
DR VEuPathDB; HostDB:ENSMFAG00000032254; -.
DR eggNOG; KOG3702; Eukaryota.
DR OMA; TFYHPTV; -.
DR OrthoDB; 893844at2759; -.
DR Proteomes; UP000233100; Chromosome 7.
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; IEA:InterPro.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:InterPro.
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..736
FT /note="Zinc finger CCCH domain-containing protein 14"
FT /id="PRO_0000331312"
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 78..146
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 398..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..101
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 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
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 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 1..298
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12498619, ECO:0000303|Ref.2"
FT /id="VSP_033172"
FT VAR_SEQ 1..155
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033173"
FT VAR_SEQ 299..426
FT /note="VSSVVKVKKFNHDGEEEEEDDDYGSRTGSISSSVSVPAKPERRPSLPPSKQA
FT NKNLILKAISEAQESVTKTTNYSTVPQKQTLPVAPRTRTSQEELLAEVVQGQSRTPRIS
FT PPIKEEETKGDSVEKNQ -> MKMSSKFPSPPLPIFLPPEPVDLGSITSSSCSLNELDN
FT ISHLLRKISTDINEIKGMKAAILTVEANLFDLNVRVSQNEAKISSLEVKMNEYSTTSEC
FT NRQFEDQEEDTESQSRTTDVKIIGFLRNVEK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12498619, ECO:0000303|Ref.2"
FT /id="VSP_033174"
FT VAR_SEQ 452..582
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033175"
FT VAR_SEQ 669
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033176"
SQ SEQUENCE 736 AA; 82947 MW; B6A585E64AC94DEC CRC64;
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
RFTVWLHGVL DKLRSVTTEP SSLKSSDTNI FDSNVPSNKS NFSRGDERRH EAAVPPLAIP
STRPEKRDSR VSTSSQESKT TNVRQTYDDG AATRLMSTVK PLREPAPSED VIDIKPEPDD
LIDEDLNFVQ ENPLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADSGVHLN RLQFQQQQNS
IHAAKQLDMQ NSWVYETGRL CEPEVLNSLE ETYSPFFRNN SEKMSMEDEN FRKRKLPVVS
SVVKVKKFNH DGEEEEEDDD YGSRTGSISS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
EAQESVTKTT NYSTVPQKQT LPVAPRTRTS QEELLAEVVQ GQSRTPRISP PIKEEETKGD
SVEKNQGTQQ RQLLSRLQID PVMAETLQMS QDYYDMESMV HADTRSFILK KPKLSEEIVV
APNQESGMKT ADSLRVLSGH LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEDMC
FEGMKPVNQT AASNKGLRGL LHPQQLHLLS RQLEDPNGSF SNAEMSELSV AQKPEKLLER
CKYWPACKNG DECAYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKP DCPFTHVSRR
IPVLSPKPAV APPAPPSSSQ LCRYFPACKK MECPFYHPKH CRFNTQCTRP DCTFYHPTIN
VPPRHALKWI RPQTSE
