ZCHC8_PONAB
ID ZCHC8_PONAB Reviewed; 704 AA.
AC Q5R789;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Zinc finger CCHC domain-containing protein 8;
DE AltName: Full=TRAMP-like complex RNA-binding factor ZCCHC8;
GN Name=ZCCHC8;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scaffolding subunit of the trimeric nuclear exosome targeting
CC (NEXT) complex that is involved in the surveillance and turnover of
CC aberrant transcripts and non-coding RNAs. NEXT functions as an RNA
CC exosome cofactor that directs a subset of non-coding short-lived RNAs
CC for exosomal degradation. May be involved in pre-mRNA splicing. It is
CC required for 3'-end maturation of telomerase RNA component (TERC), TERC
CC 3'-end targeting to the nuclear RNA exosome, and for telomerase
CC function. {ECO:0000250|UniProtKB:Q6NZY4}.
CC -!- SUBUNIT: Component of a nuclear TRAMP-like complex, an ATP-dependent
CC exosome regulatory complex consisting of a helicase (MTREX), an
CC oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific
CC RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes
CC exist with specific compositions and are associated with nuclear, or
CC nucleolar RNA exosomes. Identified in the spliceosome C complex.
CC Component of the nuclear exosome targeting (NEXT) complex composed of
CC MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding short-lived
CC RNAs for exosomal degradation. Interacts with proteins involved in RNA
CC processing and degradation such as MTREX and RBM7; interaction with
CC MTREX enhances MTREX RNA helicase activity and bridges between RBM7 and
CC MTREX. Interacts with TERC, the telomerase RNA component.
CC {ECO:0000250|UniProtKB:Q6NZY4}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q6NZY4}. Note=Excluded from nucleolus.
CC {ECO:0000250|UniProtKB:Q6NZY4}.
CC -!- DOMAIN: The C-terminal part (659-707) contributes to MTREX RNA helicase
CC activity, in part, by enhancing its RNA-dependent ATPase activity.
CC {ECO:0000250|UniProtKB:Q6NZY4}.
CC -!- PTM: Phosphorylation at Thr-490 by GSK3 is triggered in cells entering
CC mitosis. {ECO:0000250|UniProtKB:Q6NZY4}.
CC -!- SIMILARITY: Belongs to the ZCCHC8 family. {ECO:0000305}.
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DR EMBL; CR860229; CAH92371.1; -; mRNA.
DR RefSeq; NP_001126396.1; NM_001132924.1.
DR AlphaFoldDB; Q5R789; -.
DR SMR; Q5R789; -.
DR STRING; 9601.ENSPPYP00000005774; -.
DR PRIDE; Q5R789; -.
DR GeneID; 100173378; -.
DR KEGG; pon:100173378; -.
DR CTD; 55596; -.
DR eggNOG; KOG2673; Eukaryota.
DR InParanoid; Q5R789; -.
DR OrthoDB; 338817at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034470; P:ncRNA processing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR006568; PSP_pro-rich.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF04046; PSP; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00581; PSP; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT CHAIN 2..704
FT /note="Zinc finger CCHC domain-containing protein 8"
FT /id="PRO_0000150962"
FT ZN_FING 225..242
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 16..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..297
FT /note="RBM7 binding"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT REGION 307..322
FT /note="RBM7 binding"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT REGION 407..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..704
FT /note="MTREX binding"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT COILED 43..78
FT /evidence="ECO:0000255"
FT COILED 514..538
FT /evidence="ECO:0000255"
FT COMPBIAS 16..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 490
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZY4"
SQ SEQUENCE 704 AA; 78274 MW; 960F1D473DFA254E CRC64;
MAAEVYFGDL ELFEPFDHPE ESIPEPVHTR FKDDDEEDEN GVGDAELRER LRQCEETIEQ
LRAENQELKR KLNILTRPSG ILVNDTKLDG PILQILFMNN AISKQYHQEI EEFVSNLVKR
FEEQQKNDVE KTSFNLLPQP SSIVLEEDHK VEEACAIKNN KEAFSVVGSV LYFTNFCLDK
LGQPLLNENP QLSEGWEIPK YHQVFSHIVS LEGQEIQVKA KRPKPHCFNC GSEEHQMKDC
PMPRNAARIS EKRKEYMDAC GEANNQNFQQ RYHAEEVEER FGRFKPGVIS EELQDALGVT
DKSLPPFIYR MRQLGYPPGW LKEAELENSG LALYDGKDGT DGETEVGEIQ QNKSVTYDLS
KLVNYPGFNI STPRGIPDEW RIFGSIPMQA CQQKDVFANY LTSNFQAPGV KSGNKRSSSH
SSPGSPKKQK KESNSAGSPA DMELDSDMEV PHGSQSSESF QFQPPLPPDT PPLPRGTPPP
IFTPPLPKGT PPLTPSDSPQ TRTASGAVDE DALTLEELEE QQRRIWAALE QAESLNSDSD
APVDTPLTGN SVASSPCPNE LDLPIPEGKT SEKQTLDEPE VPEIFTDKSE AGHASSPDCE
VTSLCQKKAE LAPVNTEGAL LDNGSVVPNC DISNGGSQKL VPADTSPSMA TKIHSPIPDM
SKFATGITPF EFENMAESTG MYLRIRSLLK NSPRNQQKNK KASE
