ID   ZN827_MACFA             Reviewed;        1081 AA.
AC   Q9BE73;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Zinc finger protein 827;
GN   Name=ZNF827; ORFNames=QflA-10067;
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].
RC   TISSUE=Frontal cortex;
RA   Hashimoto K., Osada N., Hida M., Kusuda J., Sugano S.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: As part of a ribonucleoprotein complex composed at least of
CC       HNRNPK, HNRNPL and the circular RNA circZNF827 that nucleates the
CC       complex on chromatin, may negatively regulate the transcription of
CC       genes involved in neuronal differentiation. Could also recruit the
CC       nucleosome remodeling and histone deacetylase/NuRD complex to telomeric
CC       regions of chromosomes to regulate chromatin remodeling as part of
CC       telomere maintenance. {ECO:0000250|UniProtKB:Q17R98}.
CC   -!- SUBUNIT: Part of a transcription inhibitory ribonucleoprotein complex
CC       composed at least of the circular RNA circZNF827, HNRNPK and HNRNPL.
CC       Interacts with the nucleosome remodeling and histone deacetylase/NuRD
CC       complex. Interacts with RBBP4; the interaction is direct and recruits
CC       RBBP4, a component of the NuRD complex, to telomeres.
CC       {ECO:0000250|UniProtKB:Q17R98}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q17R98}.
CC       Chromosome, telomere {ECO:0000250|UniProtKB:Q17R98}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AB056797; BAB39321.1; -; mRNA.
DR   AlphaFoldDB; Q9BE73; -.
DR   STRING; 9541.XP_005556074.1; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0120325; F:NuRD complex binding; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0070200; P:establishment of protein localization to telomere; ISS:UniProtKB.
DR   GO; GO:1904791; P:negative regulation of shelterin complex assembly; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Telomere; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1081
FT                   /note="Zinc finger protein 827"
FT                   /id="PRO_0000325890"
FT   ZN_FING         374..396
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         402..424
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         433..455
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         817..839
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         845..867
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         897..919
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         929..952
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1019..1041
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1047..1069
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..14
FT                   /note="Mediates direct interaction with RBBP4"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   REGION          258..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           3..5
FT                   /note="RRK motif; mediates NuRD recruitment to telomeres"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..348
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1012
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        176
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        216
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        226
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        360
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        372
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        466
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        475
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        523
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        549
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        580
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        587
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        597
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        634
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        639
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        658
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        673
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        673
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        704
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        710
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        742
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        778
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        798
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        870
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        891
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        958
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
FT   CROSSLNK        1014
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R98"
SQ   SEQUENCE   1081 AA;  119230 MW;  59C8902139295EF5 CRC64;
     MPRRKQEQPK RLPSHVSRQE EAEGELSEGE HWYGNSSETP SEASFGEVQE NYKLSLEDRI
     QEQSTSPDTS LGSTTPSSHT LELVALDGEV LRDSLQCQDH LSPGVSSLCD DDPGSNKPLS
     SNLRRLLEAG SLKLDAVATA NGRVESPVNV GSNLSFSPPS HHAQQLSVLA RKLAEKQEQN
     DQYTPSNRFI WNQGKWLPNS TTTCSLSPDS AILKLKAAAN AVLQDKSLTR TEETMRFESF
     SSPFSSQSAS STLAALSKKV SERSLTPGQE HPPPASSFLS LAPMTSSAAL LKEVAARAAG
     SLLAEKSSLL PEDPLPPPPS EKKPEKVSPP PPPPPPPPPP PPPQSLELLL LPVPKGRVSK
     PSNSASEEES GKPFQCPICG LVIKRKSYWK RHMVIHTGLK SHQCPLCPFR CARKDNLKSH
     MKVHQHQDRG ETFQCQLCPF TSSRHFSLKL HMRCHQHFLR TEAKVKEEIP DPDVKGSPHL
     SDSACLGQQR EGGGTELVGT MMTSNTPERT SQGGAGVSPL LVKEEPKEDN GLPTSFTLNT
     ADRPANHTKL KDPSEYVANS ASALFSQDIS VKMASDFLMK LSAANQKEPM NLNFKVKEEP
     KEGESLSTTL PRSSYVFSPE SEVSTPGVSE DALKPQEGKG NVLRRDVSVK AASELLMKLS
     AESYKETQMV KIKEEPMEVD IQDSHVSISP SRNVGYSTLI GREKTEPLQK MPEGRVPPER
     NLFSQDISVK MASELLFQLS EKVSKEHNHT KENTIRTTTS PFFSEDTFRQ SPFTSNSKEL
     LPSESVLHGR ISAPETEKIV LEAGNGLPSW KFNDQLFPCD VCGKVFGRQQ TLSRHLSLHT
     EERKYKCHLC PYAAKCRANL NQHLTVHSVK LVSTDTEDIV SAVTSEGSDG KKHPYYYSCH
     VCGFETELNV QFVSHMSLHV DKEQWMFSIC CTACDFVTME EAEIKTHIGT KHTGEDRKTP
     SESNSPSSSS LSALSDSANS KDDSDGSQKN KGGNNLLVVS VMPGSQPSLN SEEKPEKGFE
     CVFCNFVCKT KNMFERHLQI HLITRMFECD VCHKFMKTPE QLLEHKKCHT VPTGGLNSGQ
     W