ZN274_MACFA
ID ZN274_MACFA Reviewed; 653 AA.
AC Q4R8H9; Q4R322;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Neurotrophin receptor-interacting factor homolog;
DE AltName: Full=Zinc finger protein 274;
GN Name=ZNF274; ORFNames=QtsA-12436, QtsA-20146;
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] (ISOFORMS 1 AND 2).
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: Probable transcription repressor. Specifically binds to the
CC 3'-end of zinc-finger coding genes and recruiting chromatin-modifying
CC proteins such as SETDB1 and TRIM28/KAP1, leading to transcription
CC repression. The SETDB1-TRIM28-ZNF274 complex may play a role in
CC recruiting ATRX to the 3'-exons of zinc-finger coding genes with
CC atypical chromatin signatures to establish or maintain/protect H3K9me3
CC at these transcriptionally active regions (By similarity).
CC {ECO:0000250|UniProtKB:Q96GC6}.
CC -!- SUBUNIT: Interacts with SETDB1 and TRIM28/KAP1. Interacts with ATRX.
CC Forms a complex with ATRX, SETDB1 and TRIM28.
CC {ECO:0000250|UniProtKB:Q96GC6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96GC6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4R8H9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R8H9-2; Sequence=VSP_040911;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB168473; BAE00593.1; -; mRNA.
DR EMBL; AB179446; BAE02497.1; -; mRNA.
DR RefSeq; NP_001270154.1; NM_001283225.1. [Q4R8H9-1]
DR RefSeq; XP_005590640.1; XM_005590583.2. [Q4R8H9-1]
DR AlphaFoldDB; Q4R8H9; -.
DR SMR; Q4R8H9; -.
DR STRING; 9541.XP_005590639.1; -.
DR PRIDE; Q4R8H9; -.
DR Ensembl; ENSMFAT00000010981; ENSMFAP00000036733; ENSMFAG00000034673. [Q4R8H9-1]
DR GeneID; 101867030; -.
DR KEGG; mcf:101867030; -.
DR CTD; 10782; -.
DR VEuPathDB; HostDB:ENSMFAG00000034673; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162111; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000034673; Expressed in heart and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 2.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 2.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00349; KRAB; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF109640; SSF109640; 2.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50805; KRAB; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..653
FT /note="Neurotrophin receptor-interacting factor homolog"
FT /id="PRO_0000406965"
FT DOMAIN 14..85
FT /note="KRAB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT DOMAIN 161..243
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 287..360
FT /note="KRAB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 507..529
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 535..557
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 563..585
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 591..613
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 619..641
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 136..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 290..375
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040911"
FT CONFLICT 408
FT /note="N -> D (in Ref. 1; BAE02497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 74135 MW; A4036BBE9C576019 CRC64;
MASRLPTAWS CEPVNFEDVT LGFTPEEWGL LDLKQKSLYR EVMLENYRNL VSVEHQLSKP
DVVSQLEEAE DFWPVERGIP QDTIPEYSEL QLDPKLDPLP AESPLMNIEV VEVLTLNQEV
AGPRNAQIQA LYAEDGSLSP DAPSEEVQQQ GKHPGDPEAA RQRFRQFRYK DMTGPREALD
QLRQLCHQWL QPEARSKEQI LELLVLEQFL GALPVKLRTW VESQHPENCQ EVVALVEGVT
WISEEEVLPA GQPAEGTTCC LEVTAQQEEK QEDAAICPVT VLSEEPVTFQ DVAVDFSREE
WGLLGPTQRT EYRDVMLETF GHLVSVGWET TLENKELAPN SDIPQEEPAP SLKVQESSRD
CTLSSTLEDT LQGGVQEVQE TVLKQVESAK EKDLPQKKHF DNHESQANSG TLDTNQVSLQ
KIDSVESQVN NGALNTNQVL LQKIPPRKQL RKCDSQVKSM KHNSRVKIHQ KSYERQKAKE
GNGCRKTFSR SAKQITFIRI HKGSQVCRCS ECGKIFRNPR YFSVHKKIHT GERPYVCQAC
GKGFVQSSSL TQHQRVHSGE RPFECHECGR TFNDRSAISQ HLRTHTGAKP YKCQDCGKAF
RQSSHLIRHQ RTHTGERPYA CNKCGKAFTQ SSHLIGHQRT HNRTKRKKKQ PTS
