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ZN274_BOVIN
ID   ZN274_BOVIN             Reviewed;         620 AA.
AC   A6QPT6; Q0V8D6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Neurotrophin receptor-interacting factor homolog;
DE   AltName: Full=Zinc finger protein 274;
GN   Name=ZNF274;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-404.
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC149474; AAI49475.1; -; mRNA.
DR   EMBL; BT026283; ABG81439.1; -; mRNA.
DR   RefSeq; NP_001094623.1; NM_001101153.1.
DR   RefSeq; XP_010813875.1; XM_010815573.2.
DR   AlphaFoldDB; A6QPT6; -.
DR   SMR; A6QPT6; -.
DR   STRING; 9913.ENSBTAP00000012662; -.
DR   PaxDb; A6QPT6; -.
DR   PRIDE; A6QPT6; -.
DR   Ensembl; ENSBTAT00000012662; ENSBTAP00000012662; ENSBTAG00000013353.
DR   GeneID; 534170; -.
DR   KEGG; bta:534170; -.
DR   CTD; 10782; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013353; -.
DR   VGNC; VGNC:37235; ZNF274.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162111; -.
DR   HOGENOM; CLU_002678_49_6_1; -.
DR   InParanoid; A6QPT6; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF338018; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000013353; Expressed in oocyte and 103 other tissues.
DR   ExpressionAtlas; A6QPT6; baseline and differential.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 5.
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; 3.
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   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..620
FT                   /note="Neurotrophin receptor-interacting factor homolog"
FT                   /id="PRO_0000406964"
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          278..351
FT                   /note="KRAB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         478..500
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         506..528
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         534..556
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         562..584
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         590..612
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          324..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  69254 MW;  A595C4B7BC81075E CRC64;
     MASGLPTDWF REPVTFEDVA LGFTPDEWGK LDLEQKSLYR EVMLENYRNL VSVEHQLSKP
     DVVSQLEEEE ELWSVERGIP QDTFSECPEA QLEPQLDPFP AGNPLMNIEV VEVLTLNQEV
     AVPRNAQIRA LYAEDEGLSP EVLREPPQHL DKPTADPEMA RQRFRGFHFE EVAGPREALA
     QLRELCCQWL RPEAHSKDQM LELLVLEQFL GALPEKLRLW VESQHPVDCR QAVALVEDVT
     WISEEETLPT QGAPGTLPPA AQQDTATWPV KALPEDPVTF LDVAVDFSTE EWGLLDPTQR
     TEYHDVMLET FGHLVSVGWE TTLDSKQLTP QPGPPEEGPA CPLKEEEGSS ADDARPSTSG
     EALEAGAPGV WDTALKPVTL ASENTLPPQP PGDSPQPQAS TGPDRGRVSL QKAVPRKRLR
     KRDPWLKRGT RGACVKLPPK RGGAGKAVES GGDGGRRPCA RNAPQITFTR IHKGSQVCRC
     SECGKTFRNP RYFSVHKKIH TGEKPYVCRD CGKAFVQSSS LRQHQRVHTG ERPFVCHECG
     RTFNDRSAIS QHLRTHTGAK PYPCPDCGKA FRQSSHLIRH QRTHTGERPY SCSKCGKAFT
     QSSHLIGHQK THSRVKCKKK
 
 
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