ZN652_RAT
ID ZN652_RAT Reviewed; 608 AA.
AC A1L1J6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Zinc finger protein 652;
GN Name=Znf652; Synonyms=Zfp652;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-100 AND THR-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as a transcriptional repressor. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC129097; AAI29098.1; -; mRNA.
DR RefSeq; NP_001073676.1; NM_001080207.1.
DR AlphaFoldDB; A1L1J6; -.
DR SMR; A1L1J6; -.
DR STRING; 10116.ENSRNOP00000052376; -.
DR iPTMnet; A1L1J6; -.
DR PhosphoSitePlus; A1L1J6; -.
DR PaxDb; A1L1J6; -.
DR PRIDE; A1L1J6; -.
DR Ensembl; ENSRNOT00000022811; ENSRNOP00000052376; ENSRNOG00000017001.
DR GeneID; 497984; -.
DR KEGG; rno:497984; -.
DR UCSC; RGD:1566329; rat.
DR CTD; 268469; -.
DR RGD; 1566329; Zfp652.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157416; -.
DR HOGENOM; CLU_002678_74_2_1; -.
DR InParanoid; A1L1J6; -.
DR OMA; VENCAAH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A1L1J6; -.
DR TreeFam; TF332655; -.
DR PRO; PR:A1L1J6; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017001; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; A1L1J6; RN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..608
FT /note="Zinc finger protein 652"
FT /id="PRO_0000280430"
FT ZN_FING 244..267
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..321
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..491
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 60..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..608
FT /note="Mediates interaction with CBFA2T3"
FT /evidence="ECO:0000250"
FT REGION 540..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D9"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D9"
SQ SEQUENCE 608 AA; 69558 MW; 65EEE1086C2C2EF9 CRC64;
MSYTASPCQE LVEPCAVHAE GMAQEESHRS QAPPTFYHGA SQELDLSTKV YKRESGSPYS
VLADSKMSKP HLHETEEQPY FREPRAVSDV HTVKEDRENS DDTEEEEEVS YKREQIIVEV
NLNNQTLNVS KGEKGVSSQS KETPVLKTSS EEEEEETEED ATDNSSDYGE NGRQKKKEKQ
VEKVRVTQRR TRRAASVAAA TTSPTPRTTR GRRKSAELPK RKKRAAKEPK APVQKAKCDE
KETLTCEKCP RVFNTRWYLE KHMNVTHRRM QICDKCGKKF VLESELSLHQ QTDCEKNIQC
VSCNKSFKKL WSLHEHIKIV HGYAEKKFAC EICEKKFYTM AHVRKHMVAH TKDMPFTCET
CGKSFKRSMS LKVHSLQHSG EKPFRCENCD ERFQYKYQLR SHMSIHIGHK QFMCQWCGKD
FNMKQYFDEH MKTHTGEKPF ICEICGKSFT SRPNMKRHRR THTGEKPYPC DVCGQRFRFS
NMLKAHKEKC FRVTSPVNVP PAVQIPLASA PAAPAPAVAN TPTSPAPAVS MNPVGSALPS
RPVPHPFSHL HIHTHPHHSH HLPIPPVPHL PPPPALFKSE PLNHRSQSED TFLRHLAEKN
SPAQAQHH
