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   27-MAR-2024, entry version 106.
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; 10116-ENSRNOP00000052376; -.
DR   Ensembl; ENSRNOT00000022811.7; ENSRNOP00000052376.2; ENSRNOG00000017001.7.
DR   GeneID; 497984; -.
DR   KEGG; rno:497984; -.
DR   UCSC; RGD:1566329; rat.
DR   AGR; RGD:1566329; -.
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; HTANSCQ; -.
DR   OrthoDB; 4247334at2759; -.
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 cell types or tissues.
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   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR16515:SF46; FINGER PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
DR   Genevisible; A1L1J6; RN.
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
//