ID   ZFP30_MACFA             Reviewed;         519 AA.
AC   Q9BE27;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Zinc finger protein 30 homolog;
DE            Short=Zfp-30;
GN   Name=ZFP30; ORFNames=QflA-14093;
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   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
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; AB060218; BAB41152.1; -; mRNA.
DR   RefSeq; NP_001270852.1; NM_001283923.1.
DR   AlphaFoldDB; Q9BE27; -.
DR   SMR; Q9BE27; -.
DR   STRING; 9541.XP_005589115.1; -.
DR   GeneID; 102137967; -.
DR   CTD; 22835; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 12.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..519
FT                   /note="Zinc finger protein 30 homolog"
FT                   /id="PRO_0000231520"
FT   DOMAIN          6..78
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         158..180
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         186..208
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         214..236
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         242..264
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         298..320
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         326..348
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         354..376
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         382..404
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         410..432
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         438..460
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         466..488
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         494..516
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   MOD_RES         75
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60585"
FT   CROSSLNK        110
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G7"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G7"
SQ   SEQUENCE   519 AA;  61477 MW;  20EEA5E63165F9C6 CRC64;
     MARDLVMFRD VAIDFSQEEW ECLNSYQRNL YRDVILENYS NLVSLAGCSI SKPDVITLLE
     QGKEPWMVMR DEKRRWTLDL ESRYDTKKLF QEKDIYEMNL SQWKVMERIK SCGLEGQESP
     HEVCFRQVTK TTSGKTPTYR KLTSLPLYQK SHNREKPYEC GECGKAFRVR QQLTFHQRIH
     TGEKPYECKE CGKAFRQCAH LSRHQRIHTS DKLYECKKCG KIFTCGSDLR VHQRIHIGEK
     PYECKECGKG FRVRGQLNLH QRIHTGEKPY ECKECGKAFR QYAHLTRHQR LNIAEKCYEC
     KECGQAFLCS TGLRIHHKLH TGEKPYECKE CGKAFRVRQQ LTLHQRIHTG EKPYDCKECG
     KTFSRGYHLT LHQRIHTGEK PYECKECQKF FRRYSELISH QGIHIGEKPY ECKECGKAFR
     LFSQLTQHQS IHFGEKPYKC KECEKTFRLL SQLTQHQSIH TGEKPHDCKE CGKAFRLHSS
     LIQHQRIHSG EKPYKCKECK KAFRQHSHLT YHQRIHNVT