ZN425_MACFA
ID ZN425_MACFA Reviewed; 741 AA.
AC Q9N003;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Zinc finger protein 425;
DE Flags: Fragment;
GN Name=ZNF425; ORFNames=QccE-16628;
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=Brain cortex;
RX PubMed=11574149; DOI=10.1016/s0378-1119(01)00665-5;
RA Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT "Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
RT chromosomes.";
RL Gene 275:31-37(2001).
RN [2]
RP ERRATUM OF PUBMED:11574149.
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
RL Gene 278:267-267(2001).
CC -!- FUNCTION: Acts as a transcriptional repressor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Predominantly expressed in the nucleus. {ECO:0000250}.
CC -!- DOMAIN: The C2H2 domain is the main region responsible for the
CC transcriprional repression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03562.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046644; BAB03562.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q9N003; -.
DR SMR; Q9N003; -.
DR PRIDE; Q9N003; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..741
FT /note="Zinc finger protein 425"
FT /id="PRO_0000234578"
FT DOMAIN <1..69
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 179..201
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..257
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..285
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..369
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..593
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 599..621
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 627..649
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 655..677
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 683..705
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 711..733
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 67..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 741 AA; 86517 MW; 1BA3045E66778407 CRC64;
DDVALYFSGQ EWEILEKWQK QMYKQEMKTN YQTLDSLGYA FSKPDLITWM EQGRMLFISE
QGCLDKTRRT TSPPTDEQLD MKDTGKLPCF DHEGTLRTKE EDCRLNGPQK QDLGAALPGK
ERKILSARRD TFQSPSLQET EIPNKKVSIT ASDPDKKDLR HKPRETPGRL EIPTGPRCYS
CYVCRKVFQV RRDLLKHKRS HSKSQLRRYP KYRNTSRGKS ELRRTQRLLC QKKRFQCSEC
EKSYFLKGSL VTHQVVHTGQ RPYPCPECDK TFRYRANLKK HLCLHRGERP FCCGECGRAF
VQQCELTEHL RLHSGEKPFQ CPQCDRCFRL KRGMKVHLSQ HSGKRPFHCP ECGRSFSRKA
ALKTHQRTHS EEKPFSCDEC GRKFIYKIKL DEHIRVHTGE KPFSCPECNK SFRLKRSLKA
HGLQHSGKRP FQCPECSRGF FWRNAMRAHQ RLHSEQKPFP CAECGKRFTR PSKLACHTRV
HDRQKEFPCG ECKKTFSQQS RLTQHLKVHN TEKPFSCAEC GRSFRRRAHL TEHTRLHSGE
EPFQCPECDK SFSWKASMKF HQRMHRDEKP FACSECGKTY THQSQLTEHL RLHSGEKPYQ
CPECQKTFRL KGNLKSHLLQ HSGQKPFSCV MCGKSFTQQY RLTEHIRVHS GEKPFQCPEC
DKSYCIRGSL KVHLYTHSGE RPFQCPECGK GFLQKRSLKA HLCLHSGERP FSCDECGRSF
TYVGALKTHI AVHAKEKPSS L