Z652B_XENLA
ID Z652B_XENLA Reviewed; 602 AA.
AC Q6INV8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc finger protein 652-B;
GN Name=znf652-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC072164; AAH72164.1; -; mRNA.
DR RefSeq; NP_001085209.1; NM_001091740.1.
DR AlphaFoldDB; Q6INV8; -.
DR SMR; Q6INV8; -.
DR GeneID; 432303; -.
DR KEGG; xla:432303; -.
DR CTD; 432303; -.
DR Xenbase; XB-GENE-1020916; znf652.S.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 432303; Expressed in internal ear and 19 other tissues.
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 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; 8.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..602
FT /note="Zinc finger protein 652-B"
FT /id="PRO_0000280432"
FT ZN_FING 235..258
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..284
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..312
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..369
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..482
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 60..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 68699 MW; C45DD54800FBC97D CRC64;
MVVDDPCLLN IPTSFYHSTN QELDLSNKTF KREVGGPYSV MMDNKIGKPH LLETDQQNFF
QDSKPTNEVH AVKGERENSG ESEEEEDEDD DDDDDDDDDD EEGEDEDEVN YKREQIIVEV
NLNNQTLNVS KGDKGVPKDP SQIKTSSDDE GGDSGEDDQD SHEDEENNPL PLDGQTNMQH
GNQDQKTENS DMVGGDGTIP ANSTKEQGKG GEAPKRKKKP KSPSDKAKSE EKETLTCDKC
PRVFNTRWYL EKHMNVTHRR MQICDKCGKK FVLESELSLH LQTDCEKNIQ CITCNKTFKK
LWSLHEHIKI VHGYAEKKFS CEICEKKFYT MAHVRKHLVA HTKDMPFTCE TCGKSFKRSM
SLKVHSLQHS GEKPFRCENC DERFQYKYQL RSHMSIHIGH KQFMCQWCGK DFNMKQYFDE
HMKTHTGEKP FICEICGKSF TSRPNMKRHR RTHTGEKPYP CDVCGMRFRF SNMLKAHKEK
CFRVTSPVGV PPALQITLNN PTLSNPSQGI SNLPNAHIPP PSPTPPLNLN ALNPLPPRPI
PHPFSHLHLH PHSHTHHLAV PPVPHLPPPP ALFKSEALNH RGQNDDSFLR HLAEKTSAGQ
HH