Z652A_XENLA
ID Z652A_XENLA Reviewed; 625 AA.
AC Q6GNP2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Zinc finger protein 652-A;
GN Name=znf652-a;
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; BC073462; AAH73462.1; -; mRNA.
DR RefSeq; NP_001085876.1; NM_001092407.1.
DR AlphaFoldDB; Q6GNP2; -.
DR SMR; Q6GNP2; -.
DR PRIDE; Q6GNP2; -.
DR DNASU; 444303; -.
DR GeneID; 444303; -.
DR KEGG; xla:444303; -.
DR CTD; 444303; -.
DR Xenbase; XB-GENE-6465969; znf652.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 444303; Expressed in neurula embryo 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..625
FT /note="Zinc finger protein 652-A"
FT /id="PRO_0000280431"
FT ZN_FING 258..281
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..335
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 426..448
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..476
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 482..505
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 80..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 71186 MW; 9AC1B6C726B46E7D CRC64;
MGQTANSCQK MLDGRPADVS GMVVNDPCLM NIPTSFYHST NQELDLSNKT FKREVGGPFS
VMMENKMGKP HLLETDQQNF FRDSKPINEV HSVKGERENS GESEEEEDDD DDDDDEDDEE
GEEDEDEVNY KREQIIVEVN LNNQTLNVSK GDKGVAQDSS HIKTSSDDEE GDSGEDDQDS
HEDEENNPLP LDGQTNMQHG NQDQKTENSD MVGGDGTIPA NSTKELGKGG EAPKRKKKTP
KEPKSPSDKA KSEEKETLTC DKCPRVFNTR WYLEKHMNVT HRRMQICDKC GKKFVLESEL
SLHLQTDCEK NIQCITCNKT FKKLWSLHEH IKIVHGYAEK KFSCEICEKK FYTMAHVRKH
LVAHTKDMPF TCETCGKSFK RSMSLKVHSL QHSGEKPFRC ENCDERFQYK YQLRSHMSIH
IGHKQFMCQW CGKDFNMKQY FDEHMKTHTG EKPFICEICG KSFTSRPNMK RHRRTHTGEK
PYPCDVCGMR FRFSNMLKAH KEKCFRVTSP VGVPPALQIA LGNPTLSNPS QGVTHLPTAH
VPPPSPTPPL NLNVLNTLPP RPIPHPFSHL HLHPHSHTHH LAVPPVPHLP PPPALFKSEA
LNHRGHNDDS FLRHLAEKTS ASQHH