ZO29_XENLA
ID ZO29_XENLA Reviewed; 537 AA.
AC P18748;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Oocyte zinc finger protein XlCOF29;
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 [MRNA] OF 1-397.
RX PubMed=2503827; DOI=10.1073/pnas.86.16.6097;
RA Knoechel W., Poeting A., Koester M., el Baradi T., Nietfeld W.,
RA Bouwmeester T., Pieler T.;
RT "Evolutionary conserved modules associated with zinc fingers in Xenopus
RT laevis.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6097-6100(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 370-537.
RX PubMed=2509712; DOI=10.1016/0022-2836(89)90155-1;
RA Nietfeld W., El-Baradi T., Mentzel H., Pieler T., Koester M., Poeting A.,
RA Knoechel W.;
RT "Second-order repeats in Xenopus laevis finger proteins.";
RL J. Mol. Biol. 208:639-659(1989).
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; M25870; AAA50017.1; -; mRNA.
DR PIR; E33282; E33282.
DR PIR; S06557; S06557.
DR AlphaFoldDB; P18748; -.
DR SMR; P18748; -.
DR Proteomes; UP000186698; Genome assembly.
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; 6.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
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..537
FT /note="Oocyte zinc finger protein XlCOF29"
FT /id="PRO_0000047823"
FT ZN_FING 375..397
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 59983 MW; 634F1B4C89A3801F CRC64;
MGMSEKASDT GMKGKKKDKN ERNEKILNLT LEMIYLLTGE GYVIPKKKKS GDDMAPPQSC
TDCILEGGCR CHVTNLTGGR ALHAPGSVIQ KENNKNDKKI LELVSNIIQL LTGEEWEYIK
RKKALYMEGI KEDPQQLSQW CEYEDKSIVM CNLEATACLN NDPRNDTVFC EHRDLSKFDT
SLAEQSLPAI GIKGEPVSCE GANQSDCNIN PLAEQIQGTD TPTPIMGCSL NNSLSDNYIS
NGIKTEATSC EAGNQSDYGN NPVAEVQLTD TTTPVKRCSL NSILSDNYIK IAIKEEPPSW
EDENQTHCSI NAPGEQNEEI DTPTSIMRFC LNSSLLDSSL LNAIKDDTLS CEGENYSDCS
FNPLTEQTSP GCKQFTCSEC GKTYTRLYNL KIHLKSHTDD KTFSCSECEE CFTDHTDLVI
HRRLHLTLKA FPCAECGKCF TNCTNLRAHS KTHTGEKPYS CTECGKTFRD RSHLNIHKKR
HTGEKPYTCS ECGKCFAYRS NLMVHVRIHT GEKPFSCSKC GKCFTDHANL IVHERMH