ZO71_XENLA
ID ZO71_XENLA Reviewed; 898 AA.
AC P18751;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Oocyte zinc finger protein XlCOF7.1;
DE Flags: Fragment;
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 1-311.
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 284-898.
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; M25866; AAA50013.1; -; mRNA.
DR PIR; A33282; A33282.
DR PIR; S06546; S06546.
DR AlphaFoldDB; P18751; -.
DR SMR; P18751; -.
DR MaxQB; P18751; -.
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; 17.
DR SMART; SM00355; ZnF_C2H2; 21.
DR SUPFAM; SSF57667; SSF57667; 12.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 21.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 21.
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..>898
FT /note="Oocyte zinc finger protein XlCOF7.1"
FT /id="PRO_0000047811"
FT ZN_FING 289..311
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 426..448
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..476
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 482..504
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 510..532
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 538..561
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 567..589
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 595..617
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 623..645
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 651..673
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 679..701
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 707..729
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 735..758
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 764..786
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..814
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 820..842
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 848..870
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 876..898
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 898
SQ SEQUENCE 898 AA; 101168 MW; 795D806E5696B0B6 CRC64;
MGMWEEASDT GMKGKKKDKN EEEEERGKKE RMVNLTLEMI YLLTGEHYIP RKKSDDGGAL
HAPGSVIQKE NNKNDKKILE LMSNIIQLLT GEVAIRTHHV SIYFSLDEWD YIKGNKELYE
EGIKEEPQQL RPQACEYKDE SNVTAHMEAT LCCNSDGNFI NPENPEISPG EQPPPANGIK
EEATSSEEGN QSDCSINPLT EEIQGTDTPT PIMGCSLNYS LSDNYISDEI KEEETSCQGR
NQSDCSITPL TEQIQGTDTP TPIMGCSLKD NKYDGNPHWS PKNTLRRKYS CNECHEYLIH
KRDFGKHQMT HKREKSFSCS ECGKCFLNQL CPDRHQTGKK PFSCSKCGKC FAFLSDLTVH
RRIHTGERPF SCSECGKGFT RPNALIIHHR THTGEKPFSC SECGKCFSKQ SSLVHHQRTH
IGEKPFCCSE CDKCFASSSE LNIHQRTHTG EKPFSCSECG KCFTNHSHFA HHQMIHTGEK
PFCCSKCGKC FASSSDLTFH RRTHTREKTF SCSECGKCFS NHSHLARHQM IHTGEKPFCC
SECGKCFSSS SGLTAHQQRT HMKVKPFSCS ACGKCFSNRS HLIRHQMIHT GEKPFSCFEC
RKCFSNPSNL ARHQMTHTGE KPFSCSECGK CFASSSDLTF HHRTHTGEKP FSCSECGKCY
SKKSSLVHHQ RTHTGEKPFS CSKCDKCFAS SSELNIHQRT HTGEKAFSCS ECGKCFTNRS
QLSRHQMIHT GEKPISCPEC EECFVSSSQL TAHQQQAHRM VKPFSCLECG KCFSNRSNFA
RHQMIHTGEK PFSCSECRKG FSNQSSLARH QMTHTGEKPF SCSECGKRFS NQSHLARHQM
IHTGEKPFSC SECAKGFSNQ SGLARHQMTH TGEKPFACSE CGKCFASSSK LTAHQRTH
