ID   D7_XENLA                Reviewed;         278 AA.
AC   P13007; Q5EAY6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein D7;
GN   Name=d7;
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].
RC   TISSUE=Oocyte;
RX   PubMed=3203907; DOI=10.1101/gad.2.10.1296;
RA   Smith R.C., Dworkin M.B., Dworkin-Rastl E.;
RT   "Destruction of a translationally controlled mRNA in Xenopus oocytes delays
RT   progesterone-induced maturation.";
RL   Genes Dev. 2:1296-1306(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in oocyte maturation. It is possible that D7 is
CC       required at a certain point in the maturation process and that
CC       maturation cannot proceed beyond this point unless a threshold amount
CC       of D7 protein is provided.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Its levels are highest during the first day of
CC       embryonic development and then decrease; D7 protein was not detected in
CC       adult tissues.
CC   -!- SIMILARITY: Belongs to the UPF0224 (FAM112) family. {ECO:0000305}.
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DR   EMBL; X13856; CAA32068.1; -; mRNA.
DR   EMBL; BC090198; AAH90198.1; -; mRNA.
DR   PIR; S06173; S06173.
DR   RefSeq; NP_001081517.1; NM_001088048.1.
DR   AlphaFoldDB; P13007; -.
DR   SMR; P13007; -.
DR   MaxQB; P13007; -.
DR   DNASU; 397887; -.
DR   GeneID; 397887; -.
DR   KEGG; xla:397887; -.
DR   CTD; 397887; -.
DR   Xenbase; XB-GENE-6489103; gtsf2.L.
DR   OrthoDB; 1359124at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 397887; Expressed in egg cell and 18 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR022776; TRM13/UPF0224_CHHC_Znf_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   Pfam; PF05253; zf-U11-48K; 2.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS51800; ZF_CHHC_U11_48K; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Metal-binding; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..278
FT                   /note="Protein D7"
FT                   /id="PRO_0000221623"
FT   ZN_FING         6..33
FT                   /note="CHHC U11-48K-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   ZN_FING         40..67
FT                   /note="CHHC U11-48K-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   REGION          149..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
SQ   SEQUENCE   278 AA;  31384 MW;  6BD0B882DAAAE4FE CRC64;
     MEFDELMQCP YDKNHMIRPS RFPYHLVKCR ENNRAAAKIL ATCPYNARHR VPKQELDLHM
     ASCEYRVTME PISAAFSHQK VETSTWQSPP CEEVWETDED PVSRPKPFIL NDFTPSQPFN
     MSEGDGNMPY TGISSNYRPE VQPMNSVMQV KQNQPEPEPF TSSERNYDPR SKEPPNPKQP
     AVNGYKPATT NTNPWCRQTG GSRGAAPPKL GAKSSDEGPR NKEFPTPKAN LMNEYVPVAA
     NANPWCRQPG GSSAASEPLG VDSFDEWPCL GRQPWVRK