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Database: UniProt
Entry: Q91431
LinkDB: Q91431
Original site: Q91431 
ID   NF7O_XENLA              Reviewed;         610 AA.
AC   Q91431; Q801R9;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Nuclear factor 7, ovary;
DE            Short=xNF7-O;
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] {ECO:0000305, ECO:0000312|EMBL:AAB35876.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Ovary {ECO:0000269|PubMed:8541218};
RX   PubMed=8541218; DOI=10.1016/0925-4773(95)00410-3;
RA   Gong S.-G., Reddy B.A., Etkin L.D.;
RT   "Two forms of Xenopus nuclear factor 7 have overlapping spatial but
RT   different temporal patterns of expression during development.";
RL   Mech. Dev. 52:305-318(1995).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH47956.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH47956.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that determines dorsal-ventral body
CC       axis. {ECO:0000269|PubMed:8541218}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q92021}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:8541218};
CC         IsoId=Q91431-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q91431-2; Sequence=VSP_051606;
CC   -!- TISSUE SPECIFICITY: Abundant in oocytes. At the neurula stage, low
CC       expression in dorsal embryo region including neural folds and somites.
CC       {ECO:0000269|PubMed:8541218}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:8541218}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH47956.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; S80988; AAB35876.1; -; mRNA.
DR   EMBL; BC047956; AAH47956.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001079694.2; NM_001086225.2. [Q91431-1]
DR   AlphaFoldDB; Q91431; -.
DR   SMR; Q91431; -.
DR   IntAct; Q91431; 2.
DR   DNASU; 379381; -.
DR   GeneID; 379381; -.
DR   KEGG; xla:379381; -.
DR   AGR; Xenbase:XB-GENE-6256071; -.
DR   CTD; 379381; -.
DR   Xenbase; XB-GENE-6256071; xnf7.S.
DR   OrthoDB; 3453019at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 379381; Expressed in neurula embryo and 19 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19800; Bbox2_xNF7-like; 1.
DR   CDD; cd18984; CBD_MOF_like; 1.
DR   CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1.
DR   CDD; cd13733; SPRY_PRY_C-I_1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR025995; Tudor-knot.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF286; E3 UBIQUITIN-PROTEIN LIGASE TRIM69; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF15227; zf-C3HC4_4; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Developmental protein; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..610
FT                   /note="Nuclear factor 7, ovary"
FT                   /id="PRO_0000055978"
FT   DOMAIN          21..75
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          415..610
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         146..186
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         220..261
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          79..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          295..374
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        96..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   MOD_RES         104
FT                   /note="Phosphothreonine; by CDK1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         62..118
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_051606"
FT   CONFLICT        265
FT                   /note="I -> V (in Ref. 2; AAH47956)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        533
FT                   /note="R -> A (in Ref. 2; AAH47956)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   610 AA;  69115 MW;  D828F60060572EC1 CRC64;
     MEEDEGADDG EQEEEEVLLV NVGSTYPCKR SDGSQHDADI VKTRYNKQAG REEYYVHYVG
     LNRRQNEWVD KSRLVLTKPP KEVETNGTDQ EEMTEPTEQP DSKTPQKRKL EEPEPEPKKA
     KVEDKDASKT AASLGAAGDF AEELTCPLCV ELFKDPVMVA CGHNFCRSCI DKVWEGQSSF
     ACPECKESIT DRKYTINRVL ANLAKKAACT PVTPVEKKTR PLEKCSEHDE RLKLYCKDDG
     TLGCVICRDS LKHASHNFLP ILDAIGVYRE ELSAIVAPLE ASLKVTEQLS GEQSDKIEQH
     NKNVSQYKEH VTSEFEKLHK FLKEREEKLL EQLKEQGDNL LTEMENNLVK MQENQDAIKK
     TISLAKERME ETDSISFLTD IKTFIDKCQE QQRAVISTGN TLLSKELCQG TFKGPIQYIM
     WKELKSVITP SLTPMLLDPN SAHPNLHLSD GLTSVRYGEN KLSLPDNPKR FSQCILVLGS
     QGFDSGRHYW EVEVGDKTAW DVGMASESSN RKGKIKLNPK NGYWAIWLRN GNRYKALESP
     SKALSLTSHP RKIGVYVDYE GGQISFYNAD NMTIIYTFSA TFTEKLYPYL SPFLHDSGKN
     VDALRFVHNQ
//
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