ID   NF7B_XENLA              Reviewed;         609 AA.
AC   Q92021;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Nuclear factor 7, brain;
DE            Short=xNF7;
DE            Short=xNF7-B;
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:AAB20269.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION AT THR-103.
RC   TISSUE=Brain {ECO:0000269|PubMed:1936552};
RX   PubMed=1936552; DOI=10.1016/0012-1606(91)90321-s;
RA   Reddy B.A., Kloc M., Etkin L.D.;
RT   "The cloning and characterization of a maternally expressed novel zinc
RT   finger nuclear phosphoprotein (xnf7) in Xenopus laevis.";
RL   Dev. Biol. 148:107-116(1991).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain {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   [3] {ECO:0000305}
RP   STRUCTURE BY NMR OF 219-260.
RX   PubMed=8846787; DOI=10.1002/j.1460-2075.1995.tb00283.x;
RA   Borden K.L.B., Lally J.M., Martin S.R., O'Reilly N.J., Etkin L.D.,
RA   Freemont P.S.;
RT   "Novel topology of a zinc-binding domain from a protein involved in
RT   regulating early Xenopus development.";
RL   EMBO J. 14:5947-5956(1995).
CC   -!- FUNCTION: Transcription factor that determines dorsal-ventral body
CC       axis. {ECO:0000269|PubMed:1936552}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8846787}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1936552}.
CC   -!- TISSUE SPECIFICITY: At the neurula stage, high expression in dorsal
CC       embryo region including neural folds and somites. Also high expression
CC       in adult brain (CNS) and low expression in oocytes.
CC       {ECO:0000269|PubMed:1936552, ECO:0000269|PubMed:8541218}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:1936552}.
CC   -!- PTM: Threonine (predominantly) and serine residues are phosphorylated
CC       during oocyte maturation, when CDK1 is active.
CC       {ECO:0000269|PubMed:1936552}.
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DR   EMBL; S64515; AAB20269.1; -; mRNA.
DR   EMBL; M63705; AAA49995.1; -; mRNA.
DR   PIR; A43906; A43906.
DR   RefSeq; NP_001081473.1; NM_001088004.1.
DR   PDB; 1FRE; NMR; -; A=219-260.
DR   PDBsum; 1FRE; -.
DR   AlphaFoldDB; Q92021; -.
DR   SMR; Q92021; -.
DR   BioGRID; 99195; 5.
DR   IntAct; Q92021; 2.
DR   iPTMnet; Q92021; -.
DR   GeneID; 397856; -.
DR   KEGG; xla:397856; -.
DR   CTD; 397856; -.
DR   Xenbase; XB-GENE-6252335; xnf7.L.
DR   OrthoDB; 423686at2759; -.
DR   EvolutionaryTrace; Q92021; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 397856; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.40.10; -; 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   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF00643; zf-B_box; 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; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF54160; SSF54160; 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   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Developmental protein; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..609
FT                   /note="Nuclear factor 7, brain"
FT                   /id="PRO_0000055977"
FT   DOMAIN          21..75
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          413..609
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         145..185
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         219..260
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          74..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          278..371
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        74..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   MOD_RES         103
FT                   /note="Phosphothreonine; by CDK1"
FT                   /evidence="ECO:0000305|PubMed:1936552"
FT   STRAND          237..242
FT                   /evidence="ECO:0007829|PDB:1FRE"
SQ   SEQUENCE   609 AA;  68876 MW;  088C8312B45C78F8 CRC64;
     MEEEEGADDG EQGEEEVLVV NVGSTYPCKR SDGSQHDAEI VKVRYNKQAG REEYYAHYVG
     LNRRQNEWVD KSRLVLTKPP KEGETNGTDQ EVTDTAEQPD SKTPQKRKIE EPEPEPKKAK
     VEEKDASKNA SSLGAAGDFA EELTCPLCVE LFKDPVMVAC GHNFCRSCID KAWEGQSSFA
     CPECRESITD RKYTINRVLA NLAKKAACTP VTPVEKKTRP LEKCSEHDER LKLYCKDDGT
     LSCVICRDSL KHASHNFLPI LDAVGVYREE LSAIVAPLEA SLKVTEQLSS EQSDKIEQHN
     KNMSQYKEHI TSEFEKLHKF LREREEKLLE QLKEQGENLL TEMENNLVKM QESQDAIKKT
     ISLAKERMED TDSISFLMDI KAFIDKCQEQ QRAVISTGNT LLSKELCQGT FKGPIQYIMW
     KELKSVVIPS LTPMLLDPTS AHPNLHLSDG LTSVRYGENK LSLPDNPKRF SQCILVLGSQ
     GFDSGRHYWE VEVGDKTAWD VGMASESSNR KGKIKLNPKN GYWAIWLRNG NAYKALESPS
     KSLSLSSHPR KIGVYVDYEG GQISFYNADD MTIIYTFNAT FTEKLYPYLS PFLHDSGKNV
     DPLRFVHNK