FOXN3_XENLA
ID FOXN3_XENLA Reviewed; 485 AA.
AC Q3BJS3; Q3BJS2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Forkhead box protein N3;
GN Name=foxn3 {ECO:0000312|EMBL:CAJ38819.1};
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:CAJ38819.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16525939; DOI=10.1387/ijdb.052126ms;
RA Schuff M., Roessner A., Donow C., Knoechel W.;
RT "Temporal and spatial expression patterns of FoxN genes in Xenopus laevis
RT embryos.";
RL Int. J. Dev. Biol. 50:429-434(2006).
CC -!- FUNCTION: Acts as a transcriptional repressor. May be involved in DNA
CC damage-inducible cell cycle arrests (checkpoints) (By similarity).
CC {ECO:0000250|UniProtKB:O00409}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:16525939};
CC IsoId=Q3BJS3-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:16525939};
CC IsoId=Q3BJS3-2; Sequence=VSP_052096;
CC -!- TISSUE SPECIFICITY: At early cleavage stages, localized within the
CC animal half of the embryo. At gastrulation, expression expands over the
CC whole embryo excluding the future endodermal cells of the blastopore.
CC During neurulation, expressed in the prospective eye field and in the
CC neural crest cells. Strongly enriched in the eye vesicles at stage 26.
CC From stage 29 onwards, expressed predominantly in the eye, the
CC branchial arches and the vagal ganglion. At stage 38, expressed
CC throughout the head with strongest expression in the head mesenchyme
CC and the eye lens. {ECO:0000269|PubMed:16525939}.
CC -!- DEVELOPMENTAL STAGE: Both isoform 1 and isoform 2 are expressed both
CC maternally and zygotically. Present in all embryonic stages including
CC early cleavage stages, with levels decreasing during gastrulation.
CC Expression is then up-regulated at stage 25 and persists until stage
CC 45. {ECO:0000269|PubMed:16525939}.
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DR EMBL; AM114794; CAJ38819.1; -; mRNA.
DR EMBL; AM114795; CAJ38820.1; -; mRNA.
DR RefSeq; NP_001090178.1; NM_001096709.1. [Q3BJS3-1]
DR AlphaFoldDB; Q3BJS3; -.
DR SMR; Q3BJS3; -.
DR GeneID; 779041; -.
DR KEGG; xla:779041; -.
DR CTD; 779041; -.
DR Xenbase; XB-GENE-864945; foxn3.S.
DR OrthoDB; 699973at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 779041; Expressed in spleen and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; DNA-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..485
FT /note="Forkhead box protein N3"
FT /id="PRO_0000247734"
FT DNA_BIND 113..209
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 248..270
FT /note="DPDIDAASAMMLLNSAHELQAGF -> V (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16525939"
FT /id="VSP_052096"
SQ SEQUENCE 485 AA; 53892 MW; E70BFE6C1CDD8A55 CRC64;
MGPVMPPSKK PEGTGISVSS QCYRSSTLSN PLQDDDDLDF PPPPVKIHKE KGGMEDEELT
NLNWLHENKN LLKSFGDTVL RSVSPVQDID DDTPPSPAQS DMPYDAKQNP NCKPPYSFSC
LIFMAVEDSP TKRLPVKDIY NWILEHFPYF ANAPTGWKNS VRHNLSLNKC FKKVDKDRSQ
SIGKGSLWCI DPEYRQNLIQ ALKKTPYHPY SHVFNTPPTS PQAYQSTSVP PLWPGSTFFK
KNGALLQDPD IDAASAMMLL NSAHELQAGF SPGVIQNGAR VLNRGIFPGV RPLPINPIGA
MAASVRNGIA NCRTRMESEP SCGSPLVSSD PKDDHNYSSA KSANKRSSSP SDSISSSADD
HYEFAAKVCR EGSDISFQSH ESFSETEEED KKQIKKELKE PLVESGYSSQ HKKKQHLLKL
RRIPSDALPL KKRRTEKPPE SDDEEMKEAA GSLLHLAGIR SCLNNITNRT AKGQKEQKDK
ETTKN
