SNAI1_XENLA
ID SNAI1_XENLA Reviewed; 259 AA.
AC P19382; Q5PRF8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein snail homolog Sna;
DE Short=Protein Xsnail;
DE Short=Protein xSna;
GN Name=snai1; Synonyms=sna;
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], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC TISSUE=Neurula;
RX PubMed=2226210; DOI=10.1242/dev.109.4.967;
RA Sargent M.G., Bennett M.F.;
RT "Identification in Xenopus of a structural homologue of the Drosophila gene
RT snail.";
RL Development 109:967-973(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12490555; DOI=10.1242/dev.00238;
RA Aybar M.J., Nieto M.A., Mayor R.;
RT "Snail precedes slug in the genetic cascade required for the specification
RT and migration of the Xenopus neural crest.";
RL Development 130:483-494(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH LIMD1; AJUBA AND WTIP.
RX PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT development in Xenopus.";
RL Dev. Cell 14:424-436(2008).
RN [5]
RP INTERACTION WITH ELP3, AND UBIQUITINATION.
RX PubMed=27189455; DOI=10.1038/srep26238;
RA Yang X., Li J., Zeng W., Li C., Mao B.;
RT "Elongator Protein 3 (Elp3) stabilizes Snail1 and regulates neural crest
RT migration in Xenopus.";
RL Sci. Rep. 6:26238-26238(2016).
CC -!- FUNCTION: Transcriptional repressor. Acts upstream of snai2/slug, zic5
CC and other neural crest markers in the specification of the neural crest
CC and neural crest migration. Involved in embryonic mesoderm formation.
CC {ECO:0000269|PubMed:12490555, ECO:0000269|PubMed:18331720,
CC ECO:0000269|PubMed:2226210}.
CC -!- SUBUNIT: Interacts (via SNAG domain) with limd1 (via LIM domains), wtip
CC (via LIM domains) and ajuba (via LIM domains) (PubMed:18331720).
CC Interacts with elp3; the interaction inhibits snai1 ubiquitination and
CC promotes snai1 stability (PubMed:27189455).
CC {ECO:0000269|PubMed:18331720, ECO:0000269|PubMed:27189455}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Maternal expression is nearly completely restricted
CC to the vegetal hemisphere. Zygotic expression begins in the dorsal
CC marginal zone just before gastrulation (stage 9), and is almost
CC completely absent in the animal hemisphere. At mid-gastrula (stage 11-
CC 11.5), expression begins in the ectoderm in an arc surrounding the
CC prospective neural plate. From stage 12, anterior expression is down-
CC regulated, while levels are increased in the prospective neural crest.
CC {ECO:0000269|PubMed:12490555, ECO:0000269|PubMed:2226210}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in embryos at a low level prior to the onset of zygotic
CC transcription. Zygotically first expressed at stage 9, increasing to a
CC plateau from stage 12 to 18, and decreasing to some extent after stage
CC 25, although expression persists until at least stage 40.
CC {ECO:0000269|PubMed:2226210}.
CC -!- INDUCTION: By two classes of mesoderm inducing factors: transforming
CC growth factor-beta (TGF-beta) family and fibroblast growth factor
CC (FGF). {ECO:0000269|PubMed:2226210}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:27189455}.
CC -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; X53450; CAA37528.1; -; mRNA.
DR EMBL; BC056857; AAH56857.1; -; mRNA.
DR PIR; S12078; S12078.
DR RefSeq; NP_001079925.1; NM_001086456.1.
DR AlphaFoldDB; P19382; -.
DR SMR; P19382; -.
DR DNASU; 379615; -.
DR GeneID; 379615; -.
DR KEGG; xla:379615; -.
DR CTD; 379615; -.
DR Xenbase; XB-GENE-17344016; snai1.L.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379615; Expressed in neurula embryo and 18 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0014036; P:neural crest cell fate specification; IMP:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; TAS:AgBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..259
FT /note="Protein snail homolog Sna"
FT /id="PRO_0000047031"
FT ZN_FING 119..141
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 150..172
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 176..198
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 204..226
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..255
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 71..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 29108 MW; 2C95BFB63FA5E86B CRC64;
MPRSFLVKKH FSASKKPNYS ELESQTVYIS PFIYDKFPVI PQPEILSTGA YYTPLVWDTG
LLTTFFTSES DYKKSPISPS SSDDSSKPLD LTSFSSEDEG GKTSDPPSPA SSATEAEKFQ
CNLCSKSYST FAGLSKHKQL HCDSQTRKSF SCKYCEKEYV SLGALKMHIR SHTLPCVCKI
CGKAFSRPWL LQGHIRTHTG EKPFSCTHCN RAFADRSNLR AHLQTHSDVK KYQCKSCSRT
FSRMSLLHKH EETGCTVAH
