SNAI2_XENLA
ID SNAI2_XENLA Reviewed; 266 AA.
AC Q91924; Q5D087;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Zinc finger protein SNAI2;
DE AltName: Full=Protein slug-alpha;
DE AltName: Full=Protein snail homolog 2;
DE AltName: Full=Snail protein homolog Slug;
DE Short=xSlu;
GN Name=snai2; Synonyms=slu, slug;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Neurula;
RX PubMed=7720581; DOI=10.1242/dev.121.3.767;
RA Mayor R.M., Morgan R.M., Sargent M.G.;
RT "Induction of the prospective neural crest of Xenopus.";
RL Development 121:767-777(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Neurula;
RX PubMed=11402039; DOI=10.1074/jbc.m103167200;
RA Vallin J., Thuret R., Giacomello E., Faraldo M.M., Thiery J.P., Broders F.;
RT "Cloning and characterization of three Xenopus slug promoters reveal direct
RT regulation by Lef/beta-catenin signaling.";
RL J. Biol. Chem. 276:30350-30358(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP INTERACTION WITH ELP3.
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: Probable transcriptional repressor. Acts downstream of snai1
CC in the specification of the neural crest and neural crest migration.
CC {ECO:0000269|PubMed:12490555, ECO:0000269|PubMed:18331720}.
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 (PubMed:27189455). {ECO:0000269|PubMed:18331720,
CC ECO:0000269|PubMed:27189455}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: First expressed on the lateral side of stage 12
CC embryos. At stage 14, strongly expressed in the lateral neural folds.
CC At stage 16, expressed in pre-migratory neural crest cells. At stage
CC 18, expression is dispersed over the neural plate in a pattern
CC surrounding the rhombomeres. At stage 22, expressed in neural crest
CC derivatives, including the branchial arches and the tissues surrounding
CC the eyes and forebrain. After stage 17, expression is weak in the
CC lateral plate mesoderm, increasing at stage 26, but was down-regulated
CC in the pronephros region at stage 26. {ECO:0000269|PubMed:11402039,
CC ECO:0000269|PubMed:12490555, ECO:0000269|PubMed:7720581}.
CC -!- INDUCTION: By a combination of noggin and fgf2/bfgf in ectoderm. By wnt
CC signaling. {ECO:0000269|PubMed:11402039, ECO:0000269|PubMed:7720581}.
CC -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; X80269; CAA56556.1; -; mRNA.
DR EMBL; AF368040; AAK54137.1; -; Genomic_DNA.
DR EMBL; AF368041; AAK54138.1; -; mRNA.
DR EMBL; BC054144; AAH54144.1; -; mRNA.
DR PIR; S52245; S52245.
DR RefSeq; NP_001079751.1; NM_001086282.1.
DR AlphaFoldDB; Q91924; -.
DR SMR; Q91924; -.
DR DNASU; 379440; -.
DR GeneID; 379440; -.
DR KEGG; xla:379440; -.
DR CTD; 379440; -.
DR Xenbase; XB-GENE-6255814; snai2.L.
DR OMA; VFFTPHI; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 379440; Expressed in neurula embryo and 18 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0014036; P:neural crest cell fate specification; IGI:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IDA: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; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..266
FT /note="Zinc finger protein SNAI2"
FT /id="PRO_0000047035"
FT ZN_FING 126..148
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 157..179
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 183..205
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 211..233
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 239..262
FT /note="C2H2-type 5; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 75..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 29895 MW; 3316D38EF220B769 CRC64;
MPRSFLVKKH FNSAKKPNYG ELDNHTVIIS PFLYERYPVS VLPQPDIYSS VAYSPITVWT
GLLHPPLPSD LSPLSGYPSS LGRVSPPPQS DTSSKDHSGS ESPISDEEER LQTKLSDSHA
IEAEKFQCSL CSKTYSTFSG LAKHKQLHCD AQSRKSFSCK YCEKEYVSLG ALKMHIRTHT
LPCVCKICGK AFSRPWLLQG HIRTHTGEKP FSCPHCNRAF ADRSNLRAHL QTHSDVKKYQ
CKNCSKTFSR MSLLHKHEES GCCVAH
