SNAI2_RAT
ID SNAI2_RAT Reviewed; 268 AA.
AC O08954; Q8R482;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Zinc finger protein SNAI2;
DE AltName: Full=Neural crest transcription factor Slug;
DE AltName: Full=Protein snail homolog 2;
GN Name=Snai2; Synonyms=Slug, Slugh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ubeda M., Habener J.;
RT "Regulation of insulin producing beta-cells survival by SLUG, a zinc-finger
RT transcription factor, with homology to CES-1.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-172.
RX PubMed=9182671; DOI=10.1083/jcb.137.6.1403;
RA Savagner P., Yamada K.M., Thiery J.P.;
RT "The zinc-finger protein Slug causes desmosome dissociation, an initial and
RT necessary step for growth factor-induced epithelial-mesenchymal
RT transition.";
RL J. Cell Biol. 137:1403-1419(1997).
RN [3]
RP FUNCTION.
RX PubMed=16924233; DOI=10.1038/sj.onc.1209902;
RA Wang Z., Wade P., Mandell K.J., Akyildiz A., Parkos C.A., Mrsny R.J.,
RA Nusrat A.;
RT "Raf 1 represses expression of the tight junction protein occludin via
RT activation of the zinc-finger transcription factor slug.";
RL Oncogene 26:1222-1230(2007).
CC -!- FUNCTION: Transcriptional repressor that modulates both activator-
CC dependent and basal transcription. Involved in the generation and
CC migration of neural crest cells. Plays a role in mediating RAF1-induced
CC transcriptional repression of the TJ protein, occludin (OCLN) and
CC subsequent oncogenic transformation of epithelial cells. Represses
CC BRCA2 expression by binding to its E2-box-containing silencer and
CC recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes,
CC binds to the E-box in ITGA3 promoter and represses its transcription.
CC Involved in the regulation of ITGB1 and ITGB4 expression and cell
CC adhesion and proliferation in epidermal keratinocytes. Binds to E-box2
CC domain of BSG and activates its expression during TGFB1-induced
CC epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-
CC Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast
CC maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive
CC and negative transcription regulator, respectively, in osteoblasts.
CC Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells
CC and osteoblasts. Plays an essential role in TWIST1-induced EMT and its
CC ability to promote invasion and metastasis (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16924233}.
CC -!- SUBUNIT: Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP
CC (via LIM domains) and AJUBA (via LIM domains) (By similarity).
CC Interacts (via zinc fingers) with KPNA2, KPNB1 and TNPO1. May interact
CC (via zinc fingers) with IPO7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43623}. Cytoplasm
CC {ECO:0000250}. Note=Observed in discrete foci in interphase nuclei.
CC These nuclear foci do not overlap with the nucleoli, the SP100 and the
CC HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated
CC with active transcription or active splicing regions (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: Repression activity depends on the C-terminal DNA-binding zinc
CC fingers and on the N-terminal repression domain. {ECO:0000250}.
CC -!- PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization
CC and degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF497973; AAM19227.1; -; mRNA.
DR EMBL; U97061; AAB58706.1; -; mRNA.
DR RefSeq; NP_037167.1; NM_013035.1.
DR AlphaFoldDB; O08954; -.
DR SMR; O08954; -.
DR STRING; 10116.ENSRNOP00000064195; -.
DR PaxDb; O08954; -.
DR Ensembl; ENSRNOT00000073049; ENSRNOP00000064195; ENSRNOG00000047699.
DR GeneID; 25554; -.
DR KEGG; rno:25554; -.
DR CTD; 6591; -.
DR RGD; 3722; Snai2.
DR eggNOG; KOG2462; Eukaryota.
DR GeneTree; ENSGT00940000154681; -.
DR HOGENOM; CLU_002678_42_3_1; -.
DR InParanoid; O08954; -.
DR OMA; VFFTPHI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O08954; -.
DR PRO; PR:O08954; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000047699; Expressed in liver and 18 other tissues.
DR Genevisible; O08954; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0070888; F:E-box binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0060536; P:cartilage morphogenesis; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISO:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0035921; P:desmosome disassembly; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISO:RGD.
DR GO; GO:0060429; P:epithelium development; ISO:RGD.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISO:RGD.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; ISO:RGD.
DR GO; GO:0070563; P:negative regulation of vitamin D receptor signaling pathway; ISO:RGD.
DR GO; GO:0014032; P:neural crest cell development; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISO:RGD.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0032642; P:regulation of chemokine production; ISO:RGD.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009314; P:response to radiation; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0006929; P:substrate-dependent cell migration; ISO:RGD.
DR GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
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; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..268
FT /note="Zinc finger protein SNAI2"
FT /id="PRO_0000047034"
FT ZN_FING 128..150
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 159..181
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 185..207
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 213..235
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 241..264
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 84..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 268 AA; 29936 MW; 92B6325E54CEFD4B CRC64;
MPRSFLVKKH FNASKKPNYS ELDTHTVIIS PYLCESYPMP VIPKPEILTS GAYSPITVWT
SAVPFHSPLP SGLSPLTGYS SSLGRVSPLP SSDTSSKDHS GSESPISDEE ERLQPKLSDP
HAIEAEKFQC NLCNKTYSTF SGLAKHKQLH CDAQARKSFS CKYCDKEYVS LGALKMHIRT
HTLPCVCKIC GKAFSRPWLL QGHIRTHTGE KPFSCPHCNR AFADRSNLRA HLQTHSDVKK
YQCKNCSKTF SRMSLLHKHE ESGCCVAH
