SNAI2_BOVIN
ID SNAI2_BOVIN Reviewed; 268 AA.
AC Q3MHQ4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC105149; AAI05150.1; -; mRNA.
DR RefSeq; NP_001029710.1; NM_001034538.2.
DR AlphaFoldDB; Q3MHQ4; -.
DR SMR; Q3MHQ4; -.
DR STRING; 9913.ENSBTAP00000017600; -.
DR PaxDb; Q3MHQ4; -.
DR Ensembl; ENSBTAT00000017600; ENSBTAP00000017600; ENSBTAG00000013227.
DR GeneID; 520631; -.
DR KEGG; bta:520631; -.
DR CTD; 6591; -.
DR VEuPathDB; HostDB:ENSBTAG00000013227; -.
DR VGNC; VGNC:35048; SNAI2.
DR eggNOG; KOG2462; Eukaryota.
DR GeneTree; ENSGT00940000154511; -.
DR HOGENOM; CLU_002678_42_3_1; -.
DR InParanoid; Q3MHQ4; -.
DR OMA; VFFTPHI; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF315515; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000013227; Expressed in uterine cervix and 95 other tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
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:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0035921; P:desmosome disassembly; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; IEA:Ensembl.
DR GO; GO:0070563; P:negative regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:0032642; P:regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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_0000259420"
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 80..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 268 AA; 29729 MW; 3FD862A802630C07 CRC64;
MPRSFLVKKH FNASKKPNYS ELDTHTVIIS PCLYEGYPVP VIPQPEVLRS GAYSPIAVWT
TASPFHAPLP AGLSPLSGYP ASLGRVSPPP PSDTSSKDHS GSESPISDEE ERLQSKLSDP
HAIEAEKFQC NLCNKTYSTF SGLGKHKQLH CDAQSRKSFS CKYCDKEYVS LGALKMHIRT
HTLPCVCKIC GKAFSRPWLL QGHIRTHTGE KPFSCSHCSR AFADRSNLRA HLQTHSDVKK
YQCKSCSKTF SRMSLLHKHE ESGCCAAH
