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Database: UniProt
Entry: F1SH27_PIG
LinkDB: F1SH27_PIG
Original site: F1SH27_PIG 
ID   F1SH27_PIG              Unreviewed;       661 AA.
AC   F1SH27; A0A480Y0X7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=SKI like proto-onco {ECO:0000313|Ensembl:ENSSSCP00000012517.3};
DE   SubName: Full=Ski-like protein isoform X1 {ECO:0000313|EMBL:HDC14335.1};
GN   Name=SKIL {ECO:0000313|Ensembl:ENSSSCP00000012517.3,
GN   ECO:0000313|VGNC:VGNC:92903};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000012517.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000012517.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000012517.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDC14335.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000012517.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SKI family. {ECO:0000256|ARBA:ARBA00009513}.
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DR   EMBL; DQIR01258857; HDC14335.1; -; Transcribed_RNA.
DR   EMBL; DQIR01258858; HDC14336.1; -; Transcribed_RNA.
DR   STRING; 9823.ENSSSCP00000012517; -.
DR   PaxDb; 9823-ENSSSCP00000012517; -.
DR   Ensembl; ENSSSCT00000012857.5; ENSSSCP00000012517.3; ENSSSCG00000011746.5.
DR   VGNC; VGNC:92903; SKIL.
DR   eggNOG; ENOG502QT5P; Eukaryota.
DR   GeneTree; ENSGT00940000158435; -.
DR   HOGENOM; CLU_025786_0_0_1; -.
DR   TreeFam; TF324133; -.
DR   Reactome; R-SSC-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Bgee; ENSSSCG00000011746; Expressed in caecum and 44 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR   GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR   GO; GO:0002260; P:lymphocyte homeostasis; IEA:Ensembl.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd21084; DHD_Sno; 1.
DR   Gene3D; 3.10.390.10; SAND domain-like; 1.
DR   Gene3D; 3.10.260.20; Ski; 1.
DR   InterPro; IPR014890; c-SKI_SMAD4-bd_dom.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR010919; SAND-like_dom_sf.
DR   InterPro; IPR003380; SKI/SNO/DAC.
DR   InterPro; IPR037000; Ski_DNA-bd_sf.
DR   InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
DR   PANTHER; PTHR10005; SKI ONCOGENE-RELATED; 1.
DR   PANTHER; PTHR10005:SF3; SKI-LIKE PROTEIN; 1.
DR   Pfam; PF08782; c-SKI_SMAD_bind; 1.
DR   Pfam; PF02437; Ski_Sno; 1.
DR   SMART; SM01046; c-SKI_SMAD_bind; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF63763; SAND domain-like; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          261..356
FT                   /note="c-SKI SMAD4-binding"
FT                   /evidence="ECO:0000259|SMART:SM01046"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          538..651
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  74668 MW;  5052DCB92C0FDFB4 CRC64;
     MENLQTSFSL VQGSNKKLNG MGDDGSPPVK KMMTDIHANG KMIINKMPAV KKEHLDDYEA
     PMETDEEHVK RTCASVPEPL HLNPSLKHTL AQFHLSSQSS LGGPAAFSAR YSQESMSPTV
     FLPLPSPQVL PGPLLIPSDS STELTQTVLE GESISCFQVG GEKRLCLPQV LNSVLREFSL
     QQINTVCDEL YIYCSRCTSD QLHILKVLGI LPFNAPSCGL ITLTDAQRLC NALLRPRTFP
     QNGSILPAKN SLAQLKETGS AFEVEHECLG KCQGLFAPQF YVQPDAPCIQ CLECCGMFAP
     QTFVMHSHRS PDKRTCHWGF ESAKWHCYLH VNQKYLGTPE EKKLKIILEE MKEKFSMRNG
     KRTQSKIDAS PGMELQSWYP VIKQEGDHVS QTHSFLHPSY YLYMCDKVVA PNVSLTSAVS
     QPKEVTKTEA SRSIPRQSEK PHSSGKHPKT VSYPDVSLEE QEKMDLKTNR ELYSRLDPSV
     SNNSTSKKKP ESTTCCLARD ASKAGNDCDA AASSPLLVKD VICEDDKGKI MEEVMRTYVK
     QQEKLNSILQ KKQQLQMEVE MLSSSKAMKE LTEEQQNLQK ELESLQNEHA QRMEEFYVEQ
     KDLEKKLEQL AELRQRLDHA EADRQELQDE LRQEREARQK LEMMIKELKL QILKSSKTAK
     E
//
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