ID   ZSC26_BOVIN             Reviewed;         479 AA.
AC   A6QNZ0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 26;
DE   AltName: Full=Zinc finger protein 187;
GN   Name=ZSCAN26; Synonyms=ZNF187;
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=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
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DR   EMBL; BC149068; AAI49069.1; -; mRNA.
DR   RefSeq; NP_001095427.1; NM_001101957.1.
DR   AlphaFoldDB; A6QNZ0; -.
DR   SMR; A6QNZ0; -.
DR   STRING; 9913.ENSBTAP00000035458; -.
DR   PaxDb; A6QNZ0; -.
DR   GeneID; 512445; -.
DR   KEGG; bta:512445; -.
DR   CTD; 7741; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; A6QNZ0; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..479
FT                   /note="Zinc finger and SCAN domain-containing protein 26"
FT                   /id="PRO_0000307312"
FT   DOMAIN          51..133
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         232..254
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         283..305
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         311..333
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         339..361
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         367..389
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         395..417
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         423..445
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         451..473
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          155..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        17
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16670"
SQ   SEQUENCE   479 AA;  55276 MW;  1CC39E9F2BECF727 CRC64;
     MAIAWGTVPS LAPVNLKKEG LQVVKEDHLS AREQGVKLQG NGTGFRQEPL CKRFRQLRYE
     ETTGPREALS RLRELCRQWL QPETHTKEQI LELLVLEQFL TILPEELQAR LREHHLESGE
     DAVVFLEDLQ LELGGTGQQE DPNQAKKQEV LMEETAPGKA TPERQVQPEG DVPQPEREKG
     EAKRIENGKL VVETDSCGRV ESSGKPFEPM EVHYKDSNLD RQQAEPKEKT DCKCSEYGQA
     FFQHSDLIKH ESSHRKEKLC EAEVCQSLSL PGHQKICSRE KGHQCHECGK AFQRSSHLVR
     HQKIHLGEKP YQCKECGKVF SQNAGLLEHL RIHTGEKPYL CIHCGKNFRR SSHLNRHQRI
     HSQEEPCQCK ECGKTFSQAL LLTHHQRIHS HSRSHQCNEC GKTFSLTSDL IRHHRIHTGE
     KPFKCTICQK AFRLNSHLAQ HVRIHNEEKP YKCNECGEAF RQRSGLFQHQ RYHHKNRLA