ID   SP2_BOVIN               Reviewed;         613 AA.
AC   Q5E9U0; B0JYR4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Transcription factor Sp2;
GN   Name=SP2;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to GC box promoters elements and selectively activates
CC       mRNA synthesis from genes that contain functional recognition sites.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors. In SP2, the motif is
CC       inactive. {ECO:0000250|UniProtKB:Q02086}.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT020830; AAX08847.1; -; mRNA.
DR   EMBL; BC151610; AAI51611.1; -; mRNA.
DR   RefSeq; NP_001015654.1; NM_001015654.1.
DR   RefSeq; XP_005220643.1; XM_005220586.3.
DR   AlphaFoldDB; Q5E9U0; -.
DR   SMR; Q5E9U0; -.
DR   STRING; 9913.ENSBTAP00000018253; -.
DR   PaxDb; Q5E9U0; -.
DR   PRIDE; Q5E9U0; -.
DR   GeneID; 534403; -.
DR   KEGG; bta:534403; -.
DR   CTD; 6668; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_034267_0_0_1; -.
DR   InParanoid; Q5E9U0; -.
DR   OrthoDB; 1085860at2759; -.
DR   TreeFam; TF350150; -.
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:0035264; P:multicellular organism growth; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR030451; SP2_TF.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23235:SF1; PTHR23235:SF1; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..613
FT                   /note="Transcription factor Sp2"
FT                   /id="PRO_0000269191"
FT   ZN_FING         525..549
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         555..579
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         585..607
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           361..369
FT                   /note="9aaTAD; inactive"
FT                   /evidence="ECO:0000250|UniProtKB:Q02086"
FT   COMPBIAS        183..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02086"
SQ   SEQUENCE   613 AA;  64718 MW;  483EEDE259F5E96B CRC64;
     MSDPQTSMAA TAAVSPSDYL QPAASTTQDS QPSPLALLAA TCSKIGPPAV EAAVTPPAPP
     QPTPRKLVPI KPAPLPLSPS KNSFGILSSK GNILQIQGSQ LSTSYPGGQL VFAIQNPTVV
     NKGTRSNTSI QYQAVPQIQA SSPQTIQVQP SLTNQIQIIP GTNQAIITPS PSSHKPVPIK
     PAPVQKSSTT TTPAQSGANV VKLTGGGGNV TLTLPVNNLV NTSDPGAATQ LLTESPPAPL
     SKTNKKARKK SLPAAQPPVA VAEQVETVLI ETTADNIIQA GNNLLIVQSP GGGQPAVVQQ
     VQVVPPKAEQ QQVVQIPQQA LRVVQAASAT LPTVPQKPSQ NFQIQAAEPS PTQVYIRTPS
     GEVQTVLVQD SPPATAATAS TTTCSSPASR AAHLSGTSKK HSAAILRKER PLPKIAPAGS
     IISLNAAQLA AAAQAMQTIN INGVQVQGVP VTITNTGGQQ QLTVQNVSGN NLTISGLSPT
     QIQLQMEQAL AGETQPGEKR RRMACTCPNC KDGDKRSGEQ GKKKHVCHIP DCGKTFRKTS
     LLRAHVRLHT GERPFVCNWF FCGKRFTRSD ELQRHARTHT GDKRFECAQC QKRFMRSDHL
     TKHYKTHLVT KNL