ID   F170A_MACFA             Reviewed;         283 AA.
AC   Q66LM5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Protein FAM170A;
DE   AltName: Full=Zinc finger domain-containing protein;
DE   AltName: Full=Zinc finger protein ZNFD;
GN   Name=FAM170A; Synonyms=ZNFD;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang C.Q., Liu S., Zhai Q.T.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a nuclear transcription factor that positively
CC       regulates the expression of heat shock genes. Binds to heat shock
CC       promoter elements (HSE) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus is necessary for nuclear localization. The C-
CC       terminus is necessary for transcriptional activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAM170 family. {ECO:0000305}.
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DR   EMBL; AY692450; AAU04858.1; -; mRNA.
DR   AlphaFoldDB; Q66LM5; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR033376; FAM170A.
DR   InterPro; IPR040879; Spt46-like.
DR   PANTHER; PTHR33517; PTHR33517; 1.
DR   PANTHER; PTHR33517:SF3; PTHR33517:SF3; 1.
DR   Pfam; PF17734; Spt46; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..283
FT                   /note="Protein FAM170A"
FT                   /id="PRO_0000326111"
FT   ZN_FING         181..205
FT                   /note="C2H2-type; degenerate"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..242
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         170
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66LM6"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66LM6"
SQ   SEQUENCE   283 AA;  32263 MW;  4BC6724078EC8D10 CRC64;
     MKRRQKRKHL ENEESQETAE KGGGIQRIHR DSPQPQSPLA QVQERGETPP RSQHVSLSFH
     SSYKTCVSSL CVNKEERGMK IYYMQVQMNK GVAVSWETEE TLESLEKQPR MEEVTLSEVV
     RVGTPPSDVS TRNLLSDSEP SGEEKEHEER TESDSLPGSP TVEDTPRAKT PDWLVTMENG
     FRCMACCRVF TTMEALQEHV QFGIREGFSC HVFHLTMAQL TGNMESESTQ DEQEEENGNE
     KEEEEKPEAK EEEGQPTEED LGLRRSWSQC PGCVFHSPKD RNS