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 24-JAN-2024, entry version 55.
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 STRING; 9541.ENSMFAP00000016656; -.
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 DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR040879; Spt46-like.
DR PANTHER; PTHR33517:SF3; PROTEIN FAM170A; 1.
DR PANTHER; PTHR33517; PROTEIN FAM170B-RELATED; 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
//
