Q8R0S1 (ATF7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclic AMP-dependent transcription factor ATF-7
Short name=cAMP-dependent transcription factor ATF-7

Alternative name(s):
Activating transcription factor 7
Transcription factor ATF-A

Gene names

Name:

Atf7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays important functions in early cell signaling. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters. Activator of the NF-ELAM1/delta-A site of the E-selectin promoter. Has no intrinsic transcriptional activity, but activates transcription on formation of JUN or FOS heterodimers. Also can bind TRE promoter sequences when heterodimerized with members of the JUN family By similarity.
Subunit structure	Homodimer; binds DNA as homodimer By similarity. Heterodimer; heterodimerizes with other members of ATF family and with JUN family members By similarity. Interacts with JNK2; the interaction does not phosphorylate ATF7 but acts as a docking site for other ATF-associated partners such as JUN family members. Interacts (via its transactivation domain) with TAF12 the interaction potentiates the transactivation activity and is inhibited by ATF7 sumoylation. Interacts with TAF4; the interaction inhibits the TAF12-dependent transactivation. Interacts with MAPK9; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN By similarity.
Subcellular location	Nucleus By similarity. Nucleus › nucleoplasm By similarity. Note: Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear peiphery By similarity.
Post-translational modification	On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity By similarity. Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase By similarity.
Sequence similarities	Belongs to the bZIP family. Contains 1 bZIP (basic-leucine zipper) domain. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear periphery Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 413	413	Cyclic AMP-dependent transcription factor ATF-7		PRO_0000076593
Regions
	Domain	332 – 395	64	bZIP
	Zinc finger	7 – 31	25	C2H2-type
	Region	1 – 285	285	Transactivation domain By similarity
	Region	334 – 354	21	Basic motif By similarity
	Region	360 – 388	29	Leucine-zipper By similarity
	Compositional bias	118 – 253	136	Pro-rich
	Compositional bias	322 – 325	4	Poly-Arg
Amino acid modifications
	Modified residue	51	1	Phosphothreonine; by MAPK11 Ref.2
	Modified residue	53	1	Phosphothreonine Ref.2
	Modified residue	101	1	Phosphothreonine By similarity
	Cross-link	107		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8R0S1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: AFF4D1A7BFE71AF3	FASTA	413	44,608
	10 20 30 40 50 60 MGDDRPFVCS APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN 70 80 90 100 110 120 CEEVGLFNEL ASSFEHEFKK ASDDDEKKGA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD 130 140 150 160 170 180 SPASSPCSPP LKEKEVTTKP VVISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP 190 200 210 220 230 240 PSNRQIGSPT GSLPLVMHLA NGQTMPMLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN 250 260 270 280 290 300 NSGSISPSGH PMPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQNQILIQHP 310 320 330 340 350 360 DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL 370 380 390 400 410 EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LGK

References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[2]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND THR-53, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC026483 mRNA. Translation: AAH26483.1.
IPI	IPI00876501.
RefSeq	NP_666177.1. NM_146065.1.
UniGene	Mm.208714. Mm.475149.
3D structure databases
ProteinModelPortal	Q8R0S1.
SMR	Q8R0S1. Positions 1-38, 334-394.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-7557949.
Proteomic databases
PaxDb	Q8R0S1.
PRIDE	Q8R0S1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000108828; ENSMUSP00000104456; ENSMUSG00000052414. ENSMUST00000169033; ENSMUSP00000130130; ENSMUSG00000052414.
GeneID	223922.
KEGG	mmu:223922.
UCSC	uc007xwo.1. mouse.
Organism-specific databases
CTD	11016.
MGI	MGI:2443472. Atf7.
Phylogenomic databases
eggNOG	NOG306955.
GeneTree	ENSGT00390000020106.
HOVERGEN	HBG004300.
KO	K09045.
OMA	CMVPNIP.
Gene expression databases
ArrayExpress	Q8R0S1.
Bgee	Q8R0S1.
CleanEx	MM_ATF7.
Genevestigator	Q8R0S1.
GermOnline	ENSMUSG00000052414. Mus musculus.
Family and domain databases
Gene3D	3.30.160.60. 1 hit.
InterPro	IPR004827. bZIP. IPR016378. TF_cAMP-dep. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF00170. bZIP_1. 1 hit. [Graphical view]
PIRSF	PIRSF003153. ATF2_CRE-BP1. 1 hit.
SMART	SM00338. BRLZ. 1 hit. SM00355. ZnF_C2H2. 1 hit. [Graphical view]
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. 1 hit. PS00028. ZINC_FINGER_C2H2_1. 1 hit. PS50157. ZINC_FINGER_C2H2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATF7. mouse.
NextBio	376970.
SOURCE	Search...

Entry information

Entry name

ATF7_MOUSE

Accession

Primary (citable) accession number: Q8R0S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 1, 2002
Last modified:	May 29, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program