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Protein

Cyclic AMP-dependent transcription factor ATF-6 alpha

Gene

Atf6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transmembrane glycoprotein of the endoplasmic reticulum that functions as a transcription activator and initiates the unfolded protein response (UPR) during endoplasmic reticulum stress. Cleaved upon ER stress, the N-terminal processed cyclic AMP-dependent transcription factor ATF-6 alpha translocates to the nucleus where it activates transcription of genes involved in the UPR. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N9-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. May play a role in foveal development and cone function in the retina (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation, Unfolded protein response

Enzyme and pathway databases

ReactomeiR-MMU-381033. ATF6 (ATF6-alpha) activates chaperones.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-dependent transcription factor ATF-6 alpha
Short name:
cAMP-dependent transcription factor ATF-6 alpha
Alternative name(s):
Activating transcription factor 6 alpha
Short name:
ATF6-alpha
Cleaved into the following chain:
Gene namesi
Name:Atf6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1926157. Atf6.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 377CytoplasmicSequence analysisAdd BLAST377
Transmembranei378 – 398Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini399 – 656LumenalSequence analysisAdd BLAST258

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Animals have normal retinal morphology and function at a young age but develop rod and cone dysfunction with increasing age.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004243361 – 656Cyclic AMP-dependent transcription factor ATF-6 alphaAdd BLAST656
ChainiPRO_00004243371 – ?Processed cyclic AMP-dependent transcription factor ATF-6 alpha

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Glycosylationi459N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi570N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi629N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (By similarity).By similarity
N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR) (By similarity).By similarity
Phosphorylated in vitro by MAPK14/P38MAPK.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei406 – 407Cleavage; by PS1By similarity2

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiF6VAN0.
PaxDbiF6VAN0.
PeptideAtlasiF6VAN0.
PRIDEiF6VAN0.

PTM databases

iPTMnetiF6VAN0.
PhosphoSitePlusiF6VAN0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026663.
GenevisibleiF6VAN0. MM.

Interactioni

Subunit structurei

Homodimer and heterodimer with ATF6-beta. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC). Interacts also with the transcription factors GTF2I, YY1 and SRF. Interacts with XBP1 isoform 2; the interaction occurs in a ER stress-dependent manner (By similarity). Interacts (via lumenal domain) with THBS1 (PubMed:22682248). Interacts with THBS4 (via EGF-like 3; calcium-binding domain) which facilitates its processing, activation and nuclear translocation (PubMed:22682248).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230540. 1 interactor.
DIPiDIP-59768N.
IntActiF6VAN0. 4 interactors.
STRINGi10090.ENSMUSP00000027974.

Structurei

3D structure databases

ProteinModelPortaliF6VAN0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini293 – 356bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 137Transcription activationBy similarityAdd BLAST137
Regioni295 – 326Basic motifAdd BLAST32
Regioni335 – 342Leucine-zipper8
Regioni455 – 575Interaction with THBS41 PublicationAdd BLAST121

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi94 – 144Ser-richAdd BLAST51

Domaini

The basic domain functions as a nuclear localization signal.By similarity
The basic leucine-zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE.By similarity

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4343. Eukaryota.
ENOG410ZAAP. LUCA.
GeneTreeiENSGT00530000063762.
HOGENOMiHOG000253938.
HOVERGENiHBG108357.
InParanoidiF6VAN0.
KOiK09054.
OMAiYRYDHSV.
OrthoDBiEOG091G0JCT.
TreeFamiTF316079.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiView protein in InterPro
IPR029801. ATF6A.
IPR004827. bZIP.
IPR008917. TF_DNA-bd_sf.
PANTHERiPTHR22952:SF116. PTHR22952:SF116. 1 hit.
PfamiView protein in Pfam
PF00170. bZIP_1. 1 hit.
SMARTiView protein in SMART
SM00338. BRLZ. 1 hit.
PROSITEiView protein in PROSITE
PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F6VAN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESPFSPVLP HGPDEDWEST LFAELGYFTD TDDVHFDAAH EAYENNFDHL
60 70 80 90 100
NFDLDLMPWE SDLWSPGSHF CSDMKAEPQP LSPASSSCSI SSPRSTDSCS
110 120 130 140 150
STQHVPEELD LLSSSQSPLS LYGDSCNSPS SVEPLKEEKP VTGPGNKTEH
160 170 180 190 200
GLTPKKKIQM SSKPSVQPKP LLLPAAPKTQ TNASVPAKAI IIQTLPALMP
210 220 230 240 250
LAKQQSIISI QPAPTKGQTV LLSQPTVVQL QSPAVLSSAQ PVLAVTGGAA
260 270 280 290 300
QLPNHVVNVL PAPVVSSPVN GKLSVTKPVL QSATRSMGSD IAVLRRQQRM
310 320 330 340 350
IKNRESACQS RKKKKEYMLG LEARLKAALS ENEQLKKENG SLKRQLDEVV
360 370 380 390 400
SENQRLKVPS PKRRAVCVMI VLAFIMLNYG PMSMLEQESR RVKPSVSPAN
410 420 430 440 450
QRRHLLEFSA KEVKDTSDGD NQKDSYSYDH SVSNDKALMV LSEEPLLYMP
460 470 480 490 500
PPPCQPLINT TESLRLNHEL RGWVHRHEVE RTKSRRMTNS QQKARILQGA
510 520 530 540 550
LEQGSNSQLM AVQYTETTSI SRNSGSELQV YYASPGSYQG FFDAIRRRGD
560 570 580 590 600
TFYVVSFRRD HLLLPATTHN KTTRPKMSIV LPAININDNV INGQDYEVMM
610 620 630 640 650
QIDCQVMDTR ILHIKSSSVP PYLRDHQRNQ TSTFFGSPPT TTETTHVVST

IPESLQ
Length:656
Mass (Da):72,694
Last modified:October 3, 2012 - v2
Checksum:iC3ADCF7DF2CB3EC9
GO

Sequence cautioni

The sequence BAC29389 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti141V → I in AAI41029 (PubMed:15489334).Curated1
Sequence conflicti237S → P in AAI41029 (PubMed:15489334).Curated1
Sequence conflicti441L → P in BAC29389 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036335 mRNA. Translation: BAC29389.1. Different initiation.
AC113490 Genomic DNA. No translation available.
AC125021 Genomic DNA. No translation available.
BC141028 mRNA. Translation: AAI41029.1.
CCDSiCCDS56653.1.
RefSeqiNP_001074773.1. NM_001081304.1.
UniGeneiMm.377046.

Genome annotation databases

EnsembliENSMUST00000027974; ENSMUSP00000027974; ENSMUSG00000026663.
GeneIDi226641.
KEGGimmu:226641.
UCSCiuc007dmj.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiATF6A_MOUSE
AccessioniPrimary (citable) accession number: F6VAN0
Secondary accession number(s): B2RU98, Q8BZ84
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2013
Last sequence update: October 3, 2012
Last modified: November 22, 2017
This is version 61 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families