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Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha]

 ATF6A_MOUSE             Reviewed;         656 AA.
F6VAN0; B2RU98; Q8BZ84;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 60.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-6 alpha;
Short=cAMP-dependent transcription factor ATF-6 alpha;
AltName: Full=Activating transcription factor 6 alpha;
Short=ATF6-alpha;
Contains:
RecName: Full=Processed cyclic AMP-dependent transcription factor ATF-6 alpha;
Name=Atf6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH THBS1 AND THBS4, AND SUBCELLULAR LOCATION.
PubMed=22682248; DOI=10.1016/j.cell.2012.03.050;
Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A.,
Blair N.S., Lynch K.A., Okada T., Aronow B.J., Osinska H., Prywes R.,
Lorenz J.N., Mori K., Lawler J., Robbins J., Molkentin J.D.;
"A thrombospondin-dependent pathway for a protective ER stress
response.";
Cell 149:1257-1268(2012).
[5]
DISRUPTION PHENOTYPE.
PubMed=26029869; DOI=10.1038/ng.3319;
Kohl S., Zobor D., Chiang W.C., Weisschuh N., Staller J.,
Gonzalez Menendez I., Chang S., Beck S.C., Garcia Garrido M.,
Sothilingam V., Seeliger M.W., Stanzial F., Benedicenti F., Inzana F.,
Heon E., Vincent A., Beis J., Strom T.M., Rudolph G., Roosing S.,
Hollander A.I., Cremers F.P., Lopez I., Ren H., Moore A.T.,
Webster A.R., Michaelides M., Koenekoop R.K., Zrenner E.,
Kaufman R.J., Tsang S.H., Wissinger B., Lin J.H.;
"Mutations in the unfolded protein response regulator ATF6 cause the
cone dysfunction disorder achromatopsia.";
Nat. Genet. 47:757-765(2015).
-!- FUNCTION: 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-N(9)-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).
{ECO:0000250|UniProtKB:P18850}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P18850, ECO:0000269|PubMed:22682248}.
-!- INTERACTION:
Q3U182:Crtc2; NbExp=2; IntAct=EBI-6171558, EBI-8018890;
Q9Z1T2:Thbs4; NbExp=3; IntAct=EBI-6171558, EBI-6171531;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed cyclic AMP-dependent transcription
factor ATF-6 alpha: Nucleus. Note=Under ER stress the cleaved N-
terminal cytoplasmic domain translocates into the nucleus. THBS4
promotes its nuclear shuttling.
-!- DOMAIN: The basic domain functions as a nuclear localization
signal. {ECO:0000250}.
-!- DOMAIN: The basic leucine-zipper domain is sufficient for
association with the NF-Y trimer and binding to ERSE.
{ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
-!- PTM: Phosphorylated in vitro by MAPK14/P38MAPK. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Animals have normal retinal morphology and
function at a young age but develop rod and cone dysfunction with
increasing age. {ECO:0000269|PubMed:26029869}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC29389.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK036335; BAC29389.1; ALT_INIT; mRNA.
EMBL; AC113490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC125021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC141028; AAI41029.1; -; mRNA.
CCDS; CCDS56653.1; -.
RefSeq; NP_001074773.1; NM_001081304.1.
UniGene; Mm.377046; -.
ProteinModelPortal; F6VAN0; -.
BioGrid; 230540; 1.
DIP; DIP-59768N; -.
IntAct; F6VAN0; 4.
STRING; 10090.ENSMUSP00000027974; -.
iPTMnet; F6VAN0; -.
PhosphoSitePlus; F6VAN0; -.
MaxQB; F6VAN0; -.
PaxDb; F6VAN0; -.
PeptideAtlas; F6VAN0; -.
PRIDE; F6VAN0; -.
Ensembl; ENSMUST00000027974; ENSMUSP00000027974; ENSMUSG00000026663.
GeneID; 226641; -.
KEGG; mmu:226641; -.
UCSC; uc007dmj.1; mouse.
CTD; 22926; -.
MGI; MGI:1926157; Atf6.
eggNOG; KOG4343; Eukaryota.
eggNOG; ENOG410ZAAP; LUCA.
GeneTree; ENSGT00530000063762; -.
HOGENOM; HOG000253938; -.
HOVERGEN; HBG108357; -.
InParanoid; F6VAN0; -.
KO; K09054; -.
OMA; YRYDHSV; -.
OrthoDB; EOG091G0JCT; -.
TreeFam; TF316079; -.
Reactome; R-MMU-381033; ATF6 (ATF6-alpha) activates chaperones.
ChiTaRS; Atf6; mouse.
PRO; PR:F6VAN0; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026663; -.
Genevisible; F6VAN0; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
GO; GO:0001654; P:eye development; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; ISS:UniProtKB.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR029801; ATF6A.
InterPro; IPR004827; bZIP.
InterPro; IPR008917; TF_DNA-bd.
PANTHER; PTHR22952:SF116; PTHR22952:SF116; 1.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Complete proteome; DNA-binding; Endoplasmic reticulum;
Glycoprotein; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Signal-anchor; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix;
Ubl conjugation; Unfolded protein response.
CHAIN 1 656 Cyclic AMP-dependent transcription factor
ATF-6 alpha.
/FTId=PRO_0000424336.
CHAIN 1 ? Processed cyclic AMP-dependent
transcription factor ATF-6 alpha.
/FTId=PRO_0000424337.
TOPO_DOM 1 377 Cytoplasmic. {ECO:0000255}.
TRANSMEM 378 398 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 399 656 Lumenal. {ECO:0000255}.
DOMAIN 293 356 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 137 Transcription activation. {ECO:0000250}.
REGION 295 326 Basic motif.
REGION 335 342 Leucine-zipper.
REGION 455 575 Interaction with THBS4.
{ECO:0000269|PubMed:22682248}.
COMPBIAS 94 144 Ser-rich.
SITE 406 407 Cleavage; by PS1. {ECO:0000250}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 570 570 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 629 629 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P18850}.
CONFLICT 141 141 V -> I (in Ref. 3; AAI41029).
{ECO:0000305}.
CONFLICT 237 237 S -> P (in Ref. 3; AAI41029).
{ECO:0000305}.
CONFLICT 441 441 L -> P (in Ref. 1; BAC29389).
{ECO:0000305}.
SEQUENCE 656 AA; 72694 MW; C3ADCF7DF2CB3EC9 CRC64;
MESPFSPVLP HGPDEDWEST LFAELGYFTD TDDVHFDAAH EAYENNFDHL NFDLDLMPWE
SDLWSPGSHF CSDMKAEPQP LSPASSSCSI SSPRSTDSCS STQHVPEELD LLSSSQSPLS
LYGDSCNSPS SVEPLKEEKP VTGPGNKTEH GLTPKKKIQM SSKPSVQPKP LLLPAAPKTQ
TNASVPAKAI IIQTLPALMP LAKQQSIISI QPAPTKGQTV LLSQPTVVQL QSPAVLSSAQ
PVLAVTGGAA QLPNHVVNVL PAPVVSSPVN GKLSVTKPVL QSATRSMGSD IAVLRRQQRM
IKNRESACQS RKKKKEYMLG LEARLKAALS ENEQLKKENG SLKRQLDEVV SENQRLKVPS
PKRRAVCVMI VLAFIMLNYG PMSMLEQESR RVKPSVSPAN QRRHLLEFSA KEVKDTSDGD
NQKDSYSYDH SVSNDKALMV LSEEPLLYMP PPPCQPLINT TESLRLNHEL RGWVHRHEVE
RTKSRRMTNS QQKARILQGA LEQGSNSQLM AVQYTETTSI SRNSGSELQV YYASPGSYQG
FFDAIRRRGD TFYVVSFRRD HLLLPATTHN KTTRPKMSIV LPAININDNV INGQDYEVMM
QIDCQVMDTR ILHIKSSSVP PYLRDHQRNQ TSTFFGSPPT TTETTHVVST IPESLQ


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