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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_HUMAN             Reviewed;         670 AA.
P18850; O15139; Q5VW62; Q6IPB5; Q9UEC9;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 3.
25-OCT-2017, entry version 190.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-67; PRO-145 AND SER-157.
TISSUE=Cervix carcinoma;
PubMed=9271374; DOI=10.1128/MCB.17.9.4957;
Zhu C., Johansen F.E., Prywes R.;
"Interaction of ATF6 and serum response factor.";
Mol. Cell. Biol. 17:4957-4966(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-145 AND SER-157.
TISSUE=Cervix carcinoma;
PubMed=9837962; DOI=10.1074/jbc.273.50.33741;
Yoshida H., Haze K., Yanagi H., Yura T., Mori K.;
"Identification of the cis-acting endoplasmic reticulum stress
response element responsible for transcriptional induction of
mammalian glucose-regulated proteins; involvement of basic-leucine
zipper transcription factors.";
J. Biol. Chem. 273:33741-33749(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-202, AND VARIANT VAL-67.
TISSUE=Pancreas;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 302-369.
PubMed=2516827; DOI=10.1101/gad.3.12b.2083;
Hai T., Liu F., Coukos W.J., Green M.R.;
"Transcription factor ATF cDNA clones: an extensive family of leucine
zipper proteins able to selectively form DNA-binding heterodimers.";
Genes Dev. 3:2083-2090(1989).
[6]
ERRATUM.
Hai T., Liu F., Coukos W.J., Green M.R.;
Genes Dev. 4:682-682(1990).
[7]
FUNCTION, AND CHARACTERIZATION.
PubMed=10564271; DOI=10.1091/mbc.10.11.3787;
Haze K., Yoshida H., Yanagi H., Yura T., Mori K.;
"Mammalian transcription factor ATF6 is synthesized as a transmembrane
protein and activated by proteolysis in response to endoplasmic
reticulum stress.";
Mol. Biol. Cell 10:3787-3799(1999).
[8]
PROTEOLYTIC PROCESSING BY PS1 AND PS2, AND MUTAGENESIS OF ASN-391;
PRO-394; 415-ARG-ARG-416 AND LEU-419.
PubMed=11163209; DOI=10.1016/S1097-2765(00)00133-7;
Ye J., Rawson R.B., Komuro R., Chen X., Dave U.P., Prywes R.,
Brown M.S., Goldstein J.L.;
"ER stress induces cleavage of membrane-bound ATF6 by the same
proteases that process SREBPs.";
Mol. Cell 6:1355-1364(2000).
[9]
FUNCTION, AND DNA-BINDING.
PubMed=11779464; DOI=10.1016/S0092-8674(01)00611-0;
Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K.;
"XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER
stress to produce a highly active transcription factor.";
Cell 107:881-891(2001).
[10]
FUNCTION.
PubMed=11158310; DOI=10.1128/MCB.21.4.1239-1248.2001;
Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M.,
Mori K.;
"Endoplasmic reticulum stress-induced formation of transcription
factor complex ERSF including NF-Y (CBF) and activating transcription
factors 6alpha and 6beta that activates the mammalian unfolded protein
response.";
Mol. Cell. Biol. 21:1239-1248(2001).
[11]
REVIEW.
PubMed=11483355; DOI=10.1016/S0378-1119(01)00551-0;
Hai T., Hartman M.G.;
"The molecular biology and nomenclature of the activating
transcription factor/cAMP responsive element binding family of
transcription factors: activating transcription factor proteins and
homeostasis.";
Gene 273:1-11(2001).
[12]
GLYCOSYLATION AT ASN-472; ASN-584 AND ASN-643, AND MUTAGENESIS OF
THR-474; THR-586 AND THR-645.
PubMed=14699159; DOI=10.1074/jbc.M309804200;
Hong M., Luo S., Baumeister P., Huang J.M., Gogia R.K., Li M.,
Lee A.S.;
"Underglycosylation of ATF6 as a novel sensing mechanism for
activation of the unfolded protein response.";
J. Biol. Chem. 279:11354-11363(2004).
[13]
INTERACTION WITH XBP1.
PubMed=17765680; DOI=10.1016/j.devcel.2007.07.018;
Yamamoto K., Sato T., Matsui T., Sato M., Okada T., Yoshida H.,
Harada A., Mori K.;
"Transcriptional induction of mammalian ER quality control proteins is
mediated by single or combined action of ATF6alpha and XBP1.";
Dev. Cell 13:365-376(2007).
[14]
INTERACTION WITH THBS4.
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).
[15]
INVOLVEMENT IN ACHM7.
PubMed=26063662; DOI=10.1007/s00439-015-1571-4;
University of Washington Center for Mendelian Genomics;
Ansar M., Santos-Cortez R.L., Saqib M.A., Zulfiqar F., Lee K.,
Ashraf N.M., Ullah E., Wang X., Sajid S., Khan F.S., Amin-ud-Din M.,
Smith J.D., Shendure J., Bamshad M.J., Nickerson D.A., Hameed A.,
Riazuddin S., Ahmed Z.M., Ahmad W., Leal S.M.;
"Mutation of ATF6 causes autosomal recessive achromatopsia.";
Hum. Genet. 134:941-950(2015).
[16]
FUNCTION, INVOLVEMENT IN ACHM7, VARIANTS ACHM7 CYS-324 AND ASN-567,
AND CHARACTERIZATION OF VARIANT ACHM7 CYS-324.
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).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- 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. {ECO:0000269|PubMed:10564271,
ECO:0000269|PubMed:11158310, ECO:0000269|PubMed:11779464,
ECO:0000269|PubMed:26029869}.
-!- 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 (via
lumenal domain) with THBS1 (By similarity). Interacts with THBS4
(via EGF-like 3; calcium-binding domain) which facilitates its
processing, activation and nuclear translocation
(PubMed:22682248). Interacts with XBP1 isoform 2; the interaction
occurs in a ER stress-dependent manner (PubMed:17765680).
{ECO:0000250, ECO:0000269|PubMed:17765680,
ECO:0000269|PubMed:22682248}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-852157, EBI-852157;
Q68CJ9:CREB3L3; NbExp=2; IntAct=EBI-852157, EBI-852194;
Q53ET0:CRTC2; NbExp=3; IntAct=EBI-852157, EBI-1181987;
Q3U182:Crtc2 (xeno); NbExp=2; IntAct=EBI-852157, EBI-8018890;
P11021:HSPA5; NbExp=2; IntAct=EBI-852157, EBI-354921;
P17861:XBP1; NbExp=2; IntAct=EBI-852157, EBI-6942961;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type II membrane protein.
-!- 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.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The basic domain functions as a nuclear localization
signal.
-!- DOMAIN: The basic leucine-zipper domain is sufficient for
association with the NF-Y trimer and binding to ERSE.
-!- 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.
{ECO:0000269|PubMed:11163209}.
-!- 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).
{ECO:0000269|PubMed:14699159}.
-!- PTM: Phosphorylated in vitro by MAPK14/P38MAPK.
-!- DISEASE: Achromatopsia 7 (ACHM7) [MIM:616517]: A form of
achromatopsia, an ocular stationary disorder due to the absence of
functioning cone photoreceptors in the retina. It is characterized
by total colorblindness, low visual acuity, photophobia and
nystagmus. {ECO:0000269|PubMed:26029869,
ECO:0000269|PubMed:26063662}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
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EMBL; AF005887; AAB64434.1; -; mRNA.
EMBL; AB015856; BAA34722.1; -; mRNA.
EMBL; AL391825; CAH73985.1; -; Genomic_DNA.
EMBL; AL359541; CAH73985.1; JOINED; Genomic_DNA.
EMBL; AL450995; CAH73985.1; JOINED; Genomic_DNA.
EMBL; AL450995; CAH71144.1; -; Genomic_DNA.
EMBL; AL359541; CAH71144.1; JOINED; Genomic_DNA.
EMBL; AL391825; CAH71144.1; JOINED; Genomic_DNA.
EMBL; AL359541; CAH74152.1; -; Genomic_DNA.
EMBL; AL391825; CAH74152.1; JOINED; Genomic_DNA.
EMBL; AL450995; CAH74152.1; JOINED; Genomic_DNA.
EMBL; BC014969; AAH14969.1; -; mRNA.
EMBL; BC071997; AAH71997.1; -; mRNA.
CCDS; CCDS1235.1; -.
PIR; F34223; F34223.
RefSeq; NP_031374.2; NM_007348.3.
UniGene; Hs.492740; -.
UniGene; Hs.617868; -.
ProteinModelPortal; P18850; -.
BioGrid; 116586; 48.
DIP; DIP-29304N; -.
ELM; P18850; -.
IntAct; P18850; 27.
MINT; MINT-268075; -.
STRING; 9606.ENSP00000356919; -.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; P18850; -.
PhosphoSitePlus; P18850; -.
BioMuta; ATF6; -.
DMDM; 66774203; -.
EPD; P18850; -.
MaxQB; P18850; -.
PaxDb; P18850; -.
PeptideAtlas; P18850; -.
PRIDE; P18850; -.
DNASU; 22926; -.
Ensembl; ENST00000367942; ENSP00000356919; ENSG00000118217.
GeneID; 22926; -.
KEGG; hsa:22926; -.
UCSC; uc001gbs.4; human.
CTD; 22926; -.
DisGeNET; 22926; -.
EuPathDB; HostDB:ENSG00000118217.5; -.
GeneCards; ATF6; -.
H-InvDB; HIX0001253; -.
HGNC; HGNC:791; ATF6.
HPA; HPA005935; -.
MalaCards; ATF6; -.
MIM; 605537; gene.
MIM; 616517; phenotype.
neXtProt; NX_P18850; -.
OpenTargets; ENSG00000118217; -.
PharmGKB; PA25091; -.
eggNOG; KOG4343; Eukaryota.
eggNOG; ENOG410ZAAP; LUCA.
GeneTree; ENSGT00530000063762; -.
HOGENOM; HOG000253938; -.
HOVERGEN; HBG108357; -.
InParanoid; P18850; -.
KO; K09054; -.
OMA; YRYDHSV; -.
OrthoDB; EOG091G0JCT; -.
PhylomeDB; P18850; -.
TreeFam; TF316079; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-381033; ATF6 (ATF6-alpha) activates chaperones.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
SignaLink; P18850; -.
SIGNOR; P18850; -.
ChiTaRS; ATF6; human.
GeneWiki; ATF6; -.
GenomeRNAi; 22926; -.
PMAP-CutDB; P18850; -.
PRO; PR:P18850; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000118217; -.
CleanEx; HS_ATF6; -.
Genevisible; P18850; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IC:NTNU_SB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:BHF-UCL.
GO; GO:0001654; P:eye development; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; TAS:ProtInc.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006950; P:response to stress; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007601; P:visual perception; IMP: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; Disease mutation; DNA-binding;
Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Membrane;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Signal-anchor; Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation; Unfolded protein response.
CHAIN 1 670 Cyclic AMP-dependent transcription factor
ATF-6 alpha.
/FTId=PRO_0000076589.
CHAIN 1 ? Processed cyclic AMP-dependent
transcription factor ATF-6 alpha.
/FTId=PRO_0000296200.
TOPO_DOM 1 377 Cytoplasmic. {ECO:0000255}.
TRANSMEM 378 398 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 399 670 Lumenal. {ECO:0000255}.
DOMAIN 306 369 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 150 Transcription activation.
REGION 308 339 Basic motif.
REGION 348 355 Leucine-zipper.
REGION 468 589 Interaction with THBS4.
{ECO:0000269|PubMed:22682248}.
COMPBIAS 124 127 Poly-Ser.
COMPBIAS 325 328 Poly-Lys.
COMPBIAS 463 466 Poly-Pro.
SITE 419 420 Cleavage; by PS1. {ECO:0000250}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14699159}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14699159}.
CARBOHYD 643 643 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14699159}.
CROSSLNK 87 87 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 67 67 M -> L (in dbSNP:rs1058405).
{ECO:0000269|PubMed:9271374}.
/FTId=VAR_022455.
VARIANT 67 67 M -> V (in dbSNP:rs1058405).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_022456.
VARIANT 145 145 A -> P (in dbSNP:rs2070150).
{ECO:0000269|PubMed:9271374,
ECO:0000269|PubMed:9837962}.
/FTId=VAR_022457.
VARIANT 157 157 P -> S (in dbSNP:rs1135983).
{ECO:0000269|PubMed:9271374,
ECO:0000269|PubMed:9837962}.
/FTId=VAR_022458.
VARIANT 324 324 R -> C (in ACHM7; reduced ATF6-mediated
unfolded protein response;
dbSNP:rs761357250).
{ECO:0000269|PubMed:26029869}.
/FTId=VAR_075681.
VARIANT 567 567 Y -> N (in ACHM7; dbSNP:rs796065053).
{ECO:0000269|PubMed:26029869}.
/FTId=VAR_075682.
MUTAGEN 391 391 N->F: Loss of proteolytic cleavage; when
associated with L-394.
{ECO:0000269|PubMed:11163209}.
MUTAGEN 394 394 P->L: Loss of proteolytic cleavage; when
associated with F-391.
{ECO:0000269|PubMed:11163209}.
MUTAGEN 415 416 RR->AA: Reduces proteolytic cleavage.
{ECO:0000269|PubMed:11163209}.
MUTAGEN 419 419 L->V: Reduces proteolytic cleavage.
{ECO:0000269|PubMed:11163209}.
MUTAGEN 474 474 T->I: Loss of glycosylation at Asn-472
and increase of Golgi translocation rate.
{ECO:0000269|PubMed:14699159}.
MUTAGEN 586 586 T->I: Loss of glycosylation at Asn-584
and increase of Golgi translocation rate.
Higher increase in Golgi translocation
rate; when associated with Ile-645.
{ECO:0000269|PubMed:14699159}.
MUTAGEN 645 645 T->I: Loss of glycosylation at Asn-643
and increase of Golgi translocation rate.
Higher increase in Golgi translocation
rate; when associated with Ile-586.
{ECO:0000269|PubMed:14699159}.
CONFLICT 195 195 N -> I (in Ref. 4; AAH14969/AAH71997).
{ECO:0000305}.
CONFLICT 198 201 VPAK -> IPPQ (in Ref. 4; AAH14969/
AAH71997). {ECO:0000305}.
CONFLICT 307 307 L -> I (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 354 354 T -> R (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 366 369 NQRL -> LRNS (in Ref. 5; no nucleotide
entry). {ECO:0000305}.
CONFLICT 410 410 S -> G (in Ref. 1; AAB64434).
{ECO:0000305}.
CONFLICT 513 514 AL -> VV (in Ref. 1; AAB64434).
{ECO:0000305}.
SEQUENCE 670 AA; 74585 MW; 5EBD08CF4121D41A CRC64;
MGEPAGVAGT MESPFSPGLF HRLDEDWDSA LFAELGYFTD TDELQLEAAN ETYENNFDNL
DFDLDLMPWE SDIWDINNQI CTVKDIKAEP QPLSPASSSY SVSSPRSVDS YSSTQHVPEE
LDLSSSSQMS PLSLYGENSN SLSSAEPLKE DKPVTGPRNK TENGLTPKKK IQVNSKPSIQ
PKPLLLPAAP KTQTNSSVPA KTIIIQTVPT LMPLAKQQPI ISLQPAPTKG QTVLLSQPTV
VQLQAPGVLP SAQPVLAVAG GVTQLPNHVV NVVPAPSANS PVNGKLSVTK PVLQSTMRNV
GSDIAVLRRQ QRMIKNRESA CQSRKKKKEY MLGLEARLKA ALSENEQLKK ENGTLKRQLD
EVVSENQRLK VPSPKRRVVC VMIVLAFIIL NYGPMSMLEQ DSRRMNPSVS PANQRRHLLG
FSAKEAQDTS DGIIQKNSYR YDHSVSNDKA LMVLTEEPLL YIPPPPCQPL INTTESLRLN
HELRGWVHRH EVERTKSRRM TNNQQKTRIL QGALEQGSNS QLMAVQYTET TSSISRNSGS
ELQVYYASPR SYQDFFEAIR RRGDTFYVVS FRRDHLLLPA TTHNKTTRPK MSIVLPAINI
NENVINGQDY EVMMQIDCQV MDTRILHIKS SSVPPYLRDQ QRNQTNTFFG SPPAATEATH
VVSTIPESLQ


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