ID   ATF6B_HUMAN             Reviewed;         703 AA.
AC   Q99941; B0UYX6; Q13269; Q14343; Q14345; Q5SSW7; Q99635; Q99637; Q9H3V9;
AC   Q9H3W1; Q9NPL0;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-6 beta;
DE            Short=cAMP-dependent transcription factor ATF-6 beta;
DE   AltName: Full=Activating transcription factor 6 beta;
DE            Short=ATF6-beta;
DE   AltName: Full=Protein G13;
DE   AltName: Full=cAMP response element-binding protein-related protein;
DE            Short=Creb-rp;
DE   AltName: Full=cAMP-responsive element-binding protein-like 1;
DE   Contains:
DE     RecName: Full=Processed cyclic AMP-dependent transcription factor ATF-6 beta;
GN   Name=ATF6B; Synonyms=CREBL1, G13;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Tonsil;
RX   PubMed=8586413; DOI=10.1006/geno.1995.9891;
RA   Min J., Shukla H., Kozono H., Bronson S.K., Weissman S.M., Chaplin D.D.;
RT   "A novel Creb family gene telomeric of HLA-DRA in the HLA complex.";
RL   Genomics 30:149-156(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX   PubMed=8870652; DOI=10.1042/bj3190081;
RA   Khanna A., Campbell R.D.;
RT   "The gene G13 in the class III region of the human MHC encodes a potential
RT   DNA-binding protein.";
RL   Biochem. J. 319:81-89(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=8923003; DOI=10.1093/hmg/5.11.1749;
RA   Speek M., Barry F., Miller W.L.;
RT   "Alternate promoters and alternate splicing of human tenascin-X, a gene
RT   with 5' and 3' ends buried in other genes.";
RL   Hum. Mol. Genet. 5:1749-1758(1996).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX   PubMed=11256944; DOI=10.1042/0264-6021:3550019;
RA   Haze K., Okada T., Yoshida H., Yanagi H., Yura T., Negishi M., Mori K.;
RT   "Identification of the G13 (cAMP-response-element-binding protein-related
RT   protein) gene product related to activating transcription factor 6 as a
RT   transcriptional activator of the mammalian unfolded protein response.";
RL   Biochem. J. 355:19-28(2001).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 beta]:
CC       Precursor of the transcription factor form (Processed cyclic AMP-
CC       dependent transcription factor ATF-6 beta), which is embedded in the
CC       endoplasmic reticulum membrane (PubMed:11256944). Endoplasmic reticulum
CC       stress promotes processing of this form, releasing the transcription
CC       factor form that translocates into the nucleus, where it activates
CC       transcription of genes involved in the unfolded protein response (UPR)
CC       (PubMed:11256944). {ECO:0000269|PubMed:11256944}.
CC   -!- FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6
CC       beta]: Transcription factor that acts in the unfolded protein response
CC       (UPR) pathway by activating UPR target genes induced during ER stress
CC       (PubMed:11256944). Binds DNA on the 5'-CCAC[GA]-3' half of the ER
CC       stress response element (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is
CC       bound to ERSE (PubMed:11256944). {ECO:0000269|PubMed:11256944}.
CC   -!- SUBUNIT: [Processed cyclic AMP-dependent transcription factor ATF-6
CC       beta]: Homodimer and heterodimer with ATF6-alpha. The dimer interacts
CC       with the nuclear transcription factor Y (NF-Y) trimer through direct
CC       binding to NF-Y subunit C (NF-YC). {ECO:0000269|PubMed:11256944}.
CC   -!- INTERACTION:
CC       Q99941; P18850: ATF6; NbExp=2; IntAct=EBI-2841031, EBI-852157;
CC       Q99941; P17861: XBP1; NbExp=2; IntAct=EBI-2841031, EBI-6942961;
CC       Q99941; PRO_0000037575 [P27958]; Xeno; NbExp=5; IntAct=EBI-2841031, EBI-8763498;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11256944}; Single-pass type II membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription
CC       factor ATF-6 beta]: Nucleus {ECO:0000269|PubMed:11256944}. Note=Under
CC       ER stress the cleaved N-terminal cytoplasmic domain translocates into
CC       the nucleus. {ECO:0000269|PubMed:11256944}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=Q99941-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q99941-2; Sequence=VSP_000593;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11256944}.
CC   -!- DOMAIN: The basic domain functions as a nuclear localization signal.
CC       {ECO:0000269|PubMed:11256944}.
CC   -!- DOMAIN: The basic leucine-zipper domain is sufficient for association
CC       with the NF-Y trimer and binding to ERSE.
CC       {ECO:0000269|PubMed:11256944}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11256944}.
CC   -!- PTM: During unfolded protein response, a fragment of approximately 60
CC       kDa containing the cytoplasmic transcription factor domain is released
CC       by proteolysis. The cleavage is probably performed sequentially by
CC       site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases.
CC       {ECO:0000305|PubMed:11256944}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC50888.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAG14898.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U31903; AAA97438.1; -; mRNA.
DR   EMBL; X98053; CAA66663.1; -; Genomic_DNA.
DR   EMBL; X98054; CAA66664.1; -; mRNA.
DR   EMBL; U89337; AAB47487.1; -; Genomic_DNA.
DR   EMBL; AL049547; CAB89295.1; -; Genomic_DNA.
DR   EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR925796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03581.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03583.1; -; Genomic_DNA.
DR   EMBL; U52694; AAG14900.1; -; Genomic_DNA.
DR   EMBL; U52696; AAC50888.1; ALT_FRAME; mRNA.
DR   EMBL; U52693; AAG14898.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U52701; AAC50883.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS4737.1; -. [Q99941-1]
DR   CCDS; CCDS47408.1; -. [Q99941-2]
DR   RefSeq; NP_001129625.1; NM_001136153.1. [Q99941-2]
DR   RefSeq; NP_004372.3; NM_004381.4. [Q99941-1]
DR   AlphaFoldDB; Q99941; -.
DR   SMR; Q99941; -.
DR   BioGRID; 107778; 75.
DR   ComplexPortal; CPX-6595; bZIP transcription factor complex, ATF6-ATF6B.
DR   ComplexPortal; CPX-6596; bZIP transcription factor complex, ATF6B-ATF6B.
DR   ComplexPortal; CPX-6600; bZIP transcription factor complex, ATF6B-XBP1.
DR   ComplexPortal; CPX-6601; bZIP transcription factor complex, ATF6B-CREBZF.
DR   IntAct; Q99941; 24.
DR   STRING; 9606.ENSP00000364349; -.
DR   GlyCosmos; Q99941; 6 sites, 1 glycan.
DR   GlyGen; Q99941; 7 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; Q99941; -.
DR   PhosphoSitePlus; Q99941; -.
DR   BioMuta; ATF6B; -.
DR   DMDM; 20137431; -.
DR   EPD; Q99941; -.
DR   jPOST; Q99941; -.
DR   MassIVE; Q99941; -.
DR   MaxQB; Q99941; -.
DR   PaxDb; 9606-ENSP00000364349; -.
DR   PeptideAtlas; Q99941; -.
DR   ProteomicsDB; 78531; -. [Q99941-1]
DR   ProteomicsDB; 78532; -. [Q99941-2]
DR   Pumba; Q99941; -.
DR   Antibodypedia; 49313; 220 antibodies from 32 providers.
DR   Antibodypedia; 7841; 34 antibodies from 3 providers.
DR   DNASU; 1388; -.
DR   Ensembl; ENST00000293709.10; ENSP00000293709.6; ENSG00000168468.12. [Q99941-1]
DR   Ensembl; ENST00000375201.8; ENSP00000364347.4; ENSG00000213676.13. [Q99941-2]
DR   Ensembl; ENST00000375203.8; ENSP00000364349.3; ENSG00000213676.13. [Q99941-1]
DR   Ensembl; ENST00000383156.8; ENSP00000372642.4; ENSG00000168468.12. [Q99941-2]
DR   Ensembl; ENST00000425571.6; ENSP00000404814.2; ENSG00000228628.8. [Q99941-1]
DR   Ensembl; ENST00000427136.6; ENSP00000404725.2; ENSG00000234539.9. [Q99941-1]
DR   Ensembl; ENST00000435768.6; ENSP00000399764.2; ENSG00000228628.8. [Q99941-2]
DR   Ensembl; ENST00000439240.6; ENSP00000391131.2; ENSG00000234539.9. [Q99941-2]
DR   GeneID; 1388; -.
DR   KEGG; hsa:1388; -.
DR   MANE-Select; ENST00000375203.8; ENSP00000364349.3; NM_004381.5; NP_004372.3.
DR   UCSC; uc003nzn.4; human. [Q99941-1]
DR   AGR; HGNC:2349; -.
DR   CTD; 1388; -.
DR   DisGeNET; 1388; -.
DR   GeneCards; ATF6B; -.
DR   HGNC; HGNC:2349; ATF6B.
DR   HPA; ENSG00000213676; Low tissue specificity.
DR   MIM; 600984; gene.
DR   neXtProt; NX_Q99941; -.
DR   OpenTargets; ENSG00000213676; -.
DR   PharmGKB; PA164716250; -.
DR   VEuPathDB; HostDB:ENSG00000213676; -.
DR   eggNOG; KOG4343; Eukaryota.
DR   GeneTree; ENSGT00940000160798; -.
DR   HOGENOM; CLU_026136_0_0_1; -.
DR   InParanoid; Q99941; -.
DR   OMA; FKCESME; -.
DR   OrthoDB; 5396881at2759; -.
DR   PhylomeDB; Q99941; -.
DR   TreeFam; TF316079; -.
DR   PathwayCommons; Q99941; -.
DR   Reactome; R-HSA-8874177; ATF6B (ATF6-beta) activates chaperones.
DR   SignaLink; Q99941; -.
DR   SIGNOR; Q99941; -.
DR   BioGRID-ORCS; 1388; 22 hits in 1184 CRISPR screens.
DR   ChiTaRS; ATF6B; human.
DR   GeneWiki; CREBL1; -.
DR   GenomeRNAi; 1388; -.
DR   Pharos; Q99941; Tbio.
DR   PRO; PR:Q99941; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q99941; Protein.
DR   Bgee; ENSG00000168468; Expressed in thyroid gland.
DR   ExpressionAtlas; Q99941; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:1903892; P:negative regulation of ATF6-mediated unfolded protein response; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd14700; bZIP_ATF6; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR46164; ATF6, ISOFORM C; 1.
DR   PANTHER; PTHR46164:SF2; CYCLIC AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-6 BETA; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   Genevisible; Q99941; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; DNA-binding;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus; Reference proteome;
KW   Signal-anchor; Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix; Unfolded protein response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..703
FT                   /note="Cyclic AMP-dependent transcription factor ATF-6
FT                   beta"
FT                   /id="PRO_0000076590"
FT   CHAIN           2..?
FT                   /note="Processed cyclic AMP-dependent transcription factor
FT                   ATF-6 beta"
FT                   /id="PRO_0000296201"
FT   TOPO_DOM        2..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..703
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          325..388
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          2..86
FT                   /note="Transcription activation"
FT   REGION          87..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..347
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          350..357
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          447..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..316
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            410
FT                   /note="Important for cleavage by MBTPS2"
FT                   /evidence="ECO:0000250|UniProtKB:P18850"
FT   SITE            413
FT                   /note="Important for cleavage by MBTPS2"
FT                   /evidence="ECO:0000250|UniProtKB:P18850"
FT   SITE            440..441
FT                   /note="Cleavage; by MBTPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P18850"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        627
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        676
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         28..31
FT                   /note="GLQN -> D (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:8586413"
FT                   /id="VSP_000593"
FT   CONFLICT        3
FT                   /note="E -> D (in Ref. 2; CAA66664)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329..330
FT                   /note="QQ -> HE (in Ref. 2; CAA66664)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="V -> D (in Ref. 6; AAC50888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        600
FT                   /note="D -> G (in Ref. 1; AAA97438)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   703 AA;  76709 MW;  B04C7B23E7D83F82 CRC64;
     MAELMLLSEI ADPTRFFTDN LLSPEDWGLQ NSTLYSGLDE VAEEQTQLFR CPEQDVPFDG
     SSLDVGMDVS PSEPPWELLP IFPDLQVKSE PSSPCSSSSL SSESSRLSTE PSSEALGVGE
     VLHVKTESLA PPLCLLGDDP TSSFETVQIN VIPTSDDSSD VQTKIEPVSP CSSVNSEASL
     LSADSSSQAF IGEEVLEVKT ESLSPSGCLL WDVPAPSLGA VQISMGPSLD GSSGKALPTR
     KPPLQPKPVV LTTVPMPSRA VPPSTTVLLQ SLVQPPPVSP VVLIQGAIRV QPEGPAPSLP
     RPERKSIVPA PMPGNSCPPE VDAKLLKRQQ RMIKNRESAC QSRRKKKEYL QGLEARLQAV
     LADNQQLRRE NAALRRRLEA LLAENSELKL GSGNRKVVCI MVFLLFIAFN FGPVSISEPP
     SAPISPRMNK GEPQPRRHLL GFSEQEPVQG VEPLQGSSQG PKEPQPSPTD QPSFSNLTAF
     PGGAKELLLR DLDQLFLSSD CRHFNRTESL RLADELSGWV QRHQRGRRKI PQRAQERQKS
     QPRKKSPPVK AVPIQPPGPP ERDSVGQLQL YRHPDRSQPA FLDAIDRRED TFYVVSFRRD
     HLLLPAISHN KTSRPKMSLV MPAMAPNETL SGRGAPGDYE EMMQIECEVM DTRVIHIKTS
     TVPPSLRKQP SPTPGNATGG PLPVSAASQA HQASHQPLYL NHP
//