ATF6B_HUMAN
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 03-AUG-2022, entry version 205.
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; 71.
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 GlyGen; Q99941; 6 sites, 1 O-linked glycan (1 site).
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; Q99941; -.
DR PeptideAtlas; Q99941; -.
DR PRIDE; Q99941; -.
DR ProteomicsDB; 78531; -. [Q99941-1]
DR ProteomicsDB; 78532; -. [Q99941-2]
DR Antibodypedia; 49313; 226 antibodies from 32 providers.
DR Antibodypedia; 7841; 6 antibodies from 2 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 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 PhylomeDB; Q99941; -.
DR TreeFam; TF316079; -.
DR PathwayCommons; Q99941; -.
DR SignaLink; Q99941; -.
DR SIGNOR; Q99941; -.
DR BioGRID-ORCS; 1388; 22 hits in 1104 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 Genevisible; Q99941; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL.
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:0035497; F:cAMP response element binding; IEA:InterPro.
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:NTNU_SB.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR029809; ATF6B.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46164:SF2; PTHR46164:SF2; 2.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
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
