FICD_HUMAN
ID FICD_HUMAN Reviewed; 458 AA.
AC Q9BVA6; O75406;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein adenylyltransferase FICD {ECO:0000305};
DE EC=2.7.7.n1 {ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:25435325, ECO:0000269|PubMed:25601083};
DE AltName: Full=AMPylator FICD {ECO:0000305};
DE AltName: Full=De-AMPylase FICD {ECO:0000250|UniProtKB:A0A061I403};
DE EC=3.1.4.- {ECO:0000250|UniProtKB:A0A061I403};
DE AltName: Full=FIC domain-containing protein {ECO:0000303|PubMed:25435325};
DE AltName: Full=Huntingtin yeast partner E {ECO:0000303|PubMed:25435325, ECO:0000303|PubMed:9700202};
DE AltName: Full=Huntingtin-interacting protein 13;
DE Short=HIP-13;
DE AltName: Full=Huntingtin-interacting protein E {ECO:0000303|PubMed:25435325, ECO:0000303|PubMed:9700202};
GN Name=FICD {ECO:0000312|HGNC:HGNC:18416};
GN Synonyms=HIP13, HYPE {ECO:0000303|PubMed:25435325,
GN ECO:0000303|PubMed:9700202}; ORFNames=UNQ3041/PRO9857;
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 [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 275-458, AND INTERACTION WITH HD.
RC TISSUE=Frontal cortex;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP HIS-363.
RX PubMed=19362538; DOI=10.1016/j.molcel.2009.03.008;
RA Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A., Mendez J.C.,
RA Zekarias B., Lazar C., Dixon J.E.;
RT "The fic domain: regulation of cell signaling by adenylylation.";
RL Mol. Cell 34:93-103(2009).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-234.
RX PubMed=22266942; DOI=10.1038/nature10729;
RA Engel P., Goepfert A., Stanger F.V., Harms A., Schmidt A., Schirmer T.,
RA Dehio C.;
RT "Adenylylation control by intra- or intermolecular active-site obstruction
RT in Fic proteins.";
RL Nature 482:107-110(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TOPOLOGY,
RP INDUCTION, AMPYLATION AT SER-79; THR-80 AND THR-183, GLYCOSYLATION AT
RP ASN-275 AND ASN-446, AND MUTAGENESIS OF 77-THR-SER-78; 79-SER-THR-80;
RP THR-183; GLU-234; ASN-275; HIS-363 AND ASN-446.
RX PubMed=25601083; DOI=10.1074/jbc.m114.618348;
RA Sanyal A., Chen A.J., Nakayasu E.S., Lazar C.S., Zbornik E.A., Worby C.A.,
RA Koller A., Mattoo S.;
RT "A novel link between Fic (filamentation induced by cAMP)-mediated
RT adenylylation/AMPylation and the unfolded protein response.";
RL J. Biol. Chem. 290:8482-8499(2015).
RN [8] {ECO:0007744|PDB:4U04, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U, ECO:0007744|PDB:4U0Z}
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 102-445 IN COMPLEX WITH ADP AND
RP ATP, FUNCTION, AMPYLATION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY
RP REGULATION, ACTIVE SITE, AND MUTAGENESIS OF THR-168; SER-170; TYR-172;
RP GLU-234 AND LEU-258.
RX PubMed=25435325; DOI=10.1016/j.str.2014.10.007;
RA Bunney T.D., Cole A.R., Broncel M., Esposito D., Tate E.W., Katan M.;
RT "Crystal structure of the human, FIC-domain containing protein HYPE and
RT implications for its functions.";
RL Structure 22:1831-1843(2014).
CC -!- FUNCTION: Protein that can both mediate the addition of adenosine 5'-
CC monophosphate (AMP) to specific residues of target proteins
CC (AMPylation), and the removal of the same modification from target
CC proteins (de-AMPylation), depending on the context (By similarity). The
CC side chain of Glu-231 determines which of the two opposing activities
CC (AMPylase or de-AMPylase) will take place (By similarity). Acts as a
CC key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR)
CC by mediating AMPylation or de-AMPylation of HSPA5/BiP
CC (PubMed:25601083). In unstressed cells, acts as an adenylyltransferase
CC by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating
CC it (By similarity). In response to endoplasmic reticulum stress, acts
CC as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from
CC HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By
CC similarity). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho
CC GTPases in vitro, Rho GTPases do not constitute physiological
CC substrates (PubMed:19362538, PubMed:25601083).
CC {ECO:0000250|UniProtKB:A0A061I403, ECO:0000269|PubMed:22266942,
CC ECO:0000269|PubMed:25435325, ECO:0000269|PubMed:25601083,
CC ECO:0000305|PubMed:19362538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:19362538};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-
CC threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:A0A061I403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:25435325,
CC ECO:0000269|PubMed:25601083};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25601083};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25601083};
CC Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+).
CC {ECO:0000269|PubMed:25601083};
CC -!- ACTIVITY REGULATION: The side chain of Glu-234 determines which of the
CC two opposing activities (AMPylase or de-AMPylase) will take place. In
CC response to endoplasmic reticulum stress, mediates de-AMPylase activity
CC (By similarity). Adenylyltransferase activity is inhibited by the
CC inhibitory helix present at the N-terminus: Glu-234 binds ATP and
CC competes with ATP-binding at Arg-374, thereby preventing
CC adenylyltransferase activity (PubMed:22266942, PubMed:25435325). In
CC unstressed cells, disengagement of Glu-234 promotes adenylyltransferase
CC activity (By similarity). Activation dissociates ATP-binding from Glu-
CC 234, allowing ordered binding of the entire ATP moiety with the alpha-
CC phosphate in an orientation that is productive for accepting an
CC incoming target hydroxyl side chain (PubMed:22266942, PubMed:25435325).
CC {ECO:0000250|UniProtKB:A0A061I403, ECO:0000269|PubMed:22266942,
CC ECO:0000269|PubMed:25435325}.
CC -!- SUBUNIT: Homodimer (PubMed:25435325). Interacts with HD
CC (PubMed:9700202). {ECO:0000269|PubMed:25435325,
CC ECO:0000269|PubMed:9700202}.
CC -!- INTERACTION:
CC Q9BVA6; Q9BVA6: FICD; NbExp=5; IntAct=EBI-3907198, EBI-3907198;
CC Q9BVA6; P42858: HTT; NbExp=3; IntAct=EBI-3907198, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25601083}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:25601083}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19362538}.
CC -!- INDUCTION: Up-regulated in response to activation of unfolded protein
CC response (UPR). {ECO:0000269|PubMed:25601083}.
CC -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC {ECO:0000269|PubMed:19362538}.
CC -!- PTM: Auto-AMPylated in vitro; it is unclear whether auto-AMPylation is
CC relevant in vivo. {ECO:0000269|PubMed:25435325,
CC ECO:0000269|PubMed:25601083}.
CC -!- PTM: N-glycosylated; predominantly glycosylated at Asn-275.
CC {ECO:0000269|PubMed:25601083}.
CC -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to mediate AMPylation of HSPA5/BiP at
CC 'Ser-365' and 'Thr-366' in vitro, leading to activate HSPA5/BiP
CC (PubMed:25601083). However, it was later shown that it mediates
CC AMPylation of HSPA5/BiP at 'Thr-518', leading to inactivate HSPA5/BiP.
CC {ECO:0000250|UniProtKB:A0A061I403, ECO:0000269|PubMed:25601083}.
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DR EMBL; AY358992; AAQ89351.1; -; mRNA.
DR EMBL; CH471054; EAW97813.1; -; Genomic_DNA.
DR EMBL; BC001342; AAH01342.2; -; mRNA.
DR EMBL; AF049611; AAC26847.1; -; mRNA.
DR CCDS; CCDS9116.1; -.
DR RefSeq; NP_009007.2; NM_007076.2.
DR PDB; 4U04; X-ray; 2.48 A; A/B=102-445.
DR PDB; 4U07; X-ray; 2.64 A; A/B=102-445.
DR PDB; 4U0S; X-ray; 2.49 A; A/B=102-445.
DR PDB; 4U0U; X-ray; 2.98 A; A/B=102-445.
DR PDB; 4U0Z; X-ray; 2.95 A; A/B/C/D/E/F/G/H=102-445.
DR PDB; 6I7G; X-ray; 2.70 A; A/B=104-445.
DR PDB; 6I7H; X-ray; 2.25 A; A=104-445.
DR PDB; 6I7I; X-ray; 2.33 A; A=104-445.
DR PDB; 6I7J; X-ray; 2.65 A; A=104-445.
DR PDB; 6I7K; X-ray; 2.54 A; A=104-445.
DR PDB; 6I7L; X-ray; 2.32 A; A=104-445.
DR PDB; 6ZMD; X-ray; 2.64 A; B=102-445.
DR PDB; 7B7Z; X-ray; 1.70 A; A=104-445.
DR PDB; 7B80; X-ray; 1.87 A; A=104-445.
DR PDBsum; 4U04; -.
DR PDBsum; 4U07; -.
DR PDBsum; 4U0S; -.
DR PDBsum; 4U0U; -.
DR PDBsum; 4U0Z; -.
DR PDBsum; 6I7G; -.
DR PDBsum; 6I7H; -.
DR PDBsum; 6I7I; -.
DR PDBsum; 6I7J; -.
DR PDBsum; 6I7K; -.
DR PDBsum; 6I7L; -.
DR PDBsum; 6ZMD; -.
DR PDBsum; 7B7Z; -.
DR PDBsum; 7B80; -.
DR AlphaFoldDB; Q9BVA6; -.
DR SMR; Q9BVA6; -.
DR BioGRID; 116324; 4.
DR DIP; DIP-44884N; -.
DR IntAct; Q9BVA6; 4.
DR STRING; 9606.ENSP00000446479; -.
DR GlyGen; Q9BVA6; 2 sites.
DR iPTMnet; Q9BVA6; -.
DR PhosphoSitePlus; Q9BVA6; -.
DR BioMuta; FICD; -.
DR DMDM; 74761284; -.
DR jPOST; Q9BVA6; -.
DR MassIVE; Q9BVA6; -.
DR PaxDb; Q9BVA6; -.
DR PeptideAtlas; Q9BVA6; -.
DR PRIDE; Q9BVA6; -.
DR ProteomicsDB; 79191; -.
DR Antibodypedia; 18273; 297 antibodies from 25 providers.
DR DNASU; 11153; -.
DR Ensembl; ENST00000552695.6; ENSP00000446479.1; ENSG00000198855.7.
DR GeneID; 11153; -.
DR KEGG; hsa:11153; -.
DR MANE-Select; ENST00000552695.6; ENSP00000446479.1; NM_007076.3; NP_009007.2.
DR UCSC; uc001tmx.2; human.
DR CTD; 11153; -.
DR GeneCards; FICD; -.
DR HGNC; HGNC:18416; FICD.
DR HPA; ENSG00000198855; Low tissue specificity.
DR neXtProt; NX_Q9BVA6; -.
DR OpenTargets; ENSG00000198855; -.
DR PharmGKB; PA162388517; -.
DR VEuPathDB; HostDB:ENSG00000198855; -.
DR eggNOG; KOG3824; Eukaryota.
DR GeneTree; ENSGT00390000008873; -.
DR HOGENOM; CLU_040460_0_0_1; -.
DR InParanoid; Q9BVA6; -.
DR OMA; CTEMTLD; -.
DR OrthoDB; 1057856at2759; -.
DR PhylomeDB; Q9BVA6; -.
DR TreeFam; TF314692; -.
DR PathwayCommons; Q9BVA6; -.
DR SignaLink; Q9BVA6; -.
DR BioGRID-ORCS; 11153; 19 hits in 1082 CRISPR screens.
DR GenomeRNAi; 11153; -.
DR Pharos; Q9BVA6; Tbio.
DR PRO; PR:Q9BVA6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BVA6; protein.
DR Bgee; ENSG00000198855; Expressed in buccal mucosa cell and 149 other tissues.
DR ExpressionAtlas; Q9BVA6; baseline and differential.
DR Genevisible; Q9BVA6; HS.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044603; F:protein adenylylhydrolase activity; ISS:UniProtKB.
DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; TAS:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR GO; GO:0044602; P:protein deadenylylation; ISS:UniProtKB.
DR GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3290.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR040198; Fido_containing.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR13504; PTHR13504; 1.
DR Pfam; PF02661; Fic; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51459; FIDO; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Magnesium; Manganese; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Reference proteome; Repeat; Signal-anchor; TPR repeat;
KW Transferase; Transmembrane; Transmembrane helix; Unfolded protein response.
FT CHAIN 1..458
FT /note="Protein adenylyltransferase FICD"
FT /id="PRO_0000317301"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25601083"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..458
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:25601083"
FT REPEAT 106..139
FT /note="TPR 1"
FT REPEAT 140..173
FT /note="TPR 2"
FT DOMAIN 285..420
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT MOTIF 230..235
FT /note="Inhibitory (S/T)XXXE(G/N) motif"
FT /evidence="ECO:0000269|PubMed:22266942"
FT ACT_SITE 363
FT /evidence="ECO:0000269|PubMed:22266942"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25435325,
FT ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U"
FT BINDING 316..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25435325,
FT ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S,
FT ECO:0007744|PDB:4U0U"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25435325,
FT ECO:0007744|PDB:4U07"
FT BINDING 399..400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25435325,
FT ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S,
FT ECO:0007744|PDB:4U0U"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25435325,
FT ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S,
FT ECO:0007744|PDB:4U0U"
FT SITE 234
FT /note="Important for autoinhibition of adenylyltransferase
FT activity"
FT /evidence="ECO:0000269|PubMed:22266942,
FT ECO:0000269|PubMed:25435325"
FT MOD_RES 79
FT /note="O-AMP-serine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:25601083"
FT MOD_RES 80
FT /note="O-AMP-threonine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:25601083"
FT MOD_RES 183
FT /note="O-AMP-threonine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:25601083"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25601083"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25601083"
FT MUTAGEN 76..77
FT /note="TS->AA: Does not affect auto-AMPylation."
FT /evidence="ECO:0000269|PubMed:25601083"
FT MUTAGEN 79..80
FT /note="ST->AA: Decreased AMPylation."
FT /evidence="ECO:0000269|PubMed:25601083"
FT MUTAGEN 168
FT /note="T->A: Does not affect level of auto-AMPylation."
FT /evidence="ECO:0000269|PubMed:25435325"
FT MUTAGEN 170
FT /note="S->A: Does not affect level of auto-AMPylation."
FT /evidence="ECO:0000269|PubMed:25435325"
FT MUTAGEN 172
FT /note="Y->F: Does not affect level of auto-AMPylation."
FT /evidence="ECO:0000269|PubMed:25435325"
FT MUTAGEN 183
FT /note="T->A: Decreased AMPylation."
FT /evidence="ECO:0000269|PubMed:25601083"
FT MUTAGEN 234
FT /note="E->G: Promotes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22266942,
FT ECO:0000269|PubMed:25435325, ECO:0000269|PubMed:25601083"
FT MUTAGEN 258
FT /note="L->D: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:25435325"
FT MUTAGEN 275
FT /note="N->Q: Strongly decreased N-glycosylation. Abolished
FT N-glycosylation; when associated with Q-446."
FT /evidence="ECO:0000269|PubMed:25601083"
FT MUTAGEN 363
FT /note="H->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:19362538,
FT ECO:0000269|PubMed:25601083"
FT MUTAGEN 446
FT /note="N->Q: Slightly decreased N-glycosylation. Abolished
FT N-glycosylation; when associated with Q-275."
FT /evidence="ECO:0000269|PubMed:25601083"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 174..206
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 214..232
FT /evidence="ECO:0007829|PDB:7B7Z"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:7B7Z"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6I7I"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:7B7Z"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:7B7Z"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:7B7Z"
FT TURN 303..307
FT /evidence="ECO:0007829|PDB:7B7Z"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:7B7Z"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 396..407
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 412..432
FT /evidence="ECO:0007829|PDB:7B7Z"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:6I7G"
SQ SEQUENCE 458 AA; 51778 MW; 8393EAA46D61C48E CRC64;
MMLIPMASVM AVTEPKWVSV WSRFLWVTLL SMVLGSLLAL LLPLGAVEEQ CLAVLKGLYL
LRSKPDRAQH AATKCTSPST ELSITSRGAT LLVAKTKASP AGKLEARAAL NQALEMKRQG
KREKAQKLFM HALKMDPDFV DALTEFGIFS EEDKDIIQAD YLYTRALTIS PYHEKALVNR
DRTLPLVEEI DQRYFSIIDS KVKKVMSIPK GNSALRRVME ETYYHHIYHT VAIEGNTLTL
SEIRHILETR YAVPGKSLEE QNEVIGMHAA MKYINTTLVS RIGSVTISDV LEIHRRVLGY
VDPVEAGRFR TTQVLVGHHI PPHPQDVEKQ MQEFVQWLNS EEAMNLHPVE FAALAHYKLV
YIHPFIDGNG RTSRLLMNLI LMQAGYPPIT IRKEQRSDYY HVLEAANEGD VRPFIRFIAK
CTETTLDTLL FATTEYSVAL PEAQPNHSGF KETLPVKP
