Ficd
entrez
231630
canonical
uniprot
Q8BIX9
canonical
ensembl
ENSMUSG00000053334
resolver
ensp
ENSMUSP00000071719
resolver
ensp
ENSMUSP00000291727
resolver
ensp
ENSMUSP00000291731
resolver
genesymbol
Ficd
resolver
genesymbol_syn
D5Ertd40e
resolver
uniprot
A4QPF9
resolver
uniprot
Q8BIC9
resolver
uniprot
Q8BJ12
resolver
uniprot_entry
FICD_MOUSE
resolver
uniprot_sec
A4QPF9
resolver
uniprot_sec
Q8BIC9
resolver
uniprot_sec
Q8BJ12
resolver
activity_regulation
ACTIVITY REGULATION: The side chain of Glu-234 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place. In response to endoplasmic reticulum stress, mediates de-AMPylase activity (By similarity). Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-234 binds ATP and competes with ATP-binding at Arg-374, thereby preventing adenylyltransferase activity (By similarity). In unstressed cells, disengagement of Glu-234 promotes adenylyltransferase activity (By similarity). Activation dissociates ATP-binding from Glu-234, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q9BVA6}.
uniprot
proteins
amino_acid_sequence
MILMPMASVVAVAEPKWVSVWGRFLWMALLSMALGSLLALLLPLGVVEEHCLAVLRGFHLLRSKLDRAQPVVPKCTSLCTELSVSSRDAGLLTVKTTASPAGKLEAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSVIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTMDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITIRKEQRSEYYHVLEVANEGDVRPFIRFIAKCTEVTLDTLLLATTEYSVALPEAQPNHSGFKETLPVRP
uniprot
proteins
ec_number
2.7.7.108
uniprot
proteins
ec_number
3.1.4.-
uniprot
proteins
function
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (By similarity). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q9BVA6}.
uniprot
proteins
mass_dalton
51754
uniprot
proteins
post_translational_modification
PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}.
uniprot
proteins
protein_family
Fic family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
sequence_length
458
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..44; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins