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FICD_RAT
ID   FICD_RAT                Reviewed;         458 AA.
AC   Q6AY47;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Protein adenylyltransferase FICD {ECO:0000305};
DE            EC=2.7.7.n1 {ECO:0000250|UniProtKB:Q9BVA6};
DE   AltName: Full=AMPylator FICD {ECO:0000250|UniProtKB:Q9BVA6};
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:0000250|UniProtKB:Q9BVA6};
GN   Name=Ficd {ECO:0000312|RGD:1359391};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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 (By similarity).
CC       In unstressed cells, acts as an adenylyltransferase by mediating
CC       AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By
CC       similarity). In response to endoplasmic reticulum stress, acts as a
CC       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 (By similarity). {ECO:0000250|UniProtKB:A0A061I403,
CC       ECO:0000250|UniProtKB:Q9BVA6}.
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:0000250|UniProtKB:Q9BVA6};
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:0000250|UniProtKB:Q9BVA6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9BVA6};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9BVA6};
CC       Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+).
CC       {ECO:0000250|UniProtKB:Q9BVA6};
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 (By similarity). In unstressed cells,
CC       disengagement of Glu-234 promotes adenylyltransferase activity (By
CC       similarity). Activation dissociates ATP-binding from Glu-234, allowing
CC       ordered binding of the entire ATP moiety with the alpha-phosphate in an
CC       orientation that is productive for accepting an incoming target
CC       hydroxyl side chain (By similarity). {ECO:0000250|UniProtKB:A0A061I403,
CC       ECO:0000250|UniProtKB:Q9BVA6}.
CC   -!- SUBUNIT: Homodimer. Interacts with HD. {ECO:0000250|UniProtKB:Q9BVA6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q9BVA6}.
CC   -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q9BVA6}.
CC   -!- PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}.
CC   -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR   EMBL; BC079197; AAH79197.1; -; mRNA.
DR   RefSeq; NP_001010946.1; NM_001010946.1.
DR   RefSeq; XP_008767542.1; XM_008769320.2.
DR   RefSeq; XP_008767543.1; XM_008769321.2.
DR   AlphaFoldDB; Q6AY47; -.
DR   SMR; Q6AY47; -.
DR   STRING; 10116.ENSRNOP00000000892; -.
DR   GlyGen; Q6AY47; 1 site.
DR   PaxDb; Q6AY47; -.
DR   GeneID; 288741; -.
DR   KEGG; rno:288741; -.
DR   UCSC; RGD:1359391; rat.
DR   CTD; 11153; -.
DR   RGD; 1359391; Ficd.
DR   VEuPathDB; HostDB:ENSRNOG00000059799; -.
DR   eggNOG; KOG3824; Eukaryota.
DR   HOGENOM; CLU_040460_0_0_1; -.
DR   InParanoid; Q6AY47; -.
DR   OMA; CTEMTLD; -.
DR   OrthoDB; 1057856at2759; -.
DR   PhylomeDB; Q6AY47; -.
DR   TreeFam; TF314692; -.
DR   PRO; PR:Q6AY47; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000059799; Expressed in pancreas and 19 other tissues.
DR   Genevisible; Q6AY47; RN.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0044603; F:protein adenylylhydrolase activity; ISS:UniProtKB.
DR   GO; GO:0070733; F:protein adenylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0018117; P:protein adenylylation; ISS:UniProtKB.
DR   GO; GO:0044602; P:protein deadenylylation; ISS:UniProtKB.
DR   GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS: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   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; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Glycoprotein; Hydrolase; Magnesium;
KW   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_0000317303"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
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:0000250|UniProtKB:Q9BVA6"
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:0000250|UniProtKB:Q9BVA6"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         316..319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         367..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         399..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         407
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   SITE            234
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   MOD_RES         79
FT                   /note="O-AMP-serine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   MOD_RES         80
FT                   /note="O-AMP-threonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   MOD_RES         183
FT                   /note="O-AMP-threonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   458 AA;  51754 MW;  CA59D9A4F7D559F9 CRC64;
     MILMPMASVV AVAEPKWVSV WGRFLWMTLL SMALGSLLAL LLPLGAVEEQ CLAVLRGFHL
     LRSKLDRAQH VVTKCTSPST ELSVTSRDAG LLTVKTKASP AGKLEAKAAL NQALEMKRQG
     KRGKAHKLFL HALKMDPGFV DALNELGIFS EEDKDIIQAD YLYTRALTIS PFHEKALINR
     DRTLPLVEEI DQRYFSVLDS KVRKVMSIPK GSSALRRVME ETYYHHIYHT VAIEGNTLTL
     AEIRHILETR YAVPGKSLEE QNEVIGMHAA MKYINSTLVS RIGSVTIDHM LEIHRRVLGY
     VDPVEAGRFR RTQVLVGHHI PPHPRDVEKQ MQEFTQWLNS EDAMNLHPVE FAALAHYKLV
     YIHPFIDGNG RTSRLLMNLI LMQAGYPPIT IRKEQRSEYY HVLEVANEGD VRPFIRFIAK
     CTEVTLDTLL LATTEYSAAL PEAQPNHSGF KETLPVRP
 
 
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