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FICD_DROSE
ID   FICD_DROSE              Reviewed;         492 AA.
AC   B4I1V5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Protein adenylyltransferase Fic;
DE            EC=2.7.7.n1 {ECO:0000250|UniProtKB:Q8SWV6};
DE   AltName: Full=De-AMPylase Fic {ECO:0000305};
DE            EC=3.1.4.- {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6};
GN   ORFNames=GM18629;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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-247 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 unfolded protein response (UPR) by mediating
CC       AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts
CC       as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at
CC       'Thr-518', thereby inactivating it. In response to endoplasmic
CC       reticulum stress, acts as a phosphodiesterase by mediating removal of
CC       ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore
CC       HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403,
CC       ECO:0000250|UniProtKB:Q8SWV6}.
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=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:Q8SWV6};
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:Q8SWV6};
CC   -!- ACTIVITY REGULATION: The side chain of Glu-247 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-247 binds ATP and
CC       competes with ATP-binding at Arg-386, thereby preventing
CC       adenylyltransferase activity (By similarity). In unstressed cells,
CC       disengagement of Glu-247 promotes adenylyltransferase activity (By
CC       similarity). Activation dissociates ATP-binding from Glu-247, 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. {ECO:0000250|UniProtKB:Q8SWV6}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-
CC       pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CC   -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q9BVA6}.
CC   -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR   EMBL; CH480820; EDW54512.1; -; Genomic_DNA.
DR   RefSeq; XP_002038094.1; XM_002038058.1.
DR   AlphaFoldDB; B4I1V5; -.
DR   SMR; B4I1V5; -.
DR   STRING; 7238.B4I1V5; -.
DR   EnsemblMetazoa; FBtr0201614; FBpp0200106; FBgn0173535.
DR   GeneID; 6613624; -.
DR   KEGG; dse:6613624; -.
DR   HOGENOM; CLU_040460_0_0_1; -.
DR   OMA; CTEMTLD; -.
DR   PhylomeDB; B4I1V5; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051087; F:chaperone binding; IEA:EnsemblMetazoa.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:EnsemblMetazoa.
DR   GO; GO:0044603; F:protein adenylylhydrolase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0070733; F:protein adenylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:EnsemblMetazoa.
DR   GO; GO:0051608; P:histamine transport; IEA:EnsemblMetazoa.
DR   GO; GO:0018117; P:protein adenylylation; ISS:UniProtKB.
DR   GO; GO:0044602; P:protein deadenylylation; IEA:EnsemblMetazoa.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblMetazoa.
DR   GO; GO:0007632; P:visual behavior; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Repeat; TPR repeat;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..492
FT                   /note="Protein adenylyltransferase Fic"
FT                   /id="PRO_0000381789"
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          118..151
FT                   /note="TPR 1"
FT   REPEAT          152..186
FT                   /note="TPR 2"
FT   DOMAIN          297..432
FT                   /note="Fido"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           243..248
FT                   /note="Inhibitory (S/T)XXXE(G/N) motif"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000250|UniProtKB:A0A061I403"
FT   BINDING         247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         328..331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         379..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         411..412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         419
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   SITE            247
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
SQ   SEQUENCE   492 AA;  55679 MW;  F4BED83D9946F2F9 CRC64;
     MCTEAEQPSP PAQQQEQGNP PLCKAQNPKP ARLYRLVLLF VAGSLAAWTF HALSSTNLVW
     KLRQLHHLPT AHYLQTRDEF ALYSVEELNA FKEFYDKSVS DSVGASYTEA EQTNIKEALG
     ALRMAQDLYL AGKDDKAARL FEHALALAPR HPEVLLRYGE FLEHNQRNIV LADQYYFQAL
     TISPSNSEAL ANRQRTADVV QSLDERRLES LDSKRDALSA IHESNGALRR AKKEAYFQHI
     YHSVGIEGNT MTLAQTRSIL ETRMAVDGKS IDEHNEILGM DLAMKYINAS LVQKIDITIK
     DILELHRRVL GHVDPIEGGE FRRNQVYVGG HIPPGPGDLA LLMQRFERWL NSEHSSTLHP
     VNYAALAHYK LVHIHPFVDG NGRTSRLLMN TLLMRAGYPP VIIPKQQRSK YYHFLKLANE
     GDIRPFVRFI ADCTEKTLDL YLWATSDLPQ QIPMLIQTES EAGERLAQMQ SPNVAQRSSI
     LEFYESGSGD IP
 
 
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