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FICD_DROMO
ID   FICD_DROMO              Reviewed;         502 AA.
AC   B4KFW6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=GI11595;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
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-251 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-251 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-251 binds ATP and
CC       competes with ATP-binding at Arg-390, thereby preventing
CC       adenylyltransferase activity (By similarity). In unstressed cells,
CC       disengagement of Glu-251 promotes adenylyltransferase activity (By
CC       similarity). Activation dissociates ATP-binding from Glu-251, 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; CH933807; EDW12092.1; -; Genomic_DNA.
DR   RefSeq; XP_002002650.1; XM_002002614.2.
DR   AlphaFoldDB; B4KFW6; -.
DR   SMR; B4KFW6; -.
DR   STRING; 7230.FBpp0160812; -.
DR   EnsemblMetazoa; FBtr0162320; FBpp0160812; FBgn0134355.
DR   GeneID; 6576662; -.
DR   KEGG; dmo:Dmoj_GI11595; -.
DR   eggNOG; KOG3824; Eukaryota.
DR   HOGENOM; CLU_040460_0_0_1; -.
DR   InParanoid; B4KFW6; -.
DR   OMA; CTEMTLD; -.
DR   OrthoDB; 1057856at2759; -.
DR   PhylomeDB; B4KFW6; -.
DR   Proteomes; UP000009192; 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   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; 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..502
FT                   /note="Protein adenylyltransferase Fic"
FT                   /id="PRO_0000381786"
FT   TRANSMEM        38..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          122..155
FT                   /note="TPR 1"
FT   REPEAT          156..190
FT                   /note="TPR 2"
FT   DOMAIN          301..436
FT                   /note="Fido"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           247..252
FT                   /note="Inhibitory (S/T)XXXE(G/N) motif"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000250|UniProtKB:A0A061I403"
FT   BINDING         251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         332..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         383..390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         415..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         423
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   SITE            251
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
SQ   SEQUENCE   502 AA;  56299 MW;  5B26B110B281BD5F CRC64;
     MAMATGKATE EEQPEQGQQQ QQLQQQQKQT TLQSTYRFAL FFIAGCLAAF GFHALTSSSG
     SLLGWRLRLH HLPTAHYLQT RDEFAVYSVD ELNAFKEFYD KSVSDSVGAS LSEAEETNIK
     EAMGALRLAQ EMYMTGKDDK AARLFEHALA LAPKHPEVLL RYGEFLEHNQ RNIVLADQYY
     FQALSINPSN TEALANRQRT ADVVQLLDER RLSSLDEKRD ALSAIHEANS ALRRAKKEAY
     FQHIYHSVGI EGNTMTLAQT RSVLETRMAV DGKSIDEHNE ILGMDLAMKY INASLVQKLY
     ITLKDILELH RRVLGHVDPI EGGEFRRNQV YVGGHIPPGP GDLAILMQRF EHWLNSEQSN
     SLHPVNYAAL AHYKLVHIHP FVDGNGRTSR LLMNTLLMRA GYPPVIIPKQ QRSQYYHFLK
     LANEGDIRPF VRFIADCTEK TLDLYLWATS DLPQQIPMLI QTESDGNVLA QLQSHTSSPE
     LYESGSGSGA GAGAGSGQKG MP
 
 
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