位置:首页 > 蛋白库 > FICD_DROGR
FICD_DROGR
ID   FICD_DROGR              Reviewed;         483 AA.
AC   B4JBN5;
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=GH10751;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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-236 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-236 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-236 binds ATP and
CC       competes with ATP-binding at Arg-375, thereby preventing
CC       adenylyltransferase activity (By similarity). In unstressed cells,
CC       disengagement of Glu-236 promotes adenylyltransferase activity (By
CC       similarity). Activation dissociates ATP-binding from Glu-236, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH916368; EDW02970.1; -; Genomic_DNA.
DR   RefSeq; XP_001988103.1; XM_001988067.1.
DR   AlphaFoldDB; B4JBN5; -.
DR   SMR; B4JBN5; -.
DR   STRING; 7222.FBpp0144657; -.
DR   EnsemblMetazoa; FBtr0146165; FBpp0144657; FBgn0118232.
DR   EnsemblMetazoa; FBtr0453775; FBpp0404414; FBgn0118232.
DR   GeneID; 6562043; -.
DR   KEGG; dgr:6562043; -.
DR   eggNOG; KOG3824; Eukaryota.
DR   HOGENOM; CLU_040460_0_0_1; -.
DR   InParanoid; B4JBN5; -.
DR   OMA; CTEMTLD; -.
DR   OrthoDB; 1057856at2759; -.
DR   PhylomeDB; B4JBN5; -.
DR   Proteomes; UP000001070; 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..483
FT                   /note="Protein adenylyltransferase Fic"
FT                   /id="PRO_0000381784"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          107..140
FT                   /note="TPR 1"
FT   REPEAT          141..175
FT                   /note="TPR 2"
FT   DOMAIN          286..421
FT                   /note="Fido"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT   REGION          464..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           232..237
FT                   /note="Inhibitory (S/T)XXXE(G/N) motif"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000250|UniProtKB:A0A061I403"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         317..320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         368..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         400..401
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   BINDING         408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT   SITE            236
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVA6"
SQ   SEQUENCE   483 AA;  54540 MW;  B1D013EA8CD2885E CRC64;
     METGKVTQEP KQMKFTYRFA FFFIAGSLAT FVFHALTSSS SVSLFGWRLQ LRQLHHLPTA
     HYLQTRDEFA VYSVDELNAF KEFYDKSVSD SVGASYTEAE QTNIKEALGA MRLALDMHIS
     GKDDKAARLF EHALALAPKH PEVLLRYGEF LEHNQRNIVL ADQYYFQALS ISPSNSEAFA
     NRQRTANVVQ TLDERRLVSL DEKRDALSAI HEANAALRRA KKEAYFQHIY HSVGIEGNTM
     TLAQTRSVLE TRMAVDGKSI DEHNEILGMD LAMKYINASL VQKLEITLKD ILELHRRVLG
     HVDPIEGGEF RRTQVYVGGH VPPGPGDLAL LMQRFEHWLN SEQSNSLHPV NYAALAHYKL
     VHIHPFIDGN GRTSRLLMNT LLMRAGYPPV IIPKQQRSQY YHFLKLANEG DIRPFVRFIA
     DCTEKTLDLY LWATSDLPQQ IPMLIQTESE GGVLAQLQSH IAQSAPEPYE SGSGLDSGVN
     GMP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024