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Adenosine monophosphate-protein transferase FICD (EC 2.7.7.n1) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) (Huntingtin-interacting protein E)

 FICD_CRIGR              Reviewed;         455 AA.
A0A061I403; G3HVJ3;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
03-SEP-2014, sequence version 1.
25-APR-2018, entry version 14.
RecName: Full=Adenosine monophosphate-protein transferase FICD {ECO:0000305};
EC=2.7.7.n1 {ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368};
AltName: Full=AMPylator FICD {ECO:0000305};
AltName: Full=De-AMPylase FICD {ECO:0000305};
EC=3.1.4.- {ECO:0000269|PubMed:27918543};
AltName: Full=FIC domain-containing protein {ECO:0000303|PubMed:26673894};
AltName: Full=Huntingtin-interacting protein E {ECO:0000250|UniProtKB:Q9BVA6};
Name=FICD {ECO:0000303|PubMed:26673894};
Synonyms=HYPE {ECO:0000250|UniProtKB:Q9BVA6};
ORFNames=H671_4g11989 {ECO:0000312|EMBL:ERE76236.1},
I79_014982 {ECO:0000312|EMBL:EGW11974.1};
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21804562; DOI=10.1038/nbt.1932;
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
line.";
Nat. Biotechnol. 29:735-741(2011).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=23929341; DOI=10.1038/nbt.2645;
Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B.,
Kofler R., Romand S., Hesse F., Budach W.E., Galosy S., Muller D.,
Noll T., Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A.,
Goesmann A., Helk B., Mott J.E., Puhler A., Borth N.;
"Chinese hamster genome sequenced from sorted chromosomes.";
Nat. Biotechnol. 31:694-695(2013).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-231.
PubMed=26673894; DOI=10.7554/eLife.12621;
Preissler S., Rato C., Chen R., Antrobus R., Ding S., Fearnley I.M.,
Ron D.;
"AMPylation matches BiP activity to client protein load in the
endoplasmic reticulum.";
Elife 4:E12621-E12621(2015).
[4]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=29064368; DOI=10.7554/eLife.29428;
Preissler S., Rohland L., Yan Y., Chen R., Read R.J., Ron D.;
"AMPylation targets the rate-limiting step of BiP's ATPase cycle for
its functional inactivation.";
Elife 6:0-0(2017).
[5]
FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF GLU-231
AND HIS-360.
PubMed=27918543; DOI=10.1038/nsmb.3337;
Preissler S., Rato C., Perera L., Saudek V., Ron D.;
"FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic
reticulum chaperone BiP.";
Nat. Struct. Mol. Biol. 24:23-29(2017).
-!- 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
(PubMed:27918543). The side chain of Glu-231 determines which of
the two opposing activities (AMPylase or de-AMPylase) will take
place (PubMed:27918543). Acts as a key regulator of the ERN1/IRE1-
mediated unfolded protein response (UPR) by mediating AMPylation
or de-AMPylation of HSPA5/BiP (PubMed:27918543). In unstressed
cells, acts as an adenylyltransferase by mediating AMPylation of
HSPA5/BiP at 'Thr-518', thereby inactivating it (PubMed:26673894,
PubMed:29064368, PubMed:27918543). 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 (PubMed:27918543). 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:Q9BVA6, ECO:0000269|PubMed:26673894,
ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368}.
-!- CATALYTIC ACTIVITY: ATP + [protein]-L-tyrosine = diphosphate +
[protein]-O(4)-(5'-adenylyl)-L-tyrosine.
{ECO:0000250|UniProtKB:Q9BVA6}.
-!- CATALYTIC ACTIVITY: [protein]-O(4)-(5'-adenylyl)-L-threonine +
H(2)O = [protein]-L-threonine + AMP.
{ECO:0000269|PubMed:27918543}.
-!- CATALYTIC ACTIVITY: ATP + [protein]-L-threonine = diphosphate +
[protein]-O(4)-(5'-adenylyl)-L-threonine.
{ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543,
ECO:0000269|PubMed:29064368}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9BVA6};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q9BVA6};
Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+).
{ECO:0000250|UniProtKB:Q9BVA6};
-!- ENZYME REGULATION: The side chain of Glu-231 determines which of
the two opposing activities (AMPylase or de-AMPylase) will take
place (PubMed:27918543). In response to endoplasmic reticulum
stress, mediates de-AMPylase activity (PubMed:27918543).
Adenylyltransferase activity is inhibited by the inhibitory helix
present at the N-terminus: Glu-231 binds ATP and competes with
ATP-binding at Arg-371, thereby preventing adenylyltransferase
activity (By similarity). In unstressed cells, disengagement of
Glu-231 promotes adenylyltransferase activity (PubMed:27918543).
Activation dissociates ATP-binding from Glu-231, 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:Q9BVA6, ECO:0000269|PubMed:27918543}.
-!- SUBUNIT: Homodimer. Interacts with HD.
{ECO:0000250|UniProtKB:Q9BVA6}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q9BVA6}.
-!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
{ECO:0000250|UniProtKB:Q9BVA6}.
-!- PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}.
-!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EGW11974.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; KE674650; ERE76236.1; -; Genomic_DNA.
EMBL; JH000777; EGW11974.1; ALT_SEQ; Genomic_DNA.
InParanoid; G3HVJ3; -.
Proteomes; UP000001075; Unassembled WGS sequence.
Proteomes; UP000030759; Unassembled WGS sequence.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
GO; GO:0044603; F:protein adenylylhydrolase activity; IDA:UniProtKB.
GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
GO; GO:0044602; P:protein deadenylylation; IDA:UniProtKB.
GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; IDA:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
Gene3D; 1.10.3290.10; -; 1.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR003812; Fido.
InterPro; IPR036597; Fido-like_dom_sf.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF02661; Fic; 1.
SUPFAM; SSF140931; SSF140931; 1.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS51459; FIDO; 1.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Endoplasmic reticulum; Glycoprotein;
Hydrolase; Magnesium; Manganese; Membrane; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Reference proteome; Repeat;
Signal-anchor; TPR repeat; Transferase; Transmembrane;
Transmembrane helix; Unfolded protein response.
CHAIN 1 455 Adenosine monophosphate-protein
transferase FICD.
/FTId=PRO_0000443449.
TOPO_DOM 1 20 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9BVA6}.
TRANSMEM 21 41 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 42 455 Lumenal. {ECO:0000250|UniProtKB:Q9BVA6}.
REPEAT 103 136 TPR 1. {ECO:0000255|PROSITE-
ProRule:PRU00339}.
REPEAT 137 170 TPR 2. {ECO:0000255|PROSITE-
ProRule:PRU00339}.
DOMAIN 282 417 Fido. {ECO:0000255|PROSITE-
ProRule:PRU00791}.
NP_BIND 313 316 ATP. {ECO:0000250|UniProtKB:Q9BVA6}.
NP_BIND 364 371 ATP. {ECO:0000250|UniProtKB:Q9BVA6}.
NP_BIND 396 397 ATP. {ECO:0000250|UniProtKB:Q9BVA6}.
MOTIF 227 232 Inhibitory (S/T)XXXE(G/N) motif.
{ECO:0000250|UniProtKB:Q9BVA6}.
ACT_SITE 360 360 {ECO:0000269|PubMed:27918543}.
BINDING 231 231 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:Q9BVA6}.
BINDING 404 404 ATP. {ECO:0000250|UniProtKB:Q9BVA6}.
SITE 231 231 Important for autoinhibition of
adenylyltransferase activity.
{ECO:0000250|UniProtKB:Q9BVA6}.
MOD_RES 76 76 O-AMP-serine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9BVA6}.
MOD_RES 77 77 O-AMP-threonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9BVA6}.
MOD_RES 180 180 O-AMP-threonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9BVA6}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 231 231 E->G: Impaired phosphodiesterase
activity. Promotes adenylyltransferase
activity. {ECO:0000269|PubMed:26673894,
ECO:0000269|PubMed:27918543}.
MUTAGEN 360 360 H->A: Abolishes adenylyltransferase and
phosphodiesterase activities.
{ECO:0000269|PubMed:27918543}.
SEQUENCE 455 AA; 51477 MW; 076346720C9EA6EE CRC64;
MPMASVIAVA EPKWISVWGR FLWLTLLSMA LGSLLALLLP LGAVEEQCLA VLRSFHLLRS
KLDRTQHVVT KCTSPSTELS VTSGDVGLLT VKTKTSPAGK LEAKAALNQA LEMKRQGKRE
KAHKLFLHAL KMDPGFVDAL NEFGIFSEEE KDIIQADYLY TRALTISPFH EKALVNRDRT
LPLVEEIDQR YFSIIDSKVK KVMSIPKGSS ALRRVMEETY YHHIYHTVAI EGNTLTLSEI
RHILETRYAV PGKSLEEQNE VIGMHAAMKY INTTLVSRIG SVTIDDMLEI HRRVLGYVDP
VEAGRFRRTQ VLVGHHIPPH PRDVEKQMQE FTQWLNSEDA MNLHPVEFAA LAHYKLVYIH
PFIDGNGRTS RLLMNLILMQ AGYPPITILK EQRSEYYHVL EVANEGDVRP FIRFIAKCTE
VTLDTLLLAT TEYSVALPEA QPNHSGLKET LPVRP


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