PAR16_RAT
ID PAR16_RAT Reviewed; 322 AA.
AC Q5U2Q4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP16 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q8N5Y8};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 15 {ECO:0000250|UniProtKB:Q8N5Y8};
DE AltName: Full=Poly [ADP-ribose] polymerase 16 {ECO:0000250|UniProtKB:Q8N5Y8};
DE Short=PARP-16 {ECO:0000250|UniProtKB:Q8N5Y8};
GN Name=Parp16 {ECO:0000312|RGD:1306243};
GN Synonyms=Artd15 {ECO:0000312|RGD:1306243};
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=Lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Intracellular mono-ADP-ribosyltransferase that may play a
CC role in different processes through the mono-ADP-ribosylation of
CC proteins involved in those processes. May play a role in the unfolded
CC protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and
CC ERN1, two important UPR effectors. May also mediate mono-ADP-
CC ribosylation of karyopherin KPNB1 a nuclear import factor. May not
CC modify proteins on arginine or cysteine residues compared to other
CC mono-ADP-ribosyltransferases. {ECO:0000250|UniProtKB:Q8N5Y8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Y8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-
CC lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:Q8N5Y8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Y8};
CC -!- SUBUNIT: Interacts with KPNB1. {ECO:0000250|UniProtKB:Q8N5Y8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N5Y8}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q8N5Y8}.
CC -!- DOMAIN: The N-terminal PARP alpha-helical domain is regulatory, it
CC packs against the catalytic domain, and may relay effector-binding
CC event to the NAD-binding site. {ECO:0000250}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q8N5Y8}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; BC085908; AAH85908.1; -; mRNA.
DR RefSeq; NP_001014115.1; NM_001014093.1.
DR RefSeq; XP_006243320.1; XM_006243258.3.
DR AlphaFoldDB; Q5U2Q4; -.
DR SMR; Q5U2Q4; -.
DR STRING; 10116.ENSRNOP00000043841; -.
DR PaxDb; Q5U2Q4; -.
DR PRIDE; Q5U2Q4; -.
DR GeneID; 315760; -.
DR KEGG; rno:315760; -.
DR UCSC; RGD:1306243; rat.
DR CTD; 54956; -.
DR RGD; 1306243; Parp16.
DR eggNOG; ENOG502QPKE; Eukaryota.
DR InParanoid; Q5U2Q4; -.
DR OrthoDB; 1618442at2759; -.
DR Reactome; R-RNO-197264; Nicotinamide salvaging.
DR PRO; PR:Q5U2Q4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:RGD.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:RGD.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR InterPro; IPR041400; PARP16_N.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR Pfam; PF18084; ARTD15_N; 1.
DR Pfam; PF00644; PARP; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW NAD; Nucleotidyltransferase; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Unfolded protein response.
FT CHAIN 1..322
FT /note="Protein mono-ADP-ribosyltransferase PARP16"
FT /id="PRO_0000252439"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..91
FT /note="PARP alpha-helical"
FT DOMAIN 77..280
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y8"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y8"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y8"
FT SITE 193
FT /note="Nicotinamide-stacking aromate"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y8"
SQ SEQUENCE 322 AA; 36712 MW; 9D45121DB8D093CF CRC64;
MQLSNRAAAR ESVSRDVLAA DLRCSLFASA LQSYKRDSVL RPFPASYARH DCKDFEALLA
DTGRLPNLKE LLQSSRDTDK QTWDLVSWIL SSKILTIHSA EKAEFEKIQQ LTGAPHTPVP
IPDFLFEIEY FDPANARFYE TKGGRDLIYA FHGSRLENFH SIIHNGLHCH LNKTSLFGEG
TYLTSDLSLA LIYSPHGRGW QHSLLGQTLS CVAVCEVIDH PDVKCQTKKK DSKEIDRSRA
RIKHSEGGDV PPKYFVVTNN QLLRVKYLLV YSQKQPKRAS SQLSWLCSHW FMVAMSLYLL
LLLIVSVTNS SAFQHFWNRL KR
