PAR16_MOUSE
ID PAR16_MOUSE Reviewed; 322 AA.
AC Q7TMM8; Q3V031; Q8CC71;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
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|MGI:MGI:2446133};
GN Synonyms=Artd15 {ECO:0000250|UniProtKB:Q8N5Y8};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Epididymis, Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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|UniProtKB:Q8N5Y8}.
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; AK033791; BAC28475.1; -; mRNA.
DR EMBL; AK133475; BAE21674.1; -; mRNA.
DR EMBL; BC055447; AAH55447.1; -; mRNA.
DR CCDS; CCDS23286.1; -.
DR RefSeq; NP_803411.3; NM_177460.4.
DR AlphaFoldDB; Q7TMM8; -.
DR SMR; Q7TMM8; -.
DR IntAct; Q7TMM8; 1.
DR STRING; 10090.ENSMUSP00000070098; -.
DR PhosphoSitePlus; Q7TMM8; -.
DR MaxQB; Q7TMM8; -.
DR PaxDb; Q7TMM8; -.
DR PRIDE; Q7TMM8; -.
DR ProteomicsDB; 294386; -.
DR Antibodypedia; 25928; 170 antibodies from 25 providers.
DR DNASU; 214424; -.
DR Ensembl; ENSMUST00000069000; ENSMUSP00000070098; ENSMUSG00000032392.
DR Ensembl; ENSMUST00000213396; ENSMUSP00000150318; ENSMUSG00000032392.
DR Ensembl; ENSMUST00000216702; ENSMUSP00000149927; ENSMUSG00000032392.
DR GeneID; 214424; -.
DR KEGG; mmu:214424; -.
DR UCSC; uc009qcx.2; mouse.
DR CTD; 54956; -.
DR MGI; MGI:2446133; Parp16.
DR VEuPathDB; HostDB:ENSMUSG00000032392; -.
DR eggNOG; ENOG502QPKE; Eukaryota.
DR GeneTree; ENSGT00950000183129; -.
DR HOGENOM; CLU_053263_1_0_1; -.
DR InParanoid; Q7TMM8; -.
DR OMA; NSPAFLY; -.
DR OrthoDB; 1618442at2759; -.
DR PhylomeDB; Q7TMM8; -.
DR TreeFam; TF323413; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 214424; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Parp16; mouse.
DR PRO; PR:Q7TMM8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q7TMM8; protein.
DR Bgee; ENSMUSG00000032392; Expressed in saccule of membranous labyrinth and 193 other tissues.
DR ExpressionAtlas; Q7TMM8; baseline and differential.
DR Genevisible; Q7TMM8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:MGI.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
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 1: Evidence at protein 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_0000252438"
FT TOPO_DOM 1..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..322
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 5..91
FT /note="PARP alpha-helical"
FT DOMAIN 94..279
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"
FT CONFLICT 25
FT /note="S -> N (in Ref. 1; BAC28475)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="H -> Q (in Ref. 1; BAC28475)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="V -> A (in Ref. 2; AAH55447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 36764 MW; CA90D8E628AD1874 CRC64;
MQLSNRAAAR EAASRDVLAA DLRCSLFASA LQSYKRDSVL RPFPASYARH DCKDFEALLA
DTGRLPNLKE LLQSSRDTDK QAWDLVSWIL SSKILTIHSA KKAEFEKIQQ LTGAPHTPVP
TPDFLFEIEY FDPANSRFYE TKGERDLIYA FHGSRLENFH SIIHNGLHCH LNKTSLFGEG
TYLTSDLSLA LIYSPHGHGW QHSLLGPILS CVAVCEVIDH PDVKCQIKKK DSKEIDRSRA
RIKHSEGGEI PPKYFVVTNN QLLRVKYLLV YSQKQPKRAS SQLSWLSSHW FVIMMSLYLL
LLLIVSVTNS SVFHHFWNRV KR
