PAR16_DROME
ID PAR16_DROME Reviewed; 359 AA.
AC A1ZAG4; Q8T910;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein mono-ADP-ribosyltransferase Parp16 {ECO:0000305};
DE Short=PARP-16 {ECO:0000303|PubMed:27874829};
DE EC=2.4.2.- {ECO:0000269|PubMed:27874829};
GN Name=Parp16 {ECO:0000312|FlyBase:FBgn0034129};
GN ORFNames=CG15925 {ECO:0000312|FlyBase:FBgn0034129};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL68047.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ACH92434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACH92434.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-199 AND
RP TYR-221.
RX PubMed=27874829; DOI=10.7554/elife.21475;
RA Aguilera-Gomez A., van Oorschot M.M., Veenendaal T., Rabouille C.;
RT "In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid
RT starvation.";
RL Elife 5:0-0(2016).
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. Required for amino acid
CC starvation-induced mono-ADP-ribosylation and subsequent formation of
CC Sec bodies - which are stress assemblies that promote cell survival by
CC preserving components of the ER exit sites (ERES) during amino-acid
CC starvation. Catalyzes the mono-ADP-ribosylation of Sec16 which is
CC essential for Sec body formation. {ECO:0000269|PubMed:27874829}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27874829}; Single-pass type IV membrane protein
CC {ECO:0000305}. Note=Membrane localization is required for mono-ADP-
CC ribosylation and Sec body formation. {ECO:0000269|PubMed:27874829}.
CC -!- DOMAIN: The lumenal and transmembrane domains are necessary for mono-
CC ADP-ribosylation and Sec body formation. {ECO:0000269|PubMed:27874829}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AE013599; AAF57995.1; -; Genomic_DNA.
DR EMBL; AY075177; AAL68047.1; -; mRNA.
DR EMBL; BT044369; ACH92434.1; -; mRNA.
DR RefSeq; NP_725583.1; NM_166177.3.
DR AlphaFoldDB; A1ZAG4; -.
DR SMR; A1ZAG4; -.
DR IntAct; A1ZAG4; 2.
DR STRING; 7227.FBpp0086303; -.
DR PaxDb; A1ZAG4; -.
DR DNASU; 36841; -.
DR EnsemblMetazoa; FBtr0087159; FBpp0086303; FBgn0034129.
DR GeneID; 36841; -.
DR KEGG; dme:Dmel_CG15925; -.
DR UCSC; CG15925-RA; d. melanogaster.
DR CTD; 54956; -.
DR FlyBase; FBgn0034129; Parp16.
DR VEuPathDB; VectorBase:FBgn0034129; -.
DR eggNOG; ENOG502QPKE; Eukaryota.
DR HOGENOM; CLU_774493_0_0_1; -.
DR InParanoid; A1ZAG4; -.
DR OMA; VFQDNET; -.
DR OrthoDB; 1618442at2759; -.
DR PhylomeDB; A1ZAG4; -.
DR Reactome; R-DME-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 36841; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36841; -.
DR PRO; PR:A1ZAG4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034129; Expressed in testis and 7 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:FlyBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; IBA:GO_Central.
DR InterPro; IPR041400; PARP16_N.
DR Pfam; PF18084; ARTD15_N; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; NAD;
KW Nucleotidyltransferase; Reference proteome; Stress response; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Protein mono-ADP-ribosyltransferase Parp16"
FT /id="PRO_0000438992"
FT TOPO_DOM 1..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..359
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y8"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y8"
FT MUTAGEN 199
FT /note="Y->A: Abolishes Sec body formation."
FT /evidence="ECO:0000269|PubMed:27874829"
FT MUTAGEN 221
FT /note="Y->A: Abolishes mono-ADP-ribosylation and Sec body
FT formation."
FT /evidence="ECO:0000269|PubMed:27874829"
FT CONFLICT 32
FT /note="N -> H (in Ref. 3; AAL68047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40731 MW; 5B63A66120815930 CRC64;
MTLLSGANSV GYPSQMPAKR ISWRRLVALL PNSIGLSLKP VTPHLRDLHL VQRRLQDDFL
GCEALWTIFM AAAWSYRYRT RLRPFPSHWN TIDLVFNTLG DAPRLEVLQQ QLMHCDYQAC
SPNVVRLLTD ILVDQADRVS LSSLRPCEFQ ELYAHLGMSP PKQPPTQIFE VRTGKGNEKG
EAYASLRQEN KESVRLGFYG CKLEKVYALL NSQNSLDNGK YLELTCDINE ALARSKPQAG
VGGSRCGSIL RCVAVVEFVF QDNETSRDKK QVIIKDANTM QVSYLLLYGQ SCNEYAMERQ
IKLMAEPARE LLNWLERYHK KAISLGVGLL IVSSMAHFGS TFFRLLARTG FYVFKRGIL
