PARP8_MOUSE
ID PARP8_MOUSE Reviewed; 852 AA.
AC Q3UD82; Q3UDE4; Q3UDU5; Q8VCB5; Q9CYY3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP8 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q8N3A8};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 16 {ECO:0000250|UniProtKB:Q8N3A8};
DE Short=ARTD16 {ECO:0000250|UniProtKB:Q8N3A8};
DE AltName: Full=Poly [ADP-ribose] polymerase 8 {ECO:0000250|UniProtKB:Q8N3A8};
DE Short=PARP-8 {ECO:0000250|UniProtKB:Q8N3A8};
GN Name=Parp8 {ECO:0000312|MGI:MGI:1098713};
GN Synonyms=D13Ertd275e {ECO:0000312|MGI:MGI:1098713};
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=Bone marrow, and Embryo;
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).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {ECO:0000250|UniProtKB:Q8N3A8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-
CC D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:140607; Evidence={ECO:0000250|UniProtKB:Q8N3A8};
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q8N3A8}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH21881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK013206; BAB28711.2; -; mRNA.
DR EMBL; AK149918; BAE29166.1; -; mRNA.
DR EMBL; AK150113; BAE29317.1; -; mRNA.
DR EMBL; AK150208; BAE29379.1; -; mRNA.
DR EMBL; BC021315; AAH21315.1; ALT_INIT; mRNA.
DR EMBL; BC021881; AAH21881.1; ALT_INIT; mRNA.
DR CCDS; CCDS36790.2; -.
DR RefSeq; NP_001074478.1; NM_001081009.1.
DR AlphaFoldDB; Q3UD82; -.
DR STRING; 10090.ENSMUSP00000022239; -.
DR iPTMnet; Q3UD82; -.
DR PhosphoSitePlus; Q3UD82; -.
DR PaxDb; Q3UD82; -.
DR PRIDE; Q3UD82; -.
DR ProteomicsDB; 287958; -.
DR Antibodypedia; 23287; 133 antibodies from 22 providers.
DR Ensembl; ENSMUST00000223949; ENSMUSP00000152911; ENSMUSG00000021725.
DR GeneID; 52552; -.
DR KEGG; mmu:52552; -.
DR UCSC; uc007ryi.1; mouse.
DR CTD; 79668; -.
DR MGI; MGI:1098713; Parp8.
DR VEuPathDB; HostDB:ENSMUSG00000021725; -.
DR eggNOG; ENOG502QPRC; Eukaryota.
DR GeneTree; ENSGT00950000183129; -.
DR InParanoid; Q3UD82; -.
DR OMA; AKCVPIR; -.
DR PhylomeDB; Q3UD82; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR ChiTaRS; Parp8; mouse.
DR PRO; PR:Q3UD82; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UD82; protein.
DR Bgee; ENSMUSG00000021725; Expressed in morula and 259 other tissues.
DR ExpressionAtlas; Q3UD82; baseline and differential.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR Pfam; PF00644; PARP; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Glycosyltransferase; NAD; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..852
FT /note="Protein mono-ADP-ribosyltransferase PARP8"
FT /id="PRO_0000252434"
FT DOMAIN 615..842
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3A8"
FT MOD_RES 366
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3A8"
FT MOD_RES 375
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3A8"
FT MOD_RES 394
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3A8"
FT CONFLICT 143
FT /note="N -> D (in Ref. 1; BAE29166)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="D -> E (in Ref. 2; AAH21881)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="P -> L (in Ref. 1; BAB28711)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="N -> S (in Ref. 1; BAE29166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 95560 MW; 32184686DE3A27A8 CRC64;
MGMCSRQERI QKDIDVVIQK SRAEKDCLFA DFRYSDSTFT FTYVGGPKSV SYSVHVSEDY
PDNTYVSSSE NDEDVLVTTD PIPVIFHRIA TELRKTNDIN CCLSIRSKLQ KENGEESRQN
STVEEDSEGD NDSEEFYYGG QVNYDGELHK HPQLEADLSA VRELYGPHAV SLREYGAIDD
VDIDLHIDVS FLDEEIAVAW EVIRTEPIIV RLHCSLTQYL NGPVPTVDVF QISTKERFGL
GHQLKKIMQT FVSQQWKQSK DKSNCPHGKK LSEKKVKSPL HLFSTLRRSP SYPPPGCGKS
KSKLKPEQDG ISKTHKLLRR TCSSTVKADD MCAKSHRTFG RSLSSDPRAE QAMSTIKSHK
LLGRPCPSAG KQEDCLTLKS HKLLTRSCSG DPRCEHNTNL KPHKLLSRSY SSNLRMEELY
GLKNHKLLSK SYSSAPKTSK MEHFKEPNAE GRRLSLTSGL IGILTPSSSS SQPPTNGAKS
IPIRDRGFLV QTIEFAEQRI PVLNEYCVVC DEPHVFQNGP MLRPTVCERE LCVFAFQTLG
VMNEAADEIA TGAQVVDLLV SMCRSALESP RKVVIFEPYP SVVDPNDPQM LAFNPRKKNY
DRVMKALDSI TSIREMTQAP YLEIKKQMDK QDPLAHPLLQ WVISSNRSHI VKLPVNRQLK
FMHTPHQFLL LSSPPAKESN FRAAKKLFGS TFAFHGSHIE NWHSILRNGL VVASNTRLQL
HGAMYGSGIY LSPMSSISFG YSGMNKKQKV SSKDEPASSS KSSNASQSQK KGQQSQFLQS
RNLKCIALCE VITSPDLHKH GEIWVVPNTD HVCTRFFFVY EDGQVGDANI NTQEGGIHKE
ILRVIGNQTA TG
