PARP6_MOUSE
ID PARP6_MOUSE Reviewed; 630 AA.
AC Q6P6P7; Q8BVW1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP6 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q2NL67};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 17;
DE Short=ARTD17;
DE AltName: Full=Poly [ADP-ribose] polymerase 6;
DE Short=PARP-6;
GN Name=Parp6 {ECO:0000312|MGI:MGI:1914537};
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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:Q2NL67}.
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:Q2NL67};
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:Q2NL67};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P6P7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P6P7-2; Sequence=VSP_020967, VSP_020968, VSP_020969;
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q2NL67}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AK076321; BAC36299.1; -; mRNA.
DR EMBL; BC062096; AAH62096.1; -; mRNA.
DR CCDS; CCDS57680.1; -. [Q6P6P7-1]
DR RefSeq; NP_001192168.1; NM_001205239.1.
DR AlphaFoldDB; Q6P6P7; -.
DR SMR; Q6P6P7; -.
DR BioGRID; 212075; 2.
DR STRING; 10090.ENSMUSP00000026267; -.
DR PhosphoSitePlus; Q6P6P7; -.
DR PaxDb; Q6P6P7; -.
DR PRIDE; Q6P6P7; -.
DR ProteomicsDB; 287956; -. [Q6P6P7-1]
DR ProteomicsDB; 287957; -. [Q6P6P7-2]
DR GeneID; 67287; -.
DR KEGG; mmu:67287; -.
DR CTD; 56965; -.
DR MGI; MGI:1914537; Parp6.
DR eggNOG; ENOG502QPRC; Eukaryota.
DR InParanoid; Q6P6P7; -.
DR OrthoDB; 268345at2759; -.
DR PhylomeDB; Q6P6P7; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 67287; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Parp6; mouse.
DR PRO; PR:Q6P6P7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6P6P7; protein.
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:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
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; Alternative splicing; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..630
FT /note="Protein mono-ADP-ribosyltransferase PARP6"
FT /id="PRO_0000252431"
FT DOMAIN 394..620
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT MOD_RES 237
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q2NL67"
FT MOD_RES 600
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:Q2NL67"
FT VAR_SEQ 233..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020967"
FT VAR_SEQ 498..518
FT /note="LHGAAYGKGIYLSPISSISFG -> EWAKDSTGCLPRMSWSRDTTG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020968"
FT VAR_SEQ 519..630
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020969"
FT CONFLICT 338
FT /note="Q -> L (in Ref. 1; BAC36299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 71176 MW; 10DEFC627655063A CRC64;
MDIKGQFWND DDSEGDNESE EFLYGVQGSC AADLYRHPQL DADIEAVKEI YSENSVSIRE
YGTIDDVDLD LHINISFLDE EVSTAWKVLR TEPIVLRLRF SLSQYLDGPE PSIEVFQPSN
KEGFGLGLQL KKILCMFTSQ QWKHLSNDFL KTQQEKRHSW FKASGTIKKF RAGLSIFSPI
PKSPSFPIIQ DSMLKGKLGV PELRVGRLMN RSISCTMKNP KVEVFGYPPS PQAGLLCPQH
VGLPPPARTS PLVSGHCKNI PTLEYGFLVQ IMKYAEQRIP TLNEYCVVCD EQHVFQNGSM
LKPAVCTREL CVFSFYTLGV MSGAAEEVAT GAEVVDLQVA MCRAALESPR KSIIFEPYPS
VVDPTDPKTL AFNPKKKNYE RLQKALDSVM SIREMTQGSY LEIKKQMDKL DPLAHPLLQW
IISSNRSHIV KLPLSRLKFM HTSHQFLLLS SPPAKEARFR TAKKLYGSTF AFHGSHIENW
HSILRNGLVN ASYTKLQLHG AAYGKGIYLS PISSISFGYS GMGKGQHRMP SKDELVQRYN
RMNTIPQTRS IQSRFLQSRN LNCIALCEVI TSKDLQKHGN IWVCPVSDHV CTRFFFVYED
GQVGDANINT QDPKIQKEIM RVIGTQVYTN
