ID   PARP6_PONAB             Reviewed;         610 AA.
AC   Q5RDU4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
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:0000250|UniProtKB:Q2NL67};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CR857803; CAH90063.1; -; mRNA.
DR   RefSeq; NP_001124986.1; NM_001131514.1.
DR   AlphaFoldDB; Q5RDU4; -.
DR   STRING; 9601.ENSPPYP00000007500; -.
DR   GeneID; 100171860; -.
DR   KEGG; pon:100171860; -.
DR   CTD; 56965; -.
DR   eggNOG; ENOG502QPRC; Eukaryota.
DR   InParanoid; Q5RDU4; -.
DR   OrthoDB; 268345at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
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..610
FT                   /note="Protein mono-ADP-ribosyltransferase PARP6"
FT                   /id="PRO_0000252432"
FT   DOMAIN          374..600
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT   MOD_RES         580
FT                   /note="ADP-ribosyl aspartic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NL67"
SQ   SEQUENCE   610 AA;  69060 MW;  1979ECB34E1E3A08 CRC64;
     MDIKGQFWND DDSEGDNESE EFLYGVQGSC AADLYRHPQL DADIEAVKEI YSENSVSIRE
     YGTIDDVDID LHINISFLDE EVSTAWKVLR TEPIVLRLRF SLSQYLDGPE PSIEVFQPSN
     KEGFGLGLQL KKILGMFTSQ QWKHLSNDFL KTQQEKRHSW LKASGTIKKF RAGLSIFSPI
     PKSPSFPIIQ DSMLKGKLGV PELRVGRLMN RSVSCTMKNP KVEVFGYPPS PQVSGHCKNI
     PTLEYGFLVQ IMKYAEQRIP TLNEYCVVCD EQHVFQNGSM LKPAVCTREL CVFSFYTLGV
     MSGAAEEVAT GAEVVDLLVA 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