ID   PARPT_HUMAN             Reviewed;         657 AA.
AC   Q7Z3E1; D3DNK6; Q68CY9; Q86VP4; Q9Y4P7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Protein mono-ADP-ribosyltransferase TIPARP {ECO:0000305};
DE            EC=2.4.2.- {ECO:0000269|PubMed:23275542, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:30373764};
DE   AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 14 {ECO:0000303|PubMed:20106667};
DE            Short=ARTD14 {ECO:0000303|PubMed:20106667};
DE   AltName: Full=Poly [ADP-ribose] polymerase 7 {ECO:0000303|PubMed:20106667};
DE            Short=PARP-7 {ECO:0000303|PubMed:20106667};
DE   AltName: Full=TCDD-inducible poly [ADP-ribose] polymerase {ECO:0000303|PubMed:12851707};
GN   Name=TIPARP {ECO:0000303|PubMed:12851707,
GN   ECO:0000312|HGNC:HGNC:23696};
GN   Synonyms=PARP7 {ECO:0000303|PubMed:20106667};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Endometrial tumor, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-406.
RC   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).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=12851707;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human TIPARP gene within the CCNL
RT   amplicon at human chromosome 3q25.31.";
RL   Int. J. Oncol. 23:541-547(2003).
RN   [5]
RP   NOMENCLATURE.
RX   PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA   Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT   "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL   Trends Biochem. Sci. 35:208-219(2010).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AHR, AND MUTAGENESIS OF
RP   CYS-243; HIS-532; TYR-564 AND ILE-631.
RX   PubMed=23275542; DOI=10.1093/nar/gks1337;
RA   MacPherson L., Tamblyn L., Rajendra S., Bralha F., McPherson J.P.,
RA   Matthews J.;
RT   "2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP,
RT   ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon
RT   receptor transactivation.";
RL   Nucleic Acids Res. 41:1604-1621(2013).
RN   [7]
RP   FUNCTION.
RX   PubMed=25043379; DOI=10.1038/ncomms5426;
RA   Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA   Chang P.;
RT   "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL   Nat. Commun. 5:4426-4426(2014).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   ADP-RIBOSYLATION AT CYS-39, AND MUTAGENESIS OF CYS-39; LYS-41; CYS-243 AND
RP   HIS-532.
RX   PubMed=30373764; DOI=10.1042/bcj20180347;
RA   Gomez A., Bindesboell C., Somisetty V.S., Grimaldi G., Hutin D.,
RA   MacPherson L., Ahmed S., Tamblyn L., Cho T., Nebb H.I., Moen A.,
RA   Anonsen J.H., Grant D.M., Matthews J.;
RT   "Characterization of TCDD-Inducible Poly-ADP-Ribose Polymerase
RT   (TIPARP/ARTD14) Catalytic Activity.";
RL   Biochem. J. 475:3827-3846(2018).
CC   -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC       glutamate, aspartate and cysteine residues on target proteins
CC       (PubMed:23275542, PubMed:25043379, PubMed:30373764). Acts as a negative
CC       regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to
CC       inhibit transcription activator activity of AHR (PubMed:23275542,
CC       PubMed:30373764). {ECO:0000269|PubMed:23275542,
CC       ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:30373764}.
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:0000269|PubMed:30373764};
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:0000269|PubMed:30373764};
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:0000269|PubMed:30373764};
CC   -!- ACTIVITY REGULATION: ADP-ribosyltransferase activity is inhibited by
CC       PJ34; inhibition is however not specific to TIPARP and other PARP-
CC       domain containing proteins are also inhibited by PJ34
CC       (PubMed:30373764). Partially inhibited by KU0058948 (PubMed:30373764).
CC       {ECO:0000269|PubMed:30373764}.
CC   -!- SUBUNIT: Interacts with AHR. {ECO:0000269|PubMed:23275542}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23275542,
CC       ECO:0000269|PubMed:30373764}.
CC   -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:30373764}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR   EMBL; AL080156; CAB45747.2; -; mRNA.
DR   EMBL; BX537965; CAD97929.1; -; mRNA.
DR   EMBL; CR749647; CAH18441.1; -; mRNA.
DR   EMBL; CH471052; EAW78725.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78728.1; -; Genomic_DNA.
DR   EMBL; BC050350; AAH50350.2; -; mRNA.
DR   CCDS; CCDS3177.1; -.
DR   PIR; T12540; T12540.
DR   RefSeq; NP_001171646.1; NM_001184717.1.
DR   RefSeq; NP_001171647.1; NM_001184718.1.
DR   RefSeq; NP_056323.2; NM_015508.4.
DR   AlphaFoldDB; Q7Z3E1; -.
DR   SMR; Q7Z3E1; -.
DR   BioGRID; 117460; 1546.
DR   IntAct; Q7Z3E1; 3.
DR   MINT; Q7Z3E1; -.
DR   STRING; 9606.ENSP00000420612; -.
DR   BindingDB; Q7Z3E1; -.
DR   ChEMBL; CHEMBL2380188; -.
DR   iPTMnet; Q7Z3E1; -.
DR   PhosphoSitePlus; Q7Z3E1; -.
DR   BioMuta; TIPARP; -.
DR   DMDM; 74723283; -.
DR   EPD; Q7Z3E1; -.
DR   MassIVE; Q7Z3E1; -.
DR   PaxDb; 9606-ENSP00000420612; -.
DR   PeptideAtlas; Q7Z3E1; -.
DR   ProteomicsDB; 69039; -.
DR   Antibodypedia; 33637; 97 antibodies from 24 providers.
DR   DNASU; 25976; -.
DR   Ensembl; ENST00000295924.12; ENSP00000295924.7; ENSG00000163659.13.
DR   Ensembl; ENST00000461166.5; ENSP00000420612.1; ENSG00000163659.13.
DR   Ensembl; ENST00000486483.5; ENSP00000418757.1; ENSG00000163659.13.
DR   Ensembl; ENST00000542783.5; ENSP00000438345.1; ENSG00000163659.13.
DR   GeneID; 25976; -.
DR   KEGG; hsa:25976; -.
DR   MANE-Select; ENST00000295924.12; ENSP00000295924.7; NM_015508.5; NP_056323.2.
DR   UCSC; uc003fav.4; human.
DR   AGR; HGNC:23696; -.
DR   CTD; 25976; -.
DR   DisGeNET; 25976; -.
DR   GeneCards; TIPARP; -.
DR   HGNC; HGNC:23696; TIPARP.
DR   HPA; ENSG00000163659; Low tissue specificity.
DR   MIM; 612480; gene.
DR   neXtProt; NX_Q7Z3E1; -.
DR   OpenTargets; ENSG00000163659; -.
DR   PharmGKB; PA134885396; -.
DR   VEuPathDB; HostDB:ENSG00000163659; -.
DR   eggNOG; ENOG502QQXA; Eukaryota.
DR   GeneTree; ENSGT00940000155368; -.
DR   InParanoid; Q7Z3E1; -.
DR   OMA; IEEANCR; -.
DR   OrthoDB; 5490222at2759; -.
DR   PhylomeDB; Q7Z3E1; -.
DR   TreeFam; TF328965; -.
DR   BRENDA; 2.4.2.30; 2681.
DR   PathwayCommons; Q7Z3E1; -.
DR   SignaLink; Q7Z3E1; -.
DR   BioGRID-ORCS; 25976; 195 hits in 1158 CRISPR screens.
DR   ChiTaRS; TIPARP; human.
DR   GeneWiki; TIPARP; -.
DR   GenomeRNAi; 25976; -.
DR   Pharos; Q7Z3E1; Tbio.
DR   PRO; PR:Q7Z3E1; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q7Z3E1; Protein.
DR   Bgee; ENSG00000163659; Expressed in secondary oocyte and 194 other cell types or tissues.
DR   ExpressionAtlas; Q7Z3E1; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
DR   GO; GO:0140803; F:NAD+- protein-cysteine ADP-ribosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
DR   GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR   GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR   GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:Ensembl.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR45740; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR   PANTHER; PTHR45740:SF7; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE TIPARP; 1.
DR   Pfam; PF00644; PARP; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50918; WWE; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   Genevisible; Q7Z3E1; HS.
PE   1: Evidence at protein level;
KW   ADP-ribosylation; Glycosyltransferase; Metal-binding; NAD;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..657
FT                   /note="Protein mono-ADP-ribosyltransferase TIPARP"
FT                   /id="PRO_0000247835"
FT   DOMAIN          332..410
FT                   /note="WWE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT   DOMAIN          449..657
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT   ZN_FING         237..264
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           41..47
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:30373764"
FT   MOD_RES         39
FT                   /note="ADP-ribosylcysteine"
FT                   /evidence="ECO:0000269|PubMed:30373764"
FT   VARIANT         406
FT                   /note="R -> S (in dbSNP:rs17854621)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027155"
FT   MUTAGEN         39
FT                   /note="C->A: Slight reduction of
FT                   auto-mono-ADP-ribosylation."
FT                   /evidence="ECO:0000269|PubMed:23275542,
FT                   ECO:0000269|PubMed:30373764"
FT   MUTAGEN         41
FT                   /note="K->A: Partial relocalization to the cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:30373764"
FT   MUTAGEN         243
FT                   /note="C->A: Relocalization to the cytosol."
FT                   /evidence="ECO:0000269|PubMed:23275542,
FT                   ECO:0000269|PubMed:30373764"
FT   MUTAGEN         532
FT                   /note="H->A: Abolishes ADP-ribosyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:23275542,
FT                   ECO:0000269|PubMed:30373764"
FT   MUTAGEN         564
FT                   /note="Y->A: Abolishes ADP-ribosyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:23275542"
FT   MUTAGEN         631
FT                   /note="I->A: Does not affect ADP-ribosyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:23275542"
FT   CONFLICT        43
FT                   /note="K -> E (in Ref. 1; CAH18441)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        582
FT                   /note="G -> R (in Ref. 1; CAH18441)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        633
FT                   /note="V -> A (in Ref. 1; CAH18441)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   657 AA;  76227 MW;  1E63E311F1B36CEB CRC64;
     MEMETTEPEP DCVVQPPSPP DDFSCQMRLS EKITPLKTCF KKKDQKRLGT GTLRSLRPIL
     NTLLESGSLD GVFRSRNQST DENSLHEPMM KKAMEINSSC PPAENNMSVL IPDRTNVGDQ
     IPEAHPSTEA PERVVPIQDH SFPSETLSGT VADSTPAHFQ TDLLHPVSSD VPTSPDCLDK
     VIDYVPGIFQ ENSFTIQYIL DTSDKLSTEL FQDKSEEASL DLVFELVNQL QYHTHQENGI
     EICMDFLQGT CIYGRDCLKH HTVLPYHWQI KRTTTQKWQS VFNDSQEHLE RFYCNPENDR
     MRMKYGGQEF WADLNAMNVY ETTEFDQLRR LSTPPSSNVN SIYHTVWKFF CRDHFGWREY
     PESVIRLIEE ANSRGLKEVR FMMWNNHYIL HNSFFRREIK RRPLFRSCFI LLPYLQTLGG
     VPTQAPPPLE ATSSSQIICP DGVTSANFYP ETWVYMHPSQ DFIQVPVSAE DKSYRIIYNL
     FHKTVPEFKY RILQILRVQN QFLWEKYKRK KEYMNRKMFG RDRIINERHL FHGTSQDVVD
     GICKHNFDPR VCGKHATMFG QGSYFAKKAS YSHNFSKKSS KGVHFMFLAK VLTGRYTMGS
     HGMRRPPPVN PGSVTSDLYD SCVDNFFEPQ IFVIFNDDQS YPYFVIQYEE VSNTVSI
//