PARPT_MOUSE
ID PARPT_MOUSE Reviewed; 657 AA.
AC Q8C1B2; Q3UD50; Q8C032;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein mono-ADP-ribosyltransferase TIPARP {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:23275542};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 14;
DE Short=ARTD14;
DE AltName: Full=TCDD-inducible poly [ADP-ribose] polymerase {ECO:0000303|PubMed:11716501};
GN Name=Tiparp {ECO:0000303|PubMed:11716501, ECO:0000312|MGI:MGI:2159210};
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 [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11716501; DOI=10.1006/bbrc.2001.5987;
RA Ma Q., Baldwin K.T., Renzelli A.J., McDaniel A., Dong L.;
RT "TCDD-inducible poly(ADP-ribose) polymerase: a novel response to 2,3,7,8-
RT tetrachlorodibenzo-p-dioxin.";
RL Biochem. Biophys. Res. Commun. 289:499-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Olfactory bulb, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 INDUCTION.
RX PubMed=12147270; DOI=10.1016/s0003-9861(02)00339-9;
RA Ma Q.;
RT "Induction and superinduction of 2,3,7,8-tetrachlorodibenzo-rho-dioxin-
RT inducible poly(ADP-ribose) polymerase: role of the aryl hydrocarbon
RT receptor/aryl hydrocarbon receptor nuclear translocator transcription
RT activation domains and a labile transcription repressor.";
RL Arch. Biochem. Biophys. 404:309-316(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC glutamate, aspartate and cysteine residues on target proteins (By
CC similarity). Acts as a negative regulator of AHR by mediating mono-ADP-
CC ribosylation of AHR, leading to inhibit transcription activator
CC activity of AHR (Probable). {ECO:0000250|UniProtKB:Q7Z3E1,
CC ECO:0000305|PubMed:23275542}.
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:Q7Z3E1};
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:Q7Z3E1};
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:Q7Z3E1};
CC -!- SUBUNIT: Interacts with AHR. {ECO:0000250|UniProtKB:Q7Z3E1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23275542}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11716501}.
CC -!- INDUCTION: By 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), which is a
CC by-product of industrial processes and an important environmental
CC contaminant (PubMed:11716501, PubMed:12147270). This induction is
CC concentration and time-dependent and is mediated through an aryl
CC hydrocarbon receptor (AhR) and aryl hydrocarbon receptor nuclear
CC translocation (Arnt) signal transduction (PubMed:11716501,
CC PubMed:12147270). Superinduced by cycloheximide and by inhibitors of
CC the 26S proteasome (PubMed:11716501, PubMed:12147270).
CC {ECO:0000269|PubMed:11716501, ECO:0000269|PubMed:12147270}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q7Z3E1}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AK028529; BAC25994.1; -; mRNA.
DR EMBL; AK032453; BAC27876.1; -; mRNA.
DR EMBL; AK150248; BAE29412.1; -; mRNA.
DR EMBL; AK162094; BAE36720.1; -; mRNA.
DR EMBL; BC068173; AAH68173.1; -; mRNA.
DR CCDS; CCDS17388.1; -.
DR RefSeq; NP_849223.2; NM_178892.5.
DR AlphaFoldDB; Q8C1B2; -.
DR SMR; Q8C1B2; -.
DR STRING; 10090.ENSMUSP00000048051; -.
DR iPTMnet; Q8C1B2; -.
DR PhosphoSitePlus; Q8C1B2; -.
DR PaxDb; Q8C1B2; -.
DR PRIDE; Q8C1B2; -.
DR ProteomicsDB; 294330; -.
DR Antibodypedia; 33637; 91 antibodies from 24 providers.
DR Ensembl; ENSMUST00000047906; ENSMUSP00000048051; ENSMUSG00000034640.
DR GeneID; 99929; -.
DR KEGG; mmu:99929; -.
DR UCSC; uc008pkr.1; mouse.
DR CTD; 25976; -.
DR MGI; MGI:2159210; Tiparp.
DR VEuPathDB; HostDB:ENSMUSG00000034640; -.
DR eggNOG; ENOG502QQXA; Eukaryota.
DR GeneTree; ENSGT00940000155368; -.
DR HOGENOM; CLU_014825_0_1_1; -.
DR InParanoid; Q8C1B2; -.
DR OMA; SKKMTGL; -.
DR OrthoDB; 782733at2759; -.
DR PhylomeDB; Q8C1B2; -.
DR TreeFam; TF328965; -.
DR BioGRID-ORCS; 99929; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Tiparp; mouse.
DR PRO; PR:Q8C1B2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C1B2; protein.
DR Bgee; ENSMUSG00000034640; Expressed in animal zygote and 253 other tissues.
DR ExpressionAtlas; Q8C1B2; baseline and differential.
DR Genevisible; Q8C1B2; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO: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:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0008585; P:female gonad development; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
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 Pfam; PF00644; PARP; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript 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_0000247836"
FT DOMAIN 333..411
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 238..265
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..48
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3E1"
FT MOD_RES 39
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3E1"
FT CONFLICT 521
FT /note="R -> H (in Ref. 2; BAC27876)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="D -> N (in Ref. 2; BAC27876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 75901 MW; 332CB9721C7EBC33 CRC64;
MEVETTEPEP DCVVQPPSPS DDFSCQMRIS EKISPLKTCF KKKQEQKRLG TGTLRSLRPI
LNTLLESGSL DGVFRARDQN RDESSLHEHI VKKPLEINPS CPPAENSMPV LIPDGTNVEG
QLPEAHPSTD APEQGVPIQD HSFPPETISG TVADSTTGHF QTDLLHPVSG DVPTSPDCVD
KVMDYVPGAF QDNSFTIQYI LDTSDKLSTE LFQDKSEEAS LELVFELVNQ LQYHTHQENG
IEICMDFLQG TCIYGRDCLK HHTVLPYHWQ IKRTTTQKWQ SVSNDSQEHL ERFYCNPEND
RMRMKYGGQD FWADLNAMTV FETTEFDQLR RLSTPPCSNS NSIYHTFWKF FCRDHFGWRE
YPESVVRLIE EANSRGLKEV RFMMWNNHYI LHNSFFRREI KRRPLFRSCF ILIPYLQTLG
GVPTQASLPL EATSSQIICP DGVTSANFYP ETWVYMHPSQ DFIQVPVSAE DKSYRIIYNL
FHKTVPEFKY RILQILRVQN QFLWEKYKRK KEYMNRKMSG RDRIINERHL FHGTSQDVVD
GICKHNFDPR VCGKHATMFG QGSYFAKKAS YSHNFSKKSS KGVHFMFLAK VLTGRYTMGS
HGMRRPPPVN PGSVTSDLYD SCVDNFFEPQ IFVIFNDDQS YPYFVIQYEE VSNTVSI
