PAR12_MOUSE
ID PAR12_MOUSE Reviewed; 711 AA.
AC Q8BZ20; Q0VB94; Q80VL6; Q8K333; Q8R3U2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP12 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9H0J9};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 12;
DE Short=ARTD12;
DE AltName: Full=Poly [ADP-ribose] polymerase 12;
DE Short=PARP-12;
DE AltName: Full=Zinc finger CCCH domain-containing protein 1;
GN Name=Parp12 {ECO:0000312|MGI:MGI:2143990}; Synonyms=Zc3hdc1;
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=Vagina;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {ECO:0000250|UniProtKB:Q9H0J9}.
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:Q9H0J9};
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:Q9H0J9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q9H0J9}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AK036886; BAC29622.1; -; mRNA.
DR EMBL; CH466533; EDL13617.1; -; Genomic_DNA.
DR EMBL; BC120733; AAI20734.1; -; mRNA.
DR EMBL; BC137645; AAI37646.1; -; mRNA.
DR EMBL; BC024579; AAH24579.1; -; mRNA.
DR EMBL; BC028906; AAH28906.1; -; mRNA.
DR EMBL; BC048927; AAH48927.1; -; mRNA.
DR CCDS; CCDS20019.1; -.
DR RefSeq; NP_766481.2; NM_172893.3.
DR AlphaFoldDB; Q8BZ20; -.
DR SMR; Q8BZ20; -.
DR BioGRID; 232556; 6.
DR STRING; 10090.ENSMUSP00000039704; -.
DR iPTMnet; Q8BZ20; -.
DR PhosphoSitePlus; Q8BZ20; -.
DR jPOST; Q8BZ20; -.
DR MaxQB; Q8BZ20; -.
DR PaxDb; Q8BZ20; -.
DR PRIDE; Q8BZ20; -.
DR ProteomicsDB; 287885; -.
DR Antibodypedia; 1226; 99 antibodies from 24 providers.
DR DNASU; 243771; -.
DR Ensembl; ENSMUST00000038398; ENSMUSP00000039704; ENSMUSG00000038507.
DR GeneID; 243771; -.
DR KEGG; mmu:243771; -.
DR UCSC; uc009blg.2; mouse.
DR CTD; 64761; -.
DR MGI; MGI:2143990; Parp12.
DR VEuPathDB; HostDB:ENSMUSG00000038507; -.
DR eggNOG; ENOG502QSC4; Eukaryota.
DR GeneTree; ENSGT00940000154649; -.
DR HOGENOM; CLU_014825_2_1_1; -.
DR InParanoid; Q8BZ20; -.
DR OMA; YSKSDTH; -.
DR OrthoDB; 782733at2759; -.
DR PhylomeDB; Q8BZ20; -.
DR TreeFam; TF338389; -.
DR BioGRID-ORCS; 243771; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Parp12; mouse.
DR PRO; PR:Q8BZ20; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BZ20; protein.
DR Bgee; ENSMUSG00000038507; Expressed in animal zygote and 220 other tissues.
DR Genevisible; Q8BZ20; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR Gene3D; 3.30.720.50; -; 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 Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..711
FT /note="Protein mono-ADP-ribosyltransferase PARP12"
FT /id="PRO_0000211342"
FT DOMAIN 308..371
FT /note="WWE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 374..468
FT /note="WWE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 494..708
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 103..128
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 164..188
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 189..211
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 280..307
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 281..306
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 247..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 484
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0J9"
FT MOD_RES 610
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9H0J9"
FT MOD_RES 621
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9H0J9"
FT CONFLICT 91
FT /note="K -> I (in Ref. 1; BAC29622)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="E -> K (in Ref. 1; BAC29622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 79917 MW; 5172C6602CDDB4B9 CRC64;
MAQAAVAVAE VTQLLCAAGG ALELAELRRR LRTSLGTDAL ERLLRDCGRF VVASRAVVAV
GAGREAAAAA SERLVLAVSS LRLCRAHQGP KPGCTGLCAQ LHLCKFLIYG NCKFLKTGKN
CRNGHNLKTD HNLSVLRTHG VDHLTYTELC QLLLQNDPSL LPDICLHYNK GDGPFGSCSF
QKQCIKLHIC QYFLQGECKF GTSCKRSHEF TNSESLEQLE RLGLSSDLVS RLLSTYRNAY
DIKNKGSALS KVSPSPAGPQ GSSERKDSSG PVSPGTPSQE ESEQICLYHI RKSCSFQEKC
HRVHFHLPYR WQFLDGGKWK DLDNMELIEE AYSNPSKDRI VYTESAAGFH FDNLDFNSMK
FGNTLARRLS TASSVTKPPH FILTTDWIWY WMDEFGSWQE YGRQGSGHPV TTISSSDVER
AYLAFCAPGA DAQAATLKFQ AGKHNYELHF KAFLQKNLVY GTIRKVCRRP KYVSPQDVQM
KQSCNTKLHG PKSIPDYWDP AALPDLGFKK ITLSSSSEEY QKVWNIFNRT LPFYFVQKIE
RIQNMGLWEV YQWQKCQMQK QNGGKEVDER QLFHGTSANF VDAICQQNFD WRVCGLHGTS
YGKGSYFARD AAYSHHYSKS DTHSHMMFLA RVLVGDFVRG STSFVRPPAK EGQSNAFYDS
CVNSMSDPTI FVVFEKHQVY PEYLIQYSTS SKPPASPSIF VALGNLFTSR Q
