PAR11_MOUSE
ID PAR11_MOUSE Reviewed; 331 AA.
AC Q8CFF0; Q3UAF2; Q3UZR7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP11 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9NR21};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 11;
DE Short=ARTD11;
DE AltName: Full=Poly [ADP-ribose] polymerase 11;
DE Short=PARP-11;
GN Name=Parp11 {ECO:0000312|MGI:MGI:2141505};
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] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pituitary;
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 TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25673562; DOI=10.1095/biolreprod.114.123661;
RA Meyer-Ficca M.L., Ihara M., Bader J.J., Leu N.A., Beneke S., Meyer R.G.;
RT "Spermatid head elongation with normal nuclear shaping requires ADP-
RT ribosyltransferase PARP11 (ARTD11) in mice.";
RL Biol. Reprod. 92:80-80(2015).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins (By similarity). Plays a role in
CC nuclear envelope stability and nuclear remodeling during spermiogenesis
CC (PubMed:25673562). {ECO:0000250|UniProtKB:Q9NR21,
CC ECO:0000269|PubMed:25673562}.
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:Q9NR21};
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:Q9NR21};
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:Q9NR21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-
CC lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:Q9NR21};
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q9NR21}. Note=Colocalizes with NUP153 at nuclear
CC pores. {ECO:0000250|UniProtKB:Q9NR21}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CFF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CFF0-2; Sequence=VSP_022557;
CC Name=3;
CC IsoId=Q8CFF0-3; Sequence=VSP_022558;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis, preferentially
CC in postmeiotic germ cells. Also detectable in other tissues, including
CC liver, lung, spleen, thymus and brain. {ECO:0000269|PubMed:25673562}.
CC -!- DEVELOPMENTAL STAGE: Undetectable in testis until postnatal day 18.
CC Sharply up-regulated from postnatal days 18 to 21. This timeframe
CC corresponds to the appearance of the first spermatids of the first wave
CC of spermatogenesis just before initiation of elongation. Remains
CC elevated in adult animals. {ECO:0000269|PubMed:25673562}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q9NR21}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are viable and are born in normal
CC Mendelian ratios. Knockout males, but not females, exhibit a striking
CC fertility defect, with the majority of males being sterile and a
CC minority producing infrequent and small litters. Sperm from mutant mice
CC exhibits mild to severe teratozoospermia, with structural defects in
CC elongating spermatid nuclear envelope and chromatin detachment
CC associated with abnormal nuclear shaping.
CC {ECO:0000269|PubMed:25673562}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AK133697; BAE21788.1; -; mRNA.
DR EMBL; AK151393; BAE30362.1; -; mRNA.
DR EMBL; BC040269; AAH40269.1; -; mRNA.
DR CCDS; CCDS20565.1; -. [Q8CFF0-1]
DR CCDS; CCDS85162.1; -. [Q8CFF0-2]
DR RefSeq; NP_001333441.1; NM_001346512.1. [Q8CFF0-2]
DR RefSeq; NP_001333442.1; NM_001346513.1. [Q8CFF0-2]
DR RefSeq; NP_852067.1; NM_181402.3. [Q8CFF0-1]
DR RefSeq; XP_006505294.1; XM_006505231.3. [Q8CFF0-1]
DR RefSeq; XP_006505295.1; XM_006505232.3. [Q8CFF0-1]
DR RefSeq; XP_006505296.1; XM_006505233.3. [Q8CFF0-1]
DR AlphaFoldDB; Q8CFF0; -.
DR SMR; Q8CFF0; -.
DR STRING; 10090.ENSMUSP00000036127; -.
DR PhosphoSitePlus; Q8CFF0; -.
DR PaxDb; Q8CFF0; -.
DR PRIDE; Q8CFF0; -.
DR Antibodypedia; 10533; 135 antibodies from 28 providers.
DR Ensembl; ENSMUST00000039680; ENSMUSP00000036127; ENSMUSG00000037997. [Q8CFF0-1]
DR Ensembl; ENSMUST00000112191; ENSMUSP00000107810; ENSMUSG00000037997. [Q8CFF0-2]
DR Ensembl; ENSMUST00000112193; ENSMUSP00000107812; ENSMUSG00000037997. [Q8CFF0-3]
DR Ensembl; ENSMUST00000112195; ENSMUSP00000107814; ENSMUSG00000037997. [Q8CFF0-3]
DR GeneID; 101187; -.
DR KEGG; mmu:101187; -.
DR UCSC; uc009dvw.1; mouse. [Q8CFF0-1]
DR UCSC; uc009dvz.1; mouse. [Q8CFF0-3]
DR CTD; 57097; -.
DR MGI; MGI:2141505; Parp11.
DR VEuPathDB; HostDB:ENSMUSG00000037997; -.
DR eggNOG; ENOG502QT2S; Eukaryota.
DR GeneTree; ENSGT00940000156857; -.
DR HOGENOM; CLU_014825_1_0_1; -.
DR InParanoid; Q8CFF0; -.
DR OMA; TWNPRIF; -.
DR PhylomeDB; Q8CFF0; -.
DR TreeFam; TF338389; -.
DR BioGRID-ORCS; 101187; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q8CFF0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CFF0; protein.
DR Bgee; ENSMUSG00000037997; Expressed in embryonic brain and 218 other tissues.
DR ExpressionAtlas; Q8CFF0; baseline and differential.
DR Genevisible; Q8CFF0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006998; P:nuclear envelope organization; IMP: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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Alternative splicing; Differentiation;
KW Glycosyltransferase; mRNA transport; NAD; Nuclear pore complex;
KW Nucleotidyltransferase; Nucleus; Protein transport; Reference proteome;
KW Spermatogenesis; Transferase; Translocation; Transport.
FT CHAIN 1..331
FT /note="Protein mono-ADP-ribosyltransferase PARP11"
FT /id="PRO_0000273420"
FT DOMAIN 15..99
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 116..331
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT MOD_RES 11
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR21"
FT MOD_RES 49
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR21"
FT MOD_RES 65
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR21"
FT MOD_RES 80
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9NR21"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022557"
FT VAR_SEQ 177..331
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022558"
SQ SEQUENCE 331 AA; 38737 MW; 70CF1926D8363C8F CRC64;
MFHKTEEFFP KKTDSDVDDM DTSDTQWGWF YLAECGKWHM FQPDTNIQCS VSSEDIEKSF
KTNPCGSISF TTSKFSYKID FAEMKQMNLV TGKQRLIKRA PFSISAFSYI CENEAIPMPT
HWENVNPDVP YQLVSLQNQT HEYNEVASLF GKTMDRNRIK RIQRIQNLDL WEFFCRKKAQ
LKKKRGVPQI NEQMLFHGTS SEFVEAICIH NFDWRINGVH GAVFGKGTYF ARDAAYSSRF
CKDDIKHGNT FQIHGVSLQQ RHLFRTYKSM FLARVLIGDY INGDSKYMRP PSKDGSYVNL
YDSCVDDTWN PKIFVVFDAN QIYPEYLIDF H
