PAR14_MOUSE
ID PAR14_MOUSE Reviewed; 1817 AA.
AC Q2EMV9; E9QP48; Q571C6; Q8BN35; Q8VDT6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP14 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:27796300};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 8;
DE Short=ARTD8;
DE AltName: Full=Collaborator of STAT6 {ECO:0000303|PubMed:16537510};
DE Short=CoaSt6 {ECO:0000303|PubMed:16537510};
DE AltName: Full=Poly [ADP-ribose] polymerase 14;
DE Short=PARP-14;
GN Name=Parp14 {ECO:0000312|MGI:MGI:1919489};
GN Synonyms=Kiaa1268 {ECO:0000303|Ref.4};
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] (ISOFORM 1), FUNCTION, INTERACTION WITH STAT6,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=16537510; DOI=10.1073/pnas.0506981103;
RA Goenka S., Boothby M.;
RT "Selective potentiation of Stat-dependent gene expression by collaborator
RT of Stat6 (CoaSt6), a transcriptional cofactor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4210-4215(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1393 (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-1817.
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1382-1817, AND VARIANTS SER-1384;
RP ASP-1658 AND GLY-1682.
RC STRAIN=Czech II; 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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=18069692; DOI=10.1002/dvdy.21399;
RA Hakme A., Huber A., Dolle P., Schreiber V.;
RT "The macroPARP genes Parp-9 and Parp-14 are developmentally and
RT differentially regulated in mouse tissues.";
RL Dev. Dyn. 237:209-215(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
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).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27796300; DOI=10.1038/ncomms12849;
RA Iwata H., Goettsch C., Sharma A., Ricchiuto P., Goh W.W., Halu A.,
RA Yamada I., Yoshida H., Hara T., Wei M., Inoue N., Fukuda D., Mojcher A.,
RA Mattson P.C., Barabasi A.L., Boothby M., Aikawa E., Singh S.A., Aikawa M.;
RT "PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-
RT ribosylation.";
RL Nat. Commun. 7:12849-12849(2016).
RN [9]
RP COMMENT ON STAT1 ADP-RIBOSYLATION.
RX PubMed=29858569; DOI=10.1038/s41467-018-04522-z;
RA Begitt A., Cavey J., Droescher M., Vinkemeier U.;
RT "On the role of STAT1 and STAT6 ADP-ribosylation in the regulation of
RT macrophage activation.";
RL Nat. Commun. 9:2144-2144(2018).
RN [10]
RP STRUCTURE BY NMR OF 1532-1617.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of WWE domain in Parp14 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC glutamate residues on target proteins (PubMed:27796300). In contrast to
CC PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By
CC similarity). Catalyzes mono-ADP-ribosylating STAT1 at 'Glu-657' and
CC 'Glu-705' and thus decreasing STAT1 phosphorylation, negatively
CC regulates pro-inflammatory cytokines production in macrophages in
CC response to IFNG stimulation (PubMed:27796300). However, the role of
CC ADP-ribosylation in the prevention of STAT1 phosphorylation has been
CC called into question and it has been suggested that the inhibition of
CC phosphorylation may be the result of sumoylation of STAT1 'Lys-703'
CC (PubMed:29858569). Mono-ADP-ribosylates STAT6; enhancing STAT6-
CC dependent transcription (PubMed:27796300). In macrophages, positively
CC regulates MRC1 expression in response to IL4 stimulation by promoting
CC STAT6 phosphorylation (PubMed:27796300). Mono-ADP-ribosylates PARP9 (By
CC similarity). {ECO:0000250|UniProtKB:Q460N5,
CC ECO:0000269|PubMed:27796300, ECO:0000305|PubMed:29858569}.
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:27796300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000269|PubMed:27796300};
CC -!- SUBUNIT: Interacts with STAT6 (PubMed:16537510). Interacts with PARP10
CC (By similarity). Interacts with PARP9 in IFNG-stimulated macrophages;
CC the interaction prevents PARP14-mediated STAT1 and STAT6 ADP-
CC riboslylation (By similarity). {ECO:0000250|UniProtKB:Q460N5,
CC ECO:0000269|PubMed:16537510}.
CC -!- INTERACTION:
CC Q2EMV9; P06745: Gpi; NbExp=4; IntAct=EBI-1534943, EBI-1534927;
CC Q2EMV9; P52633: Stat6; NbExp=3; IntAct=EBI-1534943, EBI-647085;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537510}. Cytoplasm
CC {ECO:0000269|PubMed:16537510}. Note=In steady state cells the protein
CC is mostly nuclear (PubMed:16537510). A minor proportion is detected in
CC the cytoplasm (PubMed:16537510). In macrophages, mainly localizes to
CC the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q460N5,
CC ECO:0000269|PubMed:16537510}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2EMV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2EMV9-2; Sequence=VSP_020020;
CC -!- TISSUE SPECIFICITY: Weakly expressed in the thymus during development
CC and in adulthood (PubMed:18069692). Expressed in macrophages
CC (PubMed:27796300). {ECO:0000269|PubMed:18069692,
CC ECO:0000269|PubMed:27796300}.
CC -!- INDUCTION: Up-regulated by IFNG in macrophages. Down-regulated by IL4
CC in macrophages. {ECO:0000269|PubMed:27796300}.
CC -!- PTM: Auto-ADP-ribosylated. {ECO:0000250|UniProtKB:Q460N5}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- CAUTION: The role of PARP14-mediated ADP-ribosylation of STAT1 in the
CC prevention of STAT1 phosphorylation has been called into question and
CC it has been suggested that the inhibition of phosphorylation may be the
CC result of sumoylation of STAT1 'Lys-703'.
CC {ECO:0000305|PubMed:29858569}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21340.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21340.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; DQ372930; ABD16173.1; -; mRNA.
DR EMBL; AC129574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK089685; BAC40943.1; -; mRNA.
DR EMBL; AK220263; BAD90188.1; -; mRNA.
DR EMBL; BC021340; AAH21340.1; ALT_INIT; mRNA.
DR CCDS; CCDS28143.1; -. [Q2EMV9-1]
DR RefSeq; NP_001034619.2; NM_001039530.3. [Q2EMV9-1]
DR PDB; 1X4R; NMR; -; A=1532-1617.
DR PDBsum; 1X4R; -.
DR AlphaFoldDB; Q2EMV9; -.
DR SMR; Q2EMV9; -.
DR BioGRID; 246104; 13.
DR DIP; DIP-38053N; -.
DR IntAct; Q2EMV9; 3.
DR STRING; 10090.ENSMUSP00000037657; -.
DR iPTMnet; Q2EMV9; -.
DR PhosphoSitePlus; Q2EMV9; -.
DR SwissPalm; Q2EMV9; -.
DR EPD; Q2EMV9; -.
DR jPOST; Q2EMV9; -.
DR MaxQB; Q2EMV9; -.
DR PaxDb; Q2EMV9; -.
DR PeptideAtlas; Q2EMV9; -.
DR PRIDE; Q2EMV9; -.
DR ProteomicsDB; 287951; -. [Q2EMV9-1]
DR ProteomicsDB; 287952; -. [Q2EMV9-2]
DR Antibodypedia; 2150; 94 antibodies from 20 providers.
DR Ensembl; ENSMUST00000042665; ENSMUSP00000037657; ENSMUSG00000034422. [Q2EMV9-1]
DR GeneID; 547253; -.
DR KEGG; mmu:547253; -.
DR UCSC; uc007zbs.2; mouse. [Q2EMV9-1]
DR CTD; 54625; -.
DR MGI; MGI:1919489; Parp14.
DR VEuPathDB; HostDB:ENSMUSG00000034422; -.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000154311; -.
DR HOGENOM; CLU_003288_1_0_1; -.
DR InParanoid; Q2EMV9; -.
DR OMA; PLWKFFQ; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q2EMV9; -.
DR TreeFam; TF328965; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 547253; 1 hit in 74 CRISPR screens.
DR EvolutionaryTrace; Q2EMV9; -.
DR PRO; PR:Q2EMV9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q2EMV9; protein.
DR Bgee; ENSMUSG00000034422; Expressed in small intestine Peyer's patch and 151 other tissues.
DR Genevisible; Q2EMV9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:0070403; F:NAD+ binding; ISO:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:1902216; P:positive regulation of interleukin-4-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISO:MGI.
DR CDD; cd12543; RRM2_PAR14; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.40.220.10; -; 3.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034517; PAR14_RRM2.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR Pfam; PF01661; Macro; 3.
DR Pfam; PF00644; PARP; 1.
DR SMART; SM00506; A1pp; 3.
DR SUPFAM; SSF117839; SSF117839; 1.
DR SUPFAM; SSF52949; SSF52949; 3.
DR PROSITE; PS51154; MACRO; 3.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Cytoplasm;
KW Glycosyltransferase; Immunity; Innate immunity; NAD;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..1817
FT /note="Protein mono-ADP-ribosyltransferase PARP14"
FT /id="PRO_0000247590"
FT DOMAIN 802..989
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1014..1202
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1227..1398
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1539..1617
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 1621..1817
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 87..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 835
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="1"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 844
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="1"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 933..937
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="1"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1034..1035
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="2"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1045
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="2"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1057..1060
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="2"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1145..1149
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="2"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1187..1190
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="2"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1246..1247
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="3"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1258
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="3"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1269
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="3"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1343..1347
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="3"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT BINDING 1382
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_label="3"
FT /ligand_part="5-O-(ADP-D-ribosyl)-L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:142540"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT MOD_RES 1419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q460N5"
FT VAR_SEQ 1..589
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020020"
FT VARIANT 1384
FT /note="P -> S (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 1658
FT /note="N -> D (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 1682
FT /note="S -> G (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 708
FT /note="N -> Y (in Ref. 1; ABD16173)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="E -> K (in Ref. 3; BAC40943)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="S -> T (in Ref. 1; ABD16173)"
FT /evidence="ECO:0000305"
FT CONFLICT 1209
FT /note="K -> E (in Ref. 3; BAC40943)"
FT /evidence="ECO:0000305"
FT CONFLICT 1609
FT /note="F -> L (in Ref. 1; ABD16173)"
FT /evidence="ECO:0000305"
FT STRAND 1532..1534
FT /evidence="ECO:0007829|PDB:1X4R"
FT TURN 1537..1541
FT /evidence="ECO:0007829|PDB:1X4R"
FT HELIX 1542..1548
FT /evidence="ECO:0007829|PDB:1X4R"
FT STRAND 1552..1556
FT /evidence="ECO:0007829|PDB:1X4R"
FT STRAND 1561..1563
FT /evidence="ECO:0007829|PDB:1X4R"
FT HELIX 1568..1577
FT /evidence="ECO:0007829|PDB:1X4R"
FT STRAND 1581..1587
FT /evidence="ECO:0007829|PDB:1X4R"
FT STRAND 1590..1595
FT /evidence="ECO:0007829|PDB:1X4R"
FT TURN 1596..1599
FT /evidence="ECO:0007829|PDB:1X4R"
FT STRAND 1600..1602
FT /evidence="ECO:0007829|PDB:1X4R"
FT STRAND 1608..1614
FT /evidence="ECO:0007829|PDB:1X4R"
SQ SEQUENCE 1817 AA; 203802 MW; 42E902CC20858931 CRC64;
MAASGSFPLL VEGSWGPDPP KNLINKLQVY FQSRKKSGGG ECEVVPEPGN PARFRVLFSP
EDVRQNVLER GNHELVWQEK GTFKLTVLMP TDPEEASASK KSRKESPEEE SKTKEDAVKQ
GDLDITHSPS SGSEKTEDVP KECENISSMV AFENLPEKVS EMVLTILVEN ISGLPSDDFK
VEVNRDFAVA VVTFQKPIDI KKFIVDCISH RSNQQLQLAP RLLETTNVVR VENLPPGVDE
YQLQLFFENP FNGGGRVARV ECFPEESSAL VEFCDSKVLD TVMAKTHSYN KMPLSVFPYY
PSLGTALYGE EKPLIKLPAS FQESLDLPLW KFFQKNNHLI EEINNEMRCC HCELTWSEIN
GKLTIRPAAT LVNHRLSIKT WQRDASAVLS GIKSKYGVEL FEVCSPVWDI IKHELESGDD
RVLVEFEKES LNIAGKSEDV QGMSQKIREL IESTTEKLRR EEQSLKEKVA ISPGKHYLLH
HSGFLKDLSK GFPEMEISYD ATAQFLYLKG FRADVYKVKC DIQEKVFSMA QKDVQVSSEV
FEFLQQVDSQ RLSKSLFEAQ NILAIYELKG TALFLVGSSF KDLAEAETKM LSALSHKQIE
VEDKEVLISN GWKKKVHPLQ KRHSSCATII VQNELTSETP AKVIVTGCVK EVNEIHRQLF
EYLENNMKVE RALKIKPSLI VDYLRTDKRL LSKIKKAHVY VHFKPKDNPN SILLTGCKSK
VLECMNLVKE IQDSVCVQRF QTDKAGVRHF FKDKESYYKT EIGRQFGCVI ELEEDREEKG
EEEDGEEEEG EEEGESSINE QKCHLQRDIA PGVKLFVLEE DLSRFPVDVV VNAANENLKH
ISGLAQALSK AAGPELQTEC DQIVKEGGVV LPGNAVISKA GKLPCHHVIH AVGPRWKGDK
VLECVSLLKK VVRQSLSLAE EHRCRSIAMP AVSAGIFDFP LELCVANIVS AIKEHFQHKR
DTHTLKKIYL VGLPAKVARA FAEAVKTTYK DSLSHTAFPS SLKALVPLGK TPQKQGSLLV
SPEGLRIRLV EEGVQNATTH AIVNSISPDL KLNKGPLSQA FLEKAGPKLQ EELTRSGQGV
SVDVGTILQT SGCNLNSRHV FHVVPPPWKS NNSAWSLKIM KNIIRDCLKT TENLSLQSIA
FPAIGTGNLR FPKPEFAKLI ISEVLKFSSR NQLKTLQEVQ FLLHPKDHEN IQAFSDEFDK
RNNGDPSDKN PKAEDTQGIY GSLSSPTLGM HEMNIGPILF QVATGNIIKE VADVIVNSTT
LTFDLKSGVS KAILEGAGQN VEQECSLLAK QSNHGYIVTG GGLLQCKNII HVVGGNDVKK
SVSCVLEECE QRNYSSICLP AIGTGNAQQD PNVVAKAIID AIEEFVQKKS VQAVKRVKVV
IFQPHILQFF YDNMKEREGS PAPPKQSPAK QSVMSKIASF LGFPKQASPK KNTLVLEKKI
EHTVFQVCGS GVDSVNKTIS WLKELITKEQ LSYTNDDECV SDFDMEEYEK LNEIQKELNI
TIEMNQKKTS IQVSGISRDV IKARDEIEGM IKSIRLAKEK ESQADYISTY VEWQYIDKNI
TQCFDKMTNM KLEVAWKAKK KDTVVQIHNQ DFTVDLSTNT ATAPQGQTFT VQRLVKAEAE
IPANWSDMKQ DKLLLVNLQT SDPEYNMVAS AFRQTCSNFF IEKIERIQNP ALWRRYQAYK
KSMDEKNGNV RNEKHLFHGT EASSLPQLNS NGFNRSYAGK NATAYGKGTY FAVKASYSAC
DTYSRPDTNG RKYMYYVRVL TGNYTNGNAS LIVPPSRDPQ NAADLYDTVT DNDKNPSIFV
VFYDNQTYPE YLITFRQ
