PAR14_HUMAN
ID PAR14_HUMAN Reviewed; 1801 AA.
AC Q460N5; B4E2H0; Q460N4; Q8J027; Q9H9X9; Q9NV60; Q9ULF2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP14 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:16061477, ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:27796300};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 8 {ECO:0000303|PubMed:20106667};
DE Short=ARTD8 {ECO:0000303|PubMed:20106667};
DE AltName: Full=B aggressive lymphoma protein 2 {ECO:0000303|PubMed:16061477};
DE AltName: Full=Poly [ADP-ribose] polymerase 14 {ECO:0000303|PubMed:20106667};
DE Short=PARP-14 {ECO:0000303|PubMed:20106667};
GN Name=PARP14 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:29232};
GN Synonyms=BAL2 {ECO:0000303|PubMed:16061477},
GN KIAA1268 {ECO:0000303|PubMed:10574462};
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] (ISOFORM 3).
RC TISSUE=Ovary;
RA Guo J.H., Yu L.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1560 (ISOFORMS 1 AND 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1380-1801 (ISOFORMS 1/3/6).
RC TISSUE=Ovarian carcinoma, Teratocarcinoma, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-266 (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R.,
RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T.,
RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K.,
RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T.,
RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T.,
RA Sugano S.;
RT "Diversification of transcriptional modulation: large-scale identification
RT and characterization of putative alternative promoters of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 160-1801 (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 160-1801 (ISOFORM 1), ALTERNATIVE SPLICING, FUNCTION, AND
RP ADP-RIBOSYLATION.
RX PubMed=16061477; DOI=10.1074/jbc.m505408200;
RA Aguiar R.C.T., Takeyama K., He C., Kreinbrink K., Shipp M.A.;
RT "B-aggressive lymphoma family proteins have unique domains that modulate
RT transcription and exhibit poly(ADP-ribose) polymerase activity.";
RL J. Biol. Chem. 280:33756-33765(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 658-1801 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [7]
RP FUNCTION.
RX PubMed=18851833; DOI=10.1016/j.molcel.2008.08.009;
RA Kleine H., Poreba E., Lesniewicz K., Hassa P.O., Hottiger M.O.,
RA Litchfield D.W., Shilton B.H., Luescher B.;
RT "Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-
RT ribosylation.";
RL Mol. Cell 32:57-69(2008).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-1411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
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 [13]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PARP9, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, AND ADP-RIBOSYLATION.
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 [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1611-1801.
RX PubMed=22823910; DOI=10.1021/jm300746d;
RA Andersson C.D., Karlberg T., Ekblad T., Lindgren A.E., Thorsell A.G.,
RA Spjut S., Uciechowska U., Niemiec M.S., Wittung-Stafshede P., Weigelt J.,
RA Elofsson M., Schuler H., Linusson A.;
RT "Discovery of ligands for ADP-ribosyltransferases via docking-based virtual
RT screening.";
RL J. Med. Chem. 55:7706-7718(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1611-1801.
RX PubMed=22343925; DOI=10.1038/nbt.2121;
RA Wahlberg E., Karlberg T., Kouznetsova E., Markova N., Macchiarulo A.,
RA Thorsell A.G., Pol E., Frostell A., Ekblad T., Oncu D., Kull B.,
RA Robertson G.M., Pellicciari R., Schuler H., Weigelt J.;
RT "Family-wide chemical profiling and structural analysis of PARP and
RT tankyrase inhibitors.";
RL Nat. Biotechnol. 30:283-288(2012).
RN [17] {ECO:0007744|PDB:3Q6Z, ECO:0007744|PDB:3Q71, ECO:0007744|PDB:3VFQ, ECO:0007744|PDB:4ABK, ECO:0007744|PDB:4ABL, ECO:0007744|PDB:4D86}
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 784-1196 AND 1208-1388 IN
RP COMPLEXES WITH ADP AND ADENOSINE-5-DIPHOSPHORIBOSE, INTERACTION WITH
RP PARP10, AND MUTAGENESIS OF GLY-1055.
RX PubMed=23473667; DOI=10.1016/j.str.2012.12.019;
RA Forst A.H., Karlberg T., Herzog N., Thorsell A.G., Gross A., Feijs K.L.,
RA Verheugd P., Kursula P., Nijmeijer B., Kremmer E., Kleine H.,
RA Ladurner A.G., Schuler H., Luscher B.;
RT "Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8
RT macrodomains.";
RL Structure 21:462-475(2013).
CC -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC glutamate residues on target proteins (PubMed:16061477,
CC PubMed:27796300, PubMed:18851833, PubMed:25043379). In contrast to
CC PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation
CC (PubMed:25043379). Has been shown to catalyze the mono-ADP-ribosylation
CC of STAT1 at 'Glu-657' and 'Glu-705', thus decreasing STAT1
CC phosphorylation which negatively regulates pro-inflammatory cytokine
CC production in macrophages in response to IFNG stimulation
CC (PubMed:27796300). However, the role of ADP-ribosylation 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' (PubMed:29858569). Mono-ADP-
CC ribosylates STAT6; enhancing STAT6-dependent transcription
CC (PubMed:27796300). In macrophages, positively regulates MRC1 expression
CC in response to IL4 stimulation by promoting STAT6 phosphorylation
CC (PubMed:27796300). Mono-ADP-ribosylates PARP9 (PubMed:27796300).
CC {ECO:0000269|PubMed:16061477, ECO:0000269|PubMed:18851833,
CC ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:27796300,
CC 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 (By similarity). Interacts with PARP10
CC (PubMed:23473667). Interacts with PARP9 in IFNG-stimulated macrophages;
CC the interaction prevents PARP14-mediated STAT1 and STAT6 ADP-
CC riboslylation (PubMed:27796300). {ECO:0000250|UniProtKB:Q2EMV9,
CC ECO:0000269|PubMed:23473667, ECO:0000269|PubMed:27796300}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2EMV9}. Cytoplasm
CC {ECO:0000269|PubMed:27796300}. Note=In steady state splenocytes the
CC protein is mostly nuclear (By similarity). A minor proportion is
CC detected in the cytoplasm (By similarity). In macrophages, mainly
CC localizes to the cytoplasm (PubMed:27796300).
CC {ECO:0000250|UniProtKB:Q2EMV9, ECO:0000269|PubMed:27796300}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=6;
CC IsoId=Q460N5-6; Sequence=Displayed;
CC Name=1; Synonyms=BAL2B;
CC IsoId=Q460N5-1; Sequence=VSP_040876;
CC Name=3; Synonyms=BAL2A;
CC IsoId=Q460N5-3; Sequence=VSP_020014;
CC Name=4;
CC IsoId=Q460N5-4; Sequence=VSP_020018, VSP_020019;
CC Name=5;
CC IsoId=Q460N5-5; Sequence=VSP_020013, VSP_020017;
CC -!- TISSUE SPECIFICITY: Expressed in macrophages.
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:0000269|PubMed:16061477,
CC ECO:0000269|PubMed:27796300}.
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=AAY64449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAY64450.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14089.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=DB237115; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY134858; AAN08627.1; -; mRNA.
DR EMBL; AC048348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK001770; BAA91897.1; -; mRNA.
DR EMBL; AK022542; BAB14089.1; ALT_INIT; mRNA.
DR EMBL; AK304269; BAG65132.1; -; mRNA.
DR EMBL; DB237115; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ063584; AAY64449.1; ALT_INIT; mRNA.
DR EMBL; DQ063585; AAY64450.1; ALT_INIT; mRNA.
DR EMBL; AB033094; BAA86582.1; -; mRNA.
DR CCDS; CCDS46894.1; -. [Q460N5-6]
DR RefSeq; NP_060024.2; NM_017554.2. [Q460N5-6]
DR PDB; 3GOY; X-ray; 2.80 A; A/B/C/D=1611-1801.
DR PDB; 3Q6Z; X-ray; 2.23 A; A=789-979.
DR PDB; 3Q71; X-ray; 2.20 A; A=999-1196.
DR PDB; 3SE2; X-ray; 2.30 A; A/B/C/D=1611-1801.
DR PDB; 3SMI; X-ray; 2.40 A; A/B=1611-1801.
DR PDB; 3SMJ; X-ray; 1.50 A; A/B=1611-1801.
DR PDB; 3VFQ; X-ray; 2.80 A; A=784-1196.
DR PDB; 4ABK; X-ray; 1.60 A; A=1208-1388.
DR PDB; 4ABL; X-ray; 1.15 A; A=1208-1388.
DR PDB; 4D86; X-ray; 2.00 A; A=784-1196.
DR PDB; 4F1L; X-ray; 1.90 A; A/B/C/D=1611-1801.
DR PDB; 4F1Q; X-ray; 2.80 A; A/B=1611-1801.
DR PDB; 4PY4; X-ray; 2.76 A; A/B=1613-1801.
DR PDB; 5LXP; X-ray; 2.07 A; A/B=1611-1801.
DR PDB; 5LYH; X-ray; 2.17 A; A/B=1611-1801.
DR PDB; 5NQE; X-ray; 2.71 A; A/B=1611-1801.
DR PDB; 5O2D; X-ray; 1.60 A; A=994-1191.
DR PDB; 5QHT; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QHU; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QHV; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QHW; X-ray; 1.12 A; A=1208-1388.
DR PDB; 5QHX; X-ray; 1.11 A; A=1208-1388.
DR PDB; 5QHY; X-ray; 1.17 A; A=1208-1388.
DR PDB; 5QHZ; X-ray; 1.15 A; A=1208-1388.
DR PDB; 5QI0; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QI1; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QI2; X-ray; 1.08 A; A=1208-1388.
DR PDB; 5QI3; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QI4; X-ray; 1.20 A; A=1208-1388.
DR PDB; 5QI5; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QI6; X-ray; 1.10 A; A=1208-1388.
DR PDB; 5QI7; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QI8; X-ray; 1.09 A; A=1208-1388.
DR PDB; 5QI9; X-ray; 1.05 A; A=1208-1388.
DR PDB; 5QIA; X-ray; 1.14 A; A=1208-1388.
DR PDB; 5V7T; X-ray; 2.30 A; A=1610-1801.
DR PDB; 5V7W; X-ray; 2.65 A; A/B=1610-1801.
DR PDB; 6FYM; X-ray; 2.15 A; A/B/C/D=1611-1801.
DR PDB; 6FZM; X-ray; 2.67 A; A/B=1611-1801.
DR PDB; 6G0W; X-ray; 2.34 A; A/B=1611-1801.
DR PDB; 6WE2; X-ray; 2.66 A; A/B=1613-1801.
DR PDB; 6WE3; X-ray; 1.95 A; A/B=1611-1801.
DR PDB; 6WE4; X-ray; 1.60 A; A/B=1611-1801.
DR PDB; 7D2C; X-ray; 1.56 A; A=1206-1387.
DR PDB; 7L9Y; X-ray; 2.25 A; A/B/C/D=1611-1801.
DR PDB; 7LUN; X-ray; 2.57 A; A/B/C/D/E/F/G/H=1611-1801.
DR PDBsum; 3GOY; -.
DR PDBsum; 3Q6Z; -.
DR PDBsum; 3Q71; -.
DR PDBsum; 3SE2; -.
DR PDBsum; 3SMI; -.
DR PDBsum; 3SMJ; -.
DR PDBsum; 3VFQ; -.
DR PDBsum; 4ABK; -.
DR PDBsum; 4ABL; -.
DR PDBsum; 4D86; -.
DR PDBsum; 4F1L; -.
DR PDBsum; 4F1Q; -.
DR PDBsum; 4PY4; -.
DR PDBsum; 5LXP; -.
DR PDBsum; 5LYH; -.
DR PDBsum; 5NQE; -.
DR PDBsum; 5O2D; -.
DR PDBsum; 5QHT; -.
DR PDBsum; 5QHU; -.
DR PDBsum; 5QHV; -.
DR PDBsum; 5QHW; -.
DR PDBsum; 5QHX; -.
DR PDBsum; 5QHY; -.
DR PDBsum; 5QHZ; -.
DR PDBsum; 5QI0; -.
DR PDBsum; 5QI1; -.
DR PDBsum; 5QI2; -.
DR PDBsum; 5QI3; -.
DR PDBsum; 5QI4; -.
DR PDBsum; 5QI5; -.
DR PDBsum; 5QI6; -.
DR PDBsum; 5QI7; -.
DR PDBsum; 5QI8; -.
DR PDBsum; 5QI9; -.
DR PDBsum; 5QIA; -.
DR PDBsum; 5V7T; -.
DR PDBsum; 5V7W; -.
DR PDBsum; 6FYM; -.
DR PDBsum; 6FZM; -.
DR PDBsum; 6G0W; -.
DR PDBsum; 6WE2; -.
DR PDBsum; 6WE3; -.
DR PDBsum; 6WE4; -.
DR PDBsum; 7D2C; -.
DR PDBsum; 7L9Y; -.
DR PDBsum; 7LUN; -.
DR AlphaFoldDB; Q460N5; -.
DR SMR; Q460N5; -.
DR BioGRID; 120082; 41.
DR DIP; DIP-61130N; -.
DR IntAct; Q460N5; 4.
DR MINT; Q460N5; -.
DR STRING; 9606.ENSP00000418194; -.
DR BindingDB; Q460N5; -.
DR ChEMBL; CHEMBL2176777; -.
DR DrugCentral; Q460N5; -.
DR GlyGen; Q460N5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q460N5; -.
DR PhosphoSitePlus; Q460N5; -.
DR BioMuta; PARP14; -.
DR DMDM; 327478567; -.
DR EPD; Q460N5; -.
DR jPOST; Q460N5; -.
DR MassIVE; Q460N5; -.
DR MaxQB; Q460N5; -.
DR PaxDb; Q460N5; -.
DR PeptideAtlas; Q460N5; -.
DR PRIDE; Q460N5; -.
DR ProteomicsDB; 61930; -. [Q460N5-6]
DR ProteomicsDB; 61931; -. [Q460N5-1]
DR ProteomicsDB; 61932; -. [Q460N5-3]
DR ProteomicsDB; 61933; -. [Q460N5-4]
DR ProteomicsDB; 61934; -. [Q460N5-5]
DR ABCD; Q460N5; 1 sequenced antibody.
DR Antibodypedia; 2150; 94 antibodies from 20 providers.
DR DNASU; 54625; -.
DR Ensembl; ENST00000474629.7; ENSP00000418194.2; ENSG00000173193.15. [Q460N5-6]
DR GeneID; 54625; -.
DR KEGG; hsa:54625; -.
DR MANE-Select; ENST00000474629.7; ENSP00000418194.2; NM_017554.3; NP_060024.2.
DR UCSC; uc003efq.5; human. [Q460N5-6]
DR CTD; 54625; -.
DR DisGeNET; 54625; -.
DR GeneCards; PARP14; -.
DR HGNC; HGNC:29232; PARP14.
DR HPA; ENSG00000173193; Low tissue specificity.
DR MIM; 610028; gene.
DR neXtProt; NX_Q460N5; -.
DR OpenTargets; ENSG00000173193; -.
DR PharmGKB; PA134861585; -.
DR VEuPathDB; HostDB:ENSG00000173193; -.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000154311; -.
DR HOGENOM; CLU_003288_1_0_1; -.
DR InParanoid; Q460N5; -.
DR OMA; PLWKFFQ; -.
DR PhylomeDB; Q460N5; -.
DR TreeFam; TF328965; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q460N5; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR Reactome; R-HSA-9683610; Maturation of nucleoprotein.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR SignaLink; Q460N5; -.
DR BioGRID-ORCS; 54625; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; PARP14; human.
DR EvolutionaryTrace; Q460N5; -.
DR GenomeRNAi; 54625; -.
DR Pharos; Q460N5; Tchem.
DR PRO; PR:Q460N5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q460N5; protein.
DR Bgee; ENSG00000173193; Expressed in sural nerve and 177 other tissues.
DR ExpressionAtlas; Q460N5; baseline and differential.
DR Genevisible; Q460N5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IMP:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA: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; IMP:UniProtKB.
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; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:UniProtKB.
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..1801
FT /note="Protein mono-ADP-ribosyltransferase PARP14"
FT /id="PRO_0000247589"
FT DOMAIN 791..978
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1003..1190
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1216..1387
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1523..1601
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 1605..1801
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 109..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 824
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q6Z"
FT BINDING 833
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q6Z"
FT BINDING 922..926
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q6Z"
FT BINDING 961
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q6Z"
FT BINDING 1023..1024
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q71, ECO:0007744|PDB:3VFQ"
FT BINDING 1034
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:4ABK"
FT BINDING 1046..1049
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q71, ECO:0007744|PDB:3VFQ"
FT BINDING 1133..1137
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q71, ECO:0007744|PDB:3VFQ"
FT BINDING 1175..1178
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q71, ECO:0007744|PDB:3VFQ"
FT BINDING 1235..1236
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:4ABK"
FT BINDING 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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:4ABK"
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:4ABK"
FT BINDING 1332..1336
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3Q71, ECO:0007744|PDB:3VFQ"
FT BINDING 1371
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:0000269|PubMed:23473667,
FT ECO:0007744|PDB:4ABK"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1004
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020013"
FT VAR_SEQ 1..283
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020014"
FT VAR_SEQ 119..199
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16061477, ECO:0000303|PubMed:16344560"
FT /id="VSP_040876"
FT VAR_SEQ 1005..1013
FT /note="KGSLVSPGG -> MYLRRLLRP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020017"
FT VAR_SEQ 1648..1680
FT /note="IERIQNPDLWNSYQAKKKTMDAKNGQTMNEKQL -> VSLLLECSFWMVEIS
FT SVMVLYKIHFHSLPITFF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:16061477"
FT /id="VSP_020018"
FT VAR_SEQ 1681..1801
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:16061477"
FT /id="VSP_020019"
FT MUTAGEN 1055
FT /note="G->E: Abolishes interaction with PARP10."
FT /evidence="ECO:0000269|PubMed:23473667"
FT CONFLICT 59
FT /note="Y -> C (in Ref. 4; DB237115)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="N -> D (in Ref. 3; BAG65132)"
FT /evidence="ECO:0000305"
FT CONFLICT 1239
FT /note="E -> G (in Ref. 3; BAA91897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1499
FT /note="G -> A (in Ref. 1; AAN08627)"
FT /evidence="ECO:0000305"
FT CONFLICT 1521
FT /note="A -> G (in Ref. 1; AAN08627)"
FT /evidence="ECO:0000305"
FT STRAND 792..799
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 802..808
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 815..823
FT /evidence="ECO:0007829|PDB:4D86"
FT HELIX 832..841
FT /evidence="ECO:0007829|PDB:4D86"
FT HELIX 844..856
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 861..868
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 872..881
FT /evidence="ECO:0007829|PDB:4D86"
FT HELIX 887..889
FT /evidence="ECO:0007829|PDB:4D86"
FT HELIX 890..910
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 914..918
FT /evidence="ECO:0007829|PDB:4D86"
FT TURN 921..926
FT /evidence="ECO:0007829|PDB:3VFQ"
FT HELIX 930..947
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 956..963
FT /evidence="ECO:0007829|PDB:4D86"
FT HELIX 964..977
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 1006..1009
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1015..1019
FT /evidence="ECO:0007829|PDB:5O2D"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:4D86"
FT STRAND 1028..1034
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1041..1044
FT /evidence="ECO:0007829|PDB:4D86"
FT HELIX 1045..1054
FT /evidence="ECO:0007829|PDB:5O2D"
FT HELIX 1057..1066
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1076..1080
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1084..1092
FT /evidence="ECO:0007829|PDB:5O2D"
FT HELIX 1097..1099
FT /evidence="ECO:0007829|PDB:5O2D"
FT HELIX 1101..1121
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1126..1130
FT /evidence="ECO:0007829|PDB:5O2D"
FT HELIX 1141..1158
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1166..1170
FT /evidence="ECO:0007829|PDB:5O2D"
FT HELIX 1176..1189
FT /evidence="ECO:0007829|PDB:5O2D"
FT STRAND 1213..1216
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1219..1224
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1227..1234
FT /evidence="ECO:0007829|PDB:5QHT"
FT HELIX 1236..1238
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1242..1248
FT /evidence="ECO:0007829|PDB:5QHT"
FT HELIX 1258..1266
FT /evidence="ECO:0007829|PDB:5QHT"
FT HELIX 1268..1280
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1284..1289
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1293..1302
FT /evidence="ECO:0007829|PDB:5QHT"
FT HELIX 1307..1320
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1325..1328
FT /evidence="ECO:0007829|PDB:5QHT"
FT HELIX 1340..1356
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1365..1372
FT /evidence="ECO:0007829|PDB:5QHT"
FT HELIX 1373..1386
FT /evidence="ECO:0007829|PDB:5QHT"
FT STRAND 1617..1621
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1629..1640
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1643..1652
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1654..1670
FT /evidence="ECO:0007829|PDB:3SMJ"
FT TURN 1671..1673
FT /evidence="ECO:0007829|PDB:6WE4"
FT STRAND 1677..1684
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1686..1688
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1689..1695
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1699..1702
FT /evidence="ECO:0007829|PDB:6WE3"
FT HELIX 1704..1706
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1707..1709
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1713..1718
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1719..1722
FT /evidence="ECO:0007829|PDB:3SMJ"
FT TURN 1725..1727
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1736..1744
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1747..1750
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1760..1762
FT /evidence="ECO:0007829|PDB:6WE4"
FT STRAND 1763..1765
FT /evidence="ECO:0007829|PDB:5LYH"
FT STRAND 1767..1769
FT /evidence="ECO:0007829|PDB:6FZM"
FT STRAND 1771..1775
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1777..1779
FT /evidence="ECO:0007829|PDB:3SMJ"
FT STRAND 1781..1785
FT /evidence="ECO:0007829|PDB:3SMJ"
FT HELIX 1788..1790
FT /evidence="ECO:0007829|PDB:7L9Y"
FT STRAND 1791..1800
FT /evidence="ECO:0007829|PDB:3SMJ"
SQ SEQUENCE 1801 AA; 202800 MW; 27B027DFC7E773BD CRC64;
MAVPGSFPLL VEGSWGPDPP KNLNTKLQMY FQSPKRSGGG ECEVRQDPRS PSRFLVFFYP
EDVRQKVLER KNHELVWQGK GTFKLTVQLP ATPDEIDHVF EEELLTKESK TKEDVKEPDV
SEELDTKLPL DGGLDKMEDI PEECENISSL VAFENLKANV TDIMLILLVE NISGLSNDDF
QVEIIRDFDV AVVTFQKHID TIRFVDDCTK HHSIKQLQLS PRLLEVTNTI RVENLPPGAD
DYSLKLFFEN PYNGGGRVAN VEYFPEESSA LIEFFDRKVL DTIMATKLDF NKMPLSVFPY
YASLGTALYG KEKPLIKLPA PFEESLDLPL WKFLQKKNHL IEEINDEMRR CHCELTWSQL
SGKVTIRPAA TLVNEGRPRI KTWQADTSTT LSSIRSKYKV NPIKVDPTMW DTIKNDVKDD
RILIEFDTLK EMVILAGKSE DVQSIEVQVR ELIESTTQKI KREEQSLKEK MIISPGRYFL
LCHSSLLDHL LTECPEIEIC YDRVTQHLCL KGPSADVYKA KCEIQEKVYT MAQKNIQVSP
EIFQFLQQVN WKEFSKCLFI AQKILALYEL EGTTVLLTSC SSEALLEAEK QMLSALNYKR
IEVENKEVLH GKKWKGLTHN LLKKQNSSPN TVIINELTSE TTAEVIITGC VKEVNETYKL
LFNFVEQNMK IERLVEVKPS LVIDYLKTEK KLFWPKIKKV NVQVSFNPEN KQKGILLTGS
KTEVLKAVDI VKQVWDSVCV KSVHTDKPGA KQFFQDKARF YQSEIKRLFG CYIELQENEV
MKEGGSPAGQ KCFSRTVLAP GVVLIVQQGD LARLPVDVVV NASNEDLKHY GGLAAALSKA
AGPELQADCD QIVKREGRLL PGNATISKAG KLPYHHVIHA VGPRWSGYEA PRCVYLLRRA
VQLSLCLAEK YKYRSIAIPA ISSGVFGFPL GRCVETIVSA IKENFQFKKD GHCLKEIYLV
DVSEKTVEAF AEAVKTVFKA TLPDTAAPPG LPPAAAGPGK TSWEKGSLVS PGGLQMLLVK
EGVQNAKTDV VVNSVPLDLV LSRGPLSKSL LEKAGPELQE ELDTVGQGVA VSMGTVLKTS
SWNLDCRYVL HVVAPEWRNG STSSLKIMED IIRECMEITE SLSLKSIAFP AIGTGNLGFP
KNIFAELIIS EVFKFSSKNQ LKTLQEVHFL LHPSDHENIQ AFSDEFARRA NGNLVSDKIP
KAKDTQGFYG TVSSPDSGVY EMKIGSIIFQ VASGDITKEE ADVIVNSTSN SFNLKAGVSK
AILECAGQNV ERECSQQAQQ RKNDYIITGG GFLRCKNIIH VIGGNDVKSS VSSVLQECEK
KNYSSICLPA IGTGNAKQHP DKVAEAIIDA IEDFVQKGSA QSVKKVKVVI FLPQVLDVFY
ANMKKREGTQ LSSQQSVMSK LASFLGFSKQ SPQKKNHLVL EKKTESATFR VCGENVTCVE
YAISWLQDLI EKEQCPYTSE DECIKDFDEK EYQELNELQK KLNINISLDH KRPLIKVLGI
SRDVMQARDE IEAMIKRVRL AKEQESRADC ISEFIEWQYN DNNTSHCFNK MTNLKLEDAR
REKKKTVDVK INHRHYTVNL NTYTATDTKG HSLSVQRLTK SKVDIPAHWS DMKQQNFCVV
ELLPSDPEYN TVASKFNQTC SHFRIEKIER IQNPDLWNSY QAKKKTMDAK NGQTMNEKQL
FHGTDAGSVP HVNRNGFNRS YAGKNAVAYG KGTYFAVNAN YSANDTYSRP DANGRKHVYY
VRVLTGIYTH GNHSLIVPPS KNPQNPTDLY DTVTDNVHHP SLFVAFYDYQ AYPEYLITFR
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