PARG_MOUSE
ID PARG_MOUSE Reviewed; 969 AA.
AC O88622; Q80YQ6; Q8CB72;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Poly(ADP-ribose) glycohydrolase {ECO:0000303|PubMed:10449915};
DE EC=3.2.1.143 {ECO:0000250|UniProtKB:Q86W56};
GN Name=Parg {ECO:0000303|PubMed:10449915, ECO:0000312|MGI:MGI:1347094};
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).
RX PubMed=10449915; DOI=10.1159/000015310;
RA Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.;
RT "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human
RT chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization.";
RL Cytogenet. Cell Genet. 85:269-270(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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-256 AND SER-259, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-137; SER-256;
RP SER-259; SER-286; SER-293 AND SER-297, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-
CC ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-
CC ribose). PARG acts both as an endo- and exoglycosidase, releasing
CC poly(ADP-ribose) of different length as well as ADP-ribose monomers. It
CC is however unable to cleave the ester bond between the terminal ADP-
CC ribose and ADP-ribosylated residues, leaving proteins that are mono-
CC ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is
CC only present transiently and is rapidly degraded by PARG. Required to
CC prevent detrimental accumulation of poly(ADP-ribose) upon prolonged
CC replicative stress, while it is not required for recovery from
CC transient replicative stress. Responsible for the prevalence of mono-
CC ADP-ribosylated proteins in cells, thanks to its ability to degrade
CC poly(ADP-ribose) without cleaving the terminal protein-ribose bond.
CC Required for retinoid acid-dependent gene transactivation, probably by
CC removing poly(ADP-ribose) from histone demethylase KDM4D, allowing
CC chromatin derepression at RAR-dependent gene promoters. Involved in the
CC synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5.
CC Nuclear ATP generation is required for extensive chromatin remodeling
CC events that are energy-consuming. {ECO:0000250|UniProtKB:Q86W56}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-
CC alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-
CC COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143;
CC Evidence={ECO:0000250|UniProtKB:Q86W56};
CC -!- SUBUNIT: Interacts with PCNA. Interacts with NUDT5.
CC {ECO:0000250|UniProtKB:Q86W56}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86W56}.
CC Note=Colocalizes with PCNA at replication foci. Relocalizes to the
CC cytoplasm in response to DNA damage (By similarity).
CC {ECO:0000250|UniProtKB:Q86W56}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88622-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88622-2; Sequence=VSP_011771, VSP_011772;
CC -!- DOMAIN: The PIP-box mediates interaction with PCNA and localization to
CC replication foci. {ECO:0000250|UniProtKB:Q86W56}.
CC -!- SIMILARITY: Belongs to the poly(ADP-ribose) glycohydrolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC050892; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BC059827; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF079557; AAC28735.1; -; mRNA.
DR EMBL; AK036656; BAC29519.1; -; mRNA.
DR EMBL; BC050892; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC059827; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 4FC2; X-ray; 1.91 A; A/B/C/D=439-959.
DR PDB; 4N9Y; X-ray; 2.30 A; A=439-959.
DR PDB; 4N9Z; X-ray; 1.90 A; A/B=439-959.
DR PDB; 4NA0; X-ray; 2.40 A; A/B/C=439-959.
DR PDB; 4NA4; X-ray; 2.50 A; A/B/C=439-959.
DR PDB; 4NA5; X-ray; 2.00 A; A=439-959.
DR PDB; 4NA6; X-ray; 2.48 A; A/B=439-959.
DR PDBsum; 4FC2; -.
DR PDBsum; 4N9Y; -.
DR PDBsum; 4N9Z; -.
DR PDBsum; 4NA0; -.
DR PDBsum; 4NA4; -.
DR PDBsum; 4NA5; -.
DR PDBsum; 4NA6; -.
DR AlphaFoldDB; O88622; -.
DR SMR; O88622; -.
DR IntAct; O88622; 2.
DR STRING; 10090.ENSMUSP00000022470; -.
DR iPTMnet; O88622; -.
DR PhosphoSitePlus; O88622; -.
DR EPD; O88622; -.
DR jPOST; O88622; -.
DR MaxQB; O88622; -.
DR PaxDb; O88622; -.
DR PeptideAtlas; O88622; -.
DR PRIDE; O88622; -.
DR ProteomicsDB; 287779; -. [O88622-1]
DR ProteomicsDB; 287780; -. [O88622-2]
DR Antibodypedia; 44981; 240 antibodies from 27 providers.
DR Ensembl; ENSMUST00000163350; ENSMUSP00000131566; ENSMUSG00000021911. [O88622-2]
DR UCSC; uc007syp.1; mouse. [O88622-1]
DR UCSC; uc007syq.1; mouse. [O88622-2]
DR MGI; MGI:1347094; Parg.
DR VEuPathDB; HostDB:ENSMUSG00000021911; -.
DR eggNOG; KOG2064; Eukaryota.
DR GeneTree; ENSGT00390000003652; -.
DR InParanoid; O88622; -.
DR PhylomeDB; O88622; -.
DR BRENDA; 3.2.1.143; 3474.
DR Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
DR ChiTaRS; Parg; mouse.
DR PRO; PR:O88622; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O88622; protein.
DR Bgee; ENSMUSG00000021911; Expressed in metanephric ureteric bud and 262 other tissues.
DR ExpressionAtlas; O88622; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IMP:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0047658; F:alpha-amino-acid esterase activity; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IMP:MGI.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0016045; P:detection of bacterium; IMP:MGI.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0031056; P:regulation of histone modification; IBA:GO_Central.
DR InterPro; IPR046372; PARG_cat.
DR InterPro; IPR007724; Poly_GlycHdrlase.
DR PANTHER; PTHR12837; PTHR12837; 1.
DR Pfam; PF05028; PARG_cat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA damage; Hydrolase;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..969
FT /note="Poly(ADP-ribose) glycohydrolase"
FT /id="PRO_0000066603"
FT REGION 1..449
FT /note="A-domain"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..788
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOTIF 10..16
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOTIF 77..84
FT /note="PIP-box (PCNA interacting peptide)"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT COMPBIAS 72..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 730
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT ACT_SITE 748
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT ACT_SITE 749
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT BINDING 719..720
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT BINDING 747
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT BINDING 788
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9QYM2"
FT BINDING 862..867
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W56"
FT MOD_RES 334
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 920
FT /note="K -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011771"
FT VAR_SEQ 921..969
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011772"
FT CONFLICT 13..14
FT /note="RP -> A (in Ref. 1; AAC28735)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> R (in Ref. 1; AAC28735)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> V (in Ref. 3; BC050892/BC059827)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="A -> V (in Ref. 2; BAC29519)"
FT /evidence="ECO:0000305"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:4NA0"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 528..536
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 543..552
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 564..571
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 576..584
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 586..595
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 597..600
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 620..631
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 645..648
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:4N9Y"
FT HELIX 664..681
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 687..694
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 711..717
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 719..722
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 726..732
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 736..743
FT /evidence="ECO:0007829|PDB:4FC2"
FT HELIX 747..754
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 756..760
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 761..764
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 772..777
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 793..797
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:4NA4"
FT STRAND 813..818
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 825..829
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 831..845
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 852..854
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 858..861
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 866..868
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 872..885
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 890..893
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 898..913
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 918..932
FT /evidence="ECO:0007829|PDB:4N9Z"
FT TURN 933..935
FT /evidence="ECO:0007829|PDB:4N9Z"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:4N9Z"
FT HELIX 945..955
FT /evidence="ECO:0007829|PDB:4N9Z"
SQ SEQUENCE 969 AA; 109324 MW; 2626996A53AC48ED CRC64;
MSAGPGWEPC TKRPRWGAAG TSAPTASDSR SFPGRQRRVL DPKDAPVQFR VPPSSPACVS
GRAGPHRGNA TSFVFKQKTI TTWMDTKGPK TAESESKENN NTRIDSMMSS VQKDNFYPHK
VEKLENVPQL NLDKSPTEKS SQYLNQQQTA SVCKWQNEGK HAEQLLASEP PAGTPLPKQL
SNANIGQSPH TDDHSDTDHE EDRDNQQFLT PIKLANTKPT VGDGQARSNC KCSGSRQSVK
DCTGCQQEEV DVLPESPLSD VGAEDIGTGP KNDNKLTGQE SSLGDSPPFE KESEPESPMD
VDNSKNSCQD SEADEETSPV FDEQDDRSSQ TANKLSSCQA READGDLRKR YLTKGSEVRL
HFQFEGENNA GTSDLNAKPS GNSSSLNVEC RSSKQHGKRD SKITDHFMRI SKSEDRRKEQ
CEVRHQRTER KIPKYIPPNL PPEKKWLGTP IEEMRKMPRC GIHLPSLRPS ASHTVTVRVD
LLRAGEVPKP FPTHYKDLWD NKHVKMPCSE QNLYPVEDEN GERTAGSRWE LIQTALLNKF
TRPQNLKDAI LKYNVAYSKK WDFTALVDFW DKVLEEAEAQ HLYQSILPDM VKIALCLPNI
CTQPIPLLKQ KMNHSVTMSQ EQIASLLANA FFCTFPRRNA KMKSEYSSYP DINFNRLFEG
RSSRKPEKLK TLFCYFRRVT EKKPTGLVTF TRQSLEDFPE WERCEKPLTR LHVTYEGTIE
GNGRGMLQVD FANRFVGGGV TGAGLVQEEI RFLINPELIV SRLFTEVLDH NECLIITGTE
QYSEYTGYAE TYRWARSHED GSEKDDWQRR CTEIVAIDAL HFRRYLDQFV PEKVRRELNK
AYCGFLRPGV PSENLSAVAT GNWGCGAFGG DARLKALIQI LAAAAAERDV VYFTFGDSEL
MRDIYSMHTF LTERKLDVGK VYKLLLRYYN EECRNCSTPG PDIKLYPFIY HAVESSAETT
DMPGQKAGT
