TNKS1_MOUSE
ID TNKS1_MOUSE Reviewed; 1320 AA.
AC Q6PFX9; Q8BX62;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Poly [ADP-ribose] polymerase tankyrase-1 {ECO:0000305};
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:O95271};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 5;
DE Short=ARTD5;
DE AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase-1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:O95271};
DE AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase 1;
DE Short=Tankyrase I;
DE AltName: Full=Tankyrase-1;
DE Short=TANK1;
GN Name=Tnks; Synonyms=Tnks1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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].
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] (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).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase involved in various processes
CC such as Wnt signaling pathway, telomere length and vesicle trafficking.
CC Acts as an activator of the Wnt signaling pathway by mediating poly-
CC ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of
CC the beta-catenin destruction complex: poly-ADP-ribosylated target
CC proteins are recognized by RNF146, which mediates their ubiquitination
CC and subsequent degradation. Also mediates PARsylation of BLZF1 and
CC CASC3, followed by recruitment of RNF146 and subsequent ubiquitination.
CC Mediates PARsylation of TERF1, thereby contributing to the regulation
CC of telomere length. Involved in centrosome maturation during
CC prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also
CC regulate vesicle trafficking and modulate the subcellular distribution
CC of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly
CC through PARsylation of NUMA1. Stimulates 26S proteasome activity.
CC {ECO:0000250|UniProtKB:O95271}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000250|UniProtKB:O95271};
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:0000305};
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:0000305};
CC -!- SUBUNIT: Oligomerizes and associates with TNKS2. Interacts with the
CC cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to
CC the N-terminus of telomeric TERF1 via the ANK repeats. Found in a
CC complex with POT1; TERF1 and TINF2. Interacts with AXIN1. Interacts
CC with AXIN2. Interacts with BLZF1 and CASC3. Interacts with NUMA1.
CC {ECO:0000250|UniProtKB:O95271}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95271}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:O95271}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O95271}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:O95271}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:O95271}. Note=Associated with the Golgi and with
CC juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at
CC nuclear pore complexes and around the pericentriolar matrix of mitotic
CC centromeres. During interphase, a small fraction of TNKS is found in
CC the nucleus, associated with TERF1. Localizes to spindle poles at
CC mitosis onset via interaction with NUMA1.
CC {ECO:0000250|UniProtKB:O95271}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PFX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PFX9-2; Sequence=VSP_041320;
CC -!- PTM: Phosphorylated on serine residues by MAPK kinases upon insulin
CC stimulation. Phosphorylated during mitosis.
CC {ECO:0000250|UniProtKB:O95271}.
CC -!- PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to
CC its degradation. {ECO:0000250|UniProtKB:O95271}.
CC -!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is
CC recognized by RNF146, followed by ubiquitination.
CC {ECO:0000250|UniProtKB:O95271}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK048860; BAC33475.1; -; mRNA.
DR EMBL; AC122458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057370; AAH57370.1; -; mRNA.
DR CCDS; CCDS22242.1; -. [Q6PFX9-1]
DR RefSeq; NP_780300.2; NM_175091.3. [Q6PFX9-1]
DR PDB; 3UTM; X-ray; 2.00 A; A/B=308-655.
DR PDB; 4N4T; X-ray; 2.32 A; A/B=1097-1307.
DR PDB; 5HKP; X-ray; 2.20 A; A/B=308-655.
DR PDB; 6CF6; X-ray; 1.93 A; A/B=308-655.
DR PDBsum; 3UTM; -.
DR PDBsum; 4N4T; -.
DR PDBsum; 5HKP; -.
DR PDBsum; 6CF6; -.
DR AlphaFoldDB; Q6PFX9; -.
DR SMR; Q6PFX9; -.
DR BioGRID; 204263; 22.
DR DIP; DIP-61463N; -.
DR IntAct; Q6PFX9; 21.
DR MINT; Q6PFX9; -.
DR STRING; 10090.ENSMUSP00000033929; -.
DR BindingDB; Q6PFX9; -.
DR ChEMBL; CHEMBL3232702; -.
DR iPTMnet; Q6PFX9; -.
DR PhosphoSitePlus; Q6PFX9; -.
DR EPD; Q6PFX9; -.
DR MaxQB; Q6PFX9; -.
DR PaxDb; Q6PFX9; -.
DR PeptideAtlas; Q6PFX9; -.
DR PRIDE; Q6PFX9; -.
DR ProteomicsDB; 258936; -. [Q6PFX9-1]
DR ProteomicsDB; 258937; -. [Q6PFX9-2]
DR Antibodypedia; 22078; 383 antibodies from 36 providers.
DR DNASU; 21951; -.
DR Ensembl; ENSMUST00000033929; ENSMUSP00000033929; ENSMUSG00000031529. [Q6PFX9-1]
DR GeneID; 21951; -.
DR KEGG; mmu:21951; -.
DR UCSC; uc009lku.1; mouse. [Q6PFX9-1]
DR CTD; 8658; -.
DR MGI; MGI:1341087; Tnks.
DR VEuPathDB; HostDB:ENSMUSG00000031529; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000156161; -.
DR HOGENOM; CLU_004303_0_0_1; -.
DR InParanoid; Q6PFX9; -.
DR OMA; CPDGKRK; -.
DR OrthoDB; 111565at2759; -.
DR PhylomeDB; Q6PFX9; -.
DR TreeFam; TF326036; -.
DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR BioGRID-ORCS; 21951; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tnks; mouse.
DR PRO; PR:Q6PFX9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PFX9; protein.
DR Bgee; ENSMUSG00000031529; Expressed in manus and 231 other tissues.
DR ExpressionAtlas; Q6PFX9; baseline and differential.
DR Genevisible; Q6PFX9; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; ISO:MGI.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:1904743; P:negative regulation of telomeric DNA binding; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051225; P:spindle assembly; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 5.
DR IDEAL; IID50231; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR028731; TANK1.
DR PANTHER; PTHR24180:SF3; PTHR24180:SF3; 3.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 17.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; ANK repeat;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Cytoskeleton;
KW Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding; Mitosis;
KW mRNA transport; NAD; Nuclear pore complex; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Telomere;
KW Transferase; Translocation; Transport; Ubl conjugation;
KW Wnt signaling pathway; Zinc.
FT CHAIN 1..1320
FT /note="Poly [ADP-ribose] polymerase tankyrase-1"
FT /id="PRO_0000409511"
FT REPEAT 174..202
FT /note="ANK 1"
FT REPEAT 208..237
FT /note="ANK 2"
FT REPEAT 241..270
FT /note="ANK 3"
FT REPEAT 274..303
FT /note="ANK 4"
FT REPEAT 361..390
FT /note="ANK 5"
FT REPEAT 394..423
FT /note="ANK 6"
FT REPEAT 427..456
FT /note="ANK 7"
FT REPEAT 514..546
FT /note="ANK 8"
FT REPEAT 550..579
FT /note="ANK 9"
FT REPEAT 583..612
FT /note="ANK 10"
FT REPEAT 676..705
FT /note="ANK 11"
FT REPEAT 709..738
FT /note="ANK 12"
FT REPEAT 742..771
FT /note="ANK 13"
FT REPEAT 775..803
FT /note="ANK 14"
FT REPEAT 829..858
FT /note="ANK 15"
FT REPEAT 862..891
FT /note="ANK 16"
FT REPEAT 895..924
FT /note="ANK 17"
FT REPEAT 928..957
FT /note="ANK 18"
FT DOMAIN 1019..1082
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1105..1310
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT VAR_SEQ 1..344
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041320"
FT CONFLICT 969
FT /note="L -> V (in Ref. 1; BAC33475)"
FT /evidence="ECO:0000305"
FT CONFLICT 1025
FT /note="S -> I (in Ref. 1; BAC33475)"
FT /evidence="ECO:0000305"
FT HELIX 317..338
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:6CF6"
FT TURN 350..354
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 365..371
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 431..437
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 441..449
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 471..491
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:6CF6"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:6CF6"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 518..524
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 530..539
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 554..560
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 587..593
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 620..623
FT /evidence="ECO:0007829|PDB:6CF6"
FT HELIX 626..633
FT /evidence="ECO:0007829|PDB:6CF6"
FT STRAND 1100..1103
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1109..1120
FT /evidence="ECO:0007829|PDB:4N4T"
FT TURN 1126..1132
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1138..1147
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1149..1165
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1172..1177
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1182..1188
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1192..1194
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1203..1209
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1211..1215
FT /evidence="ECO:0007829|PDB:4N4T"
FT TURN 1216..1219
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1221..1223
FT /evidence="ECO:0007829|PDB:4N4T"
FT TURN 1228..1230
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1236..1238
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1240..1248
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1251..1256
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1269..1273
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1284..1288
FT /evidence="ECO:0007829|PDB:4N4T"
FT HELIX 1290..1292
FT /evidence="ECO:0007829|PDB:4N4T"
FT STRAND 1293..1303
FT /evidence="ECO:0007829|PDB:4N4T"
SQ SEQUENCE 1320 AA; 140944 MW; A90360DC665FFCC0 CRC64;
MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGPTPASPTA GGLAPFASPR
HGLALPEGDG SRDPPDRPRS PDPVDGAVCT VAAPAAVPAA SAAVGVAPTP AGGGGGGGNN
SASSASSPTS SSSSSPSSPG SSLAESPEAA GVGSTATLGA GAAGLGPGVP AVSGALRELL
EACRNGDVSR VKRLVDAANV NAKDMAGRKS SPLHFAAGFG RKDVVEHLLQ MGANVHARDD
GGLIPLHNAC SFGHAEVVSL LLCQGADPNA RDNWNYTPLH EAAIKGKIDV CIVLLQHGAD
PNIRNTDGKS ALDLADPSAK AVLTGEYKKD ELLEAARSGN EEKLMALLTP LNVNCHASDG
RKSTPLHLAA GYNRVRIVQL LLQHGADVHA KDKGGLVPLH NACSYGHYEV TELLLKHGAC
VNAMDLWQFT PLHEAASKNR VEVCSLLLSH GADPTLVNCH GKSAVDMAPT PELRERLTYE
FKGHSLLQAA READLAKVKK TLALEIINFK QPQSHETALH CAVASLHPKR KQVAELLLRK
GANVNEKNKD FMTPLHVAAE RAHNDVMEVL HKHGAKMNAL DSLGQTALHR AALAGHLQTC
RLLLSYGSDP SIISLQGFTA AQMGNEAVQQ ILSESTPMRT SDVDYRLLEA SKAGDLETVK
QLCSPQNVNC RDLEGRHSTP LHFAAGYNRV SVVEYLLHHG ADVHAKDKGG LVPLHNACSY
GHYEVAELLV RHGASVNVAD LWKFTPLHEA AAKGKYEICK LLLKHGADPT KKNRDGNTPL
DLVKEGDTDI QDLLRGDAAL LDAAKKGCLA RVQKLCTPEN INCRDTQGRN STPLHLAAGY
NNLEVAEYLL EHGADVNAQD KGGLIPLHNA ASYGHVDIAA LLIKYNTCVN ATDKWAFTPL
HEAAQKGRTQ LCALLLAHGA DPTMKNQEGQ TPLDLATADD IRALLIDAMP PEALPTCFKP
QATVVSASLI SPASTPSCLS AASSIDNLTG PLTDLAVGGA SNAGDGAAGA ERKEGEVAGL
DMNISQFLKS LGLEHLRDIF ETEQITLDVL ADMGHEELKE IGINAYGHRH KLIKGVERLL
GGQQGTNPYL TFHCVNQGTI LLDLAPEDKE YQSVEEEMQS TIREHRDGGN AGGIFNRYNV
IRIQKVVNKK LRERFCHRQK EVSEENHNHH NERMLFHGSP FINAIIHKGF DERHAYIGGM
FGAGIYFAEN SSKSNQYVYG IGGGTGCPTH KDRSCYICHR QMLFCRVTLG KSFLQFSTMK
MAHAPPGHHS VIGRPSVNGL AYAEYVIYRG EQAYPEYLIT YQIMKPEAPS QTATAAEQKT
