AQR_HUMAN
ID AQR_HUMAN Reviewed; 1485 AA.
AC O60306; A0JP17; A5YKK3; Q2YDX9; Q6IRU8; Q6PIC8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=RNA helicase aquarius {ECO:0000303|PubMed:25599396};
DE EC=3.6.4.13 {ECO:0000269|PubMed:25599396};
DE AltName: Full=Intron-binding protein of 160 kDa {ECO:0000303|PubMed:16949364};
DE Short=IBP160 {ECO:0000303|PubMed:16949364};
GN Name=AQR; Synonyms=KIAA0560;
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].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [5]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16949364; DOI=10.1016/j.molcel.2006.07.011;
RA Hirose T., Ideue T., Nagai M., Hagiwara M., Shu M.-D., Steitz J.A.;
RT "A spliceosomal intron binding protein, IBP160, links Position-dependent
RT assembly of intron-encoded box C/D snoRNP to pre-mRNA splicing.";
RL Mol. Cell 23:673-684(2006).
RN [6]
RP IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
RX PubMed=17981804; DOI=10.1074/jbc.m706647200;
RA Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y.,
RA Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.;
RT "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription,
RT and transcription-coupled repair.";
RL J. Biol. Chem. 283:940-950(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1051, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
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 [9]
RP IDENTIFICATION BY 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 [10] {ECO:0007744|PDB:4PJ3}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 19-1485 IN COMPLEX WITH ATP,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE IB COMPLEX,
RP MUTAGENESIS OF LYS-829 AND TYR-1196, DOMAIN, REGION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=25599396; DOI=10.1038/nsmb.2951;
RA De I., Bessonov S., Hofele R., dos Santos K., Will C.L., Urlaub H.,
RA Luhrmann R., Pena V.;
RT "The RNA helicase Aquarius exhibits structural adaptations mediating its
RT recruitment to spliceosomes.";
RL Nat. Struct. Mol. Biol. 22:138-144(2015).
RN [11] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [12] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:11991638, PubMed:25599396, PubMed:28502770, PubMed:28076346).
CC Intron-binding spliceosomal protein required to link pre-mRNA splicing
CC and snoRNP (small nucleolar ribonucleoprotein) biogenesis
CC (PubMed:16949364). Plays a key role in position-dependent assembly of
CC intron-encoded box C/D small snoRNP, splicing being required for snoRNP
CC assembly (PubMed:16949364). May act by helping the folding of the
CC snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent
CC manner, contacting the region between snoRNA and the branchpoint of
CC introns (40 nucleotides upstream of the branchpoint) during the late
CC stages of splicing (PubMed:16949364). Has ATP-dependent RNA helicase
CC activity and can unwind double-stranded RNA molecules with a 3'
CC overhang (in vitro) (PubMed:25599396). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:16949364, ECO:0000269|PubMed:25599396,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:25599396};
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC PubMed:16949364, PubMed:25599396, PubMed:28502770, PubMed:28076346).
CC Component of the XAB2 complex, a multimeric protein complex composed of
CC XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE (PubMed:17981804). Identified
CC in a pentameric intron-binding (IB) complex composed of AQR, XAB2,
CC ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a
CC preassembled complex (PubMed:25599396). The IB complex does not contain
CC PRPF19 (PubMed:25599396). Within the spliceosome, interacts with
CC SNRPA1, SF3B1, SF3B3, SF3A1 and SF3A2 (PubMed:25599396).
CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16949364,
CC ECO:0000269|PubMed:17981804, ECO:0000269|PubMed:25599396,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- INTERACTION:
CC O60306; Q9ULR0: ISY1; NbExp=6; IntAct=EBI-2512328, EBI-2557660;
CC O60306; Q9UNP9: PPIE; NbExp=9; IntAct=EBI-2512328, EBI-591818;
CC O60306; Q9HCS7: XAB2; NbExp=6; IntAct=EBI-2512328, EBI-295232;
CC O60306; Q96NB3: ZNF830; NbExp=11; IntAct=EBI-2512328, EBI-3920997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16949364}. Note=Localizes to speckle-like regions
CC of the nucleoplasm. {ECO:0000269|PubMed:16949364}.
CC -!- DOMAIN: Contains an N-terminal domain with structural similarity to ARM
CC repeat regions; this domain functions as scaffold for protein-protein
CC interactions, but is not required for RNA binding or for ATP-dependent
CC RNA helicase activity. {ECO:0000269|PubMed:25599396}.
CC -!- SIMILARITY: Belongs to the CWF11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25486.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011132; BAA25486.3; ALT_INIT; mRNA.
DR EMBL; EF553519; ABQ66265.1; -; mRNA.
DR EMBL; BC036913; AAH36913.1; -; mRNA.
DR EMBL; BC070379; AAH70379.1; -; mRNA.
DR EMBL; BC108262; AAI08263.1; -; mRNA.
DR EMBL; BC127111; AAI27112.1; -; mRNA.
DR EMBL; BC127112; AAI27113.1; -; mRNA.
DR CCDS; CCDS42013.1; -.
DR PIR; T00333; T00333.
DR RefSeq; NP_055506.1; NM_014691.2.
DR PDB; 4PJ3; X-ray; 2.30 A; A=19-1485.
DR PDB; 5MQF; EM; 5.90 A; U=1-1485.
DR PDB; 5XJC; EM; 3.60 A; Q=1-1485.
DR PDB; 5YZG; EM; 4.10 A; Q=1-1485.
DR PDB; 5Z56; EM; 5.10 A; Q=1-1485.
DR PDB; 5Z57; EM; 6.50 A; Q=1-1485.
DR PDB; 6FF7; EM; 4.50 A; U=1-1485.
DR PDB; 6ICZ; EM; 3.00 A; Q=1-1485.
DR PDB; 6ID0; EM; 2.90 A; Q=1-1485.
DR PDB; 6ID1; EM; 2.86 A; Q=1-1485.
DR PDB; 6QDV; EM; 3.30 A; U=1-1485.
DR PDB; 7A5P; EM; 5.00 A; U=1-1485.
DR PDB; 7ABI; EM; 8.00 A; U=1-1485.
DR PDBsum; 4PJ3; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; O60306; -.
DR SMR; O60306; -.
DR BioGRID; 115065; 176.
DR CORUM; O60306; -.
DR DIP; DIP-53576N; -.
DR IntAct; O60306; 82.
DR MINT; O60306; -.
DR STRING; 9606.ENSP00000156471; -.
DR GlyGen; O60306; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O60306; -.
DR MetOSite; O60306; -.
DR PhosphoSitePlus; O60306; -.
DR BioMuta; AQR; -.
DR EPD; O60306; -.
DR jPOST; O60306; -.
DR MassIVE; O60306; -.
DR MaxQB; O60306; -.
DR PaxDb; O60306; -.
DR PeptideAtlas; O60306; -.
DR PRIDE; O60306; -.
DR ProteomicsDB; 49333; -.
DR Antibodypedia; 53026; 95 antibodies from 20 providers.
DR DNASU; 9716; -.
DR Ensembl; ENST00000156471.10; ENSP00000156471.5; ENSG00000021776.11.
DR GeneID; 9716; -.
DR KEGG; hsa:9716; -.
DR MANE-Select; ENST00000156471.10; ENSP00000156471.5; NM_014691.3; NP_055506.1.
DR UCSC; uc001ziv.4; human.
DR CTD; 9716; -.
DR DisGeNET; 9716; -.
DR GeneCards; AQR; -.
DR HGNC; HGNC:29513; AQR.
DR HPA; ENSG00000021776; Low tissue specificity.
DR MIM; 610548; gene.
DR neXtProt; NX_O60306; -.
DR OpenTargets; ENSG00000021776; -.
DR PharmGKB; PA134869224; -.
DR VEuPathDB; HostDB:ENSG00000021776; -.
DR eggNOG; KOG1806; Eukaryota.
DR GeneTree; ENSGT00940000156668; -.
DR HOGENOM; CLU_001195_0_0_1; -.
DR InParanoid; O60306; -.
DR OMA; YQFIDVP; -.
DR OrthoDB; 867854at2759; -.
DR PhylomeDB; O60306; -.
DR TreeFam; TF105711; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; O60306; -.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O60306; -.
DR BioGRID-ORCS; 9716; 747 hits in 1078 CRISPR screens.
DR ChiTaRS; AQR; human.
DR GenomeRNAi; 9716; -.
DR Pharos; O60306; Tbio.
DR PRO; PR:O60306; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O60306; protein.
DR Bgee; ENSG00000021776; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; O60306; baseline and differential.
DR Genevisible; O60306; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032174; Aquarius_N.
DR InterPro; IPR026300; CWF11_fam.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF5; PTHR10887:SF5; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF16399; Aquarius_N; 1.
DR PIRSF; PIRSF038901; AQR_cwf11; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..1485
FT /note="RNA helicase aquarius"
FT /id="PRO_0000252389"
FT REGION 1..416
FT /note="Helical region with structural similarity to ARM
FT repeat domains"
FT /evidence="ECO:0000269|PubMed:25599396"
FT REGION 417..1485
FT /note="Required for assembly of the IB complex"
FT /evidence="ECO:0000269|PubMed:25599396"
FT REGION 1419..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 801
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25599396,
FT ECO:0007744|PDB:4PJ3"
FT BINDING 806
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25599396,
FT ECO:0007744|PDB:4PJ3"
FT BINDING 826..831
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25599396,
FT ECO:0007744|PDB:4PJ3"
FT MOD_RES 1051
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 829
FT /note="K->A: Decreased affinity for ATP and ADP. Loss of
FT RNA helicase activity. Disrupts spliceosomal pre-mRNA
FT splicing and leads to the accumulation of spliceosomal B
FT complexes."
FT /evidence="ECO:0000269|PubMed:25599396"
FT MUTAGEN 1196
FT /note="Y->A: Strongly reduced RNA helicase activity. No
FT effect on ATPase activity. No effect on spliceosomal pre-
FT mRNA splicing."
FT /evidence="ECO:0000269|PubMed:25599396"
FT CONFLICT 242
FT /note="V -> A (in Ref. 2; ABQ66265)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="Y -> F (in Ref. 2; ABQ66265)"
FT /evidence="ECO:0000305"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 53..58
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 244..261
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 323..344
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 400..411
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 462..491
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 509..522
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 547..553
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 561..567
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 583..587
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 589..601
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 620..629
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 631..644
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 666..678
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 685..691
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 697..700
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 721..727
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 731..736
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 745..750
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 775..781
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 804..814
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 815..822
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 829..843
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 849..854
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 856..866
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 894..918
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 929..938
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 940..951
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 961..966
FT /evidence="ECO:0007829|PDB:4PJ3"
FT TURN 969..976
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 987..1011
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1013..1016
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1020..1029
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1033..1038
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1039..1052
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1057..1063
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1064..1066
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1069..1073
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1074..1077
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1090..1095
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1108..1113
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1119..1126
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1141..1148
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1151..1153
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1158..1162
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1164..1166
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1173..1181
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1188..1191
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1201..1217
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1221..1223
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1224..1229
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1231..1244
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1257..1259
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1260..1263
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1268..1274
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1282..1285
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1287..1293
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1296..1305
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1307..1311
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1314..1316
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1317..1323
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1328..1332
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1343..1346
FT /evidence="ECO:0007829|PDB:4PJ3"
FT STRAND 1353..1355
FT /evidence="ECO:0007829|PDB:4PJ3"
FT HELIX 1358..1375
FT /evidence="ECO:0007829|PDB:4PJ3"
SQ SEQUENCE 1485 AA; 171295 MW; D0ADDA621A9418FD CRC64;
MAAPAQPKKI VAPTVSQINA EFVTQLACKY WAPHIKKKSP FDIKVIEDIY EKEIVKSRFA
IRKIMLLEFS QYLENYLWMN YSPEVSSKAY LMSICCMVNE KFRENVPAWE IFKKKPDHFP
FFFKHILKAA LAETDGEFSL HEQTVLLLFL DHCFNSLEVD LIRSQVQQLI SLPMWMGLQL
ARLELELKKT PKLRKFWNLI KKNDEKMDPE AREQAYQERR FLSQLIQKFI SVLKSVPLSE
PVTMDKVHYC ERFIELMIDL EALLPTRRWF NTILDDSHLL VHCYLSNLVR REEDGHLFSQ
LLDMLKFYTG FEINDQTGNA LTENEMTTIH YDRITSLQRA AFAHFPELYD FALSNVAEVD
TRESLVKFFG PLSSNTLHQV ASYLCLLPTL PKNEDTTFDK EFLLELLVSR HERRISQIQQ
LNQMPLYPTE KIIWDENIVP TEYYSGEGCL ALPKLNLQFL TLHDYLLRNF NLFRLESTYE
IRQDIEDSVS RMKPWQSEYG GVVFGGWARM AQPIVAFTVV EVAKPNIGEN WPTRVRADVT
INLNVRDHIK DEWEGLRKHD VCFLITVRPT KPYGTKFDRR RPFIEQVGLV YVRGCEIQGM
LDDKGRVIED GPEPRPNLRG ESRTFRVFLD PNQYQQDMTN TIQNGAEDVY ETFNIIMRRK
PKENNFKAVL ETIRNLMNTD CVVPDWLHDI ILGYGDPSSA HYSKMPNQIA TLDFNDTFLS
IEHLKASFPG HNVKVTVEDP ALQIPPFRIT FPVRSGKGKK RKDADVEDED TEEAKTLIVE
PHVIPNRGPY PYNQPKRNTI QFTHTQIEAI RAGMQPGLTM VVGPPGTGKT DVAVQIISNI
YHNFPEQRTL IVTHSNQALN QLFEKIMALD IDERHLLRLG HGEEELETEK DFSRYGRVNY
VLARRIELLE EVKRLQKSLG VPGDASYTCE TAGYFFLYQV MSRWEEYISK VKNKGSTLPD
VTEVSTFFPF HEYFANAPQP IFKGRSYEED MEIAEGCFRH IKKIFTQLEE FRASELLRSG
LDRSKYLLVK EAKIIAMTCT HAALKRHDLV KLGFKYDNIL MEEAAQILEI ETFIPLLLQN
PQDGFSRLKR WIMIGDHHQL PPVIKNMAFQ KYSNMEQSLF TRFVRVGVPT VDLDAQGRAR
ASLCNLYNWR YKNLGNLPHV QLLPEFSTAN AGLLYDFQLI NVEDFQGVGE SEPNPYFYQN
LGEAEYVVAL FMYMCLLGYP ADKISILTTY NGQKHLIRDI INRRCGNNPL IGRPNKVTTV
DRFQGQQNDY ILLSLVRTRA VGHLRDVRRL VVAMSRARLG LYIFARVSLF QNCFELTPAF
SQLTARPLHL HIIPTEPFPT TRKNGERPSH EVQIIKNMPQ MANFVYNMYM HLIQTTHHYH
QTLLQLPPAM VEEGEEVQNQ ETELETEEEA MTVQADIIPS PTDTSCRQET PAFQTDTTPS
ETGATSTPEA IPALSETTPT VVGAVSAPAE ANTPQDATSA PEETK
