GenomeNet

Database: UniProt
Entry: O60306
LinkDB: O60306
Original site: O60306 
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   29-SEP-2021, entry version 157.
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};
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; 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   SMR; O60306; -.
DR   BioGRID; 115065; 142.
DR   CORUM; O60306; -.
DR   DIP; DIP-53576N; -.
DR   IntAct; O60306; 75.
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; 82 antibodies.
DR   DNASU; 9716; -.
DR   Ensembl; ENST00000156471; ENSP00000156471; ENSG00000021776.
DR   GeneID; 9716; -.
DR   KEGG; hsa:9716; -.
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; GYFNTVY; -.
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   BioGRID-ORCS; 9716; 743 hits in 1020 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 intestine and 236 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:0140603; 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; -; 1.
DR   InterPro; IPR032174; Aquarius_N.
DR   InterPro; IPR026300; CWF11_fam.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR027417; P-loop_NTPase.
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   NP_BIND         826..831
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:25599396,
FT                   ECO:0007744|PDB:4PJ3"
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                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:25599396,
FT                   ECO:0007744|PDB:4PJ3"
FT   BINDING         806
FT                   /note="ATP"
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
//
DBGET integrated database retrieval system