DHX15_PONAB
ID DHX15_PONAB Reviewed; 795 AA.
AC Q5RAZ4; Q5NVD9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase DHX15 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O43143};
DE AltName: Full=DEAH box protein 15;
GN Name=DHX15 {ECO:0000250|UniProtKB:O43143};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase involved in mRNA processing and antiviral innate
CC immunity. Pre-mRNA processing factor involved in disassembly of
CC spliceosomes after the release of mature mRNA. In cooperation with
CC TFIP11 seem to be involved in the transition of the U2, U5 and U6
CC snRNP-containing IL complex to the snRNP-free IS complex leading to
CC efficient debranching and turnover of excised introns. Plays a key role
CC in antiviral innate immunity by promoting both MAVS-dependent signaling
CC and NLRP6 inflammasome. Acts as an RNA virus sensor: recognizes and
CC binds viral double stranded RNA (dsRNA) and activates the MAVS-
CC dependent signaling to produce interferon-beta and interferon lambda-3
CC (IFNL3). Involved in intestinal antiviral innate immunity together with
CC NLRP6: recognizes and binds viral dsRNA and promotes activation of the
CC NLRP6 inflammasome in intestinal epithelial cells to restrict infection
CC by enteric viruses. The NLRP6 inflammasome acts by promoting maturation
CC and secretion of IL18 in the extracellular milieu (By similarity). Also
CC involved in antibacterial innate immunity by promoting Wnt-induced
CC antimicrobial protein expression in Paneth cells (By similarity).
CC {ECO:0000250|UniProtKB:O35286, ECO:0000250|UniProtKB:O43143}.
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:0000250|UniProtKB:O43143};
CC -!- ACTIVITY REGULATION: ATPase activity is enhanced upon binding to G-
CC patch domain-containing proteins. G-patch domain-containing proteins
CC act like a brace that tethers mobile sections of DHX15 together,
CC stabilizing a functional conformation with high RNA affinity, thereby
CC promoting the ATPase activity. {ECO:0000250|UniProtKB:O43143}.
CC -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC spliceosome. Identified in the Intron Large spliceosome complex (IL,
CC also named intron lariat spliceosome), a post-mRNA release spliceosomal
CC complex containing the excised intron, U2, U5 and U6 snRNPs, and
CC splicing factors; the association may be transient. The IL complex
CC exists in two distinct conformations, one with the DHX15 (ILS2) and one
CC without (ILS1). Interacts with TFIP11 (via G-patch domain); indicative
CC for a recruitment to the IL complex. Interacts with SSB/La. Interacts
CC with GPATCH2 (via G-patch domain); promoting the RNA helicase activity.
CC Interacts with NKRF (via G-patch domain); promoting the RNA helicase
CC activity. Interacts with NLRP6. {ECO:0000250|UniProtKB:O43143}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43143}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:O43143}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX15/PRP43 sub-subfamily. {ECO:0000305}.
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DR EMBL; CR858867; CAH91066.1; -; mRNA.
DR EMBL; CR926098; CAI29724.1; -; mRNA.
DR RefSeq; NP_001127370.1; NM_001133898.1.
DR AlphaFoldDB; Q5RAZ4; -.
DR SMR; Q5RAZ4; -.
DR STRING; 9601.ENSPPYP00000016358; -.
DR Ensembl; ENSPPYT00000017023; ENSPPYP00000016358; ENSPPYG00000014641.
DR GeneID; 100174435; -.
DR KEGG; pon:100174435; -.
DR CTD; 1665; -.
DR eggNOG; KOG0925; Eukaryota.
DR GeneTree; ENSGT00940000155800; -.
DR InParanoid; Q5RAZ4; -.
DR OrthoDB; 354219at2759; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IEA:Ensembl.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd17973; DEXHc_DHX15; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; Immunity; Innate immunity;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..795
FT /note="ATP-dependent RNA helicase DHX15"
FT /id="PRO_0000260306"
FT DOMAIN 147..313
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 338..518
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 260..263
FT /note="DEAH box"
FT COMPBIAS 1..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43143"
FT MOD_RES 488
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43143"
FT CROSSLNK 786
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43143"
FT CONFLICT 312
FT /note="I -> S (in Ref. 1; CAH91066)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="S -> L (in Ref. 1; CAH91066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 90903 MW; A42153D15A1E404C CRC64;
MSKRHRLDLG EDYPSGKKRA GTDGKDRDRD RDREDRSKDR DRERDRGDRE REREKEKEKE
LRASTNAMLI SAGLPPLKAS HSAHSTHSAH SAHSTHSAHS THAGHAGHTS LPQCINPFTN
LPHTPRYYDI LKKRLQLPVW EYKDRFTDIL VRHQSFVLVG ETGSGKTTQI PQWCVEYMRS
LPGPKRGVAC TQPRRVAAMS VAQRVADEMD VMLGQEVGYS IRFEDCSSAK TILKYMTDGM
LLREAMNDPL LERYGVIILD EAHERTLATD ILMGVLKEVV RQRSDLKVIV MSATLDAGKF
QIYFDNCPLL TIPGRTHPVE IFYTPEPERD YLEAAIRTVI QIHMCEEEEG DLLLFLTGQE
EIDEACKRIK REVDDLGPEV GDIKIIPLYS TLPPQQQQRI FEPPPPKKQN GAIGRKVVVS
TNIAETSLTI DGVVFVIDPG FAKQKVYNPR IRVESLLVTA ISKASAQQRA GRAGRTRPGK
CFRLYTEKAY KTEMQDNTYP EILRSNLGSV VLQLKKLGID DLVHFDFMDP PAPETLMRAL
ELLNYLAALN DDGDLTELGS MMAEFPLDPQ LAKMVIASCD YNCSNEVLSI TAMLSVPQCF
VRPTEAKKAA DEAKMRFAHI DGDHLTLLNV YHAFKQNHES VQWCYDNFIN YRSLMSADNV
RQQLSRIMDR FNLPRRSTDF TSRDYYINIR KALVTGYFMQ VAHLERTGHY LTVKDNQVVQ
LHPSTVLDHK PEWVLYNEFV LTTKNYIRTC TDIKPEWLVK IAPQYYDMSN FPQCEAKRQL
DRIIAKLQSK EYSQY
