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Q61655 (DD19A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase DDX19A

EC=3.6.4.13
Alternative name(s):
DEAD box RNA helicase DEAD5
Short name=mDEAD5
DEAD box protein 19A
Eukaryotic translation initiation factor 4A-related sequence 1
Gene names
Name:Ddx19a
Synonyms:Ddx19, Eif4a-rs1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Cytoplasm By similarity. Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Nuclear pore complex cytoplasmic fibrils.

Tissue specificity

Found in testis, heart, brain, liver, skeletal muscle, and kidney.

Domain

The N-terminal extension helix acts as an autoinhibitory domain, preventing ATP hydrolysis, unless the N-terminus of the protein is displaced by RNA binding, allowing cleft closure to bring key side chains into position for catalysis By similarity.

Sequence similarities

Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 478477ATP-dependent RNA helicase DDX19A
PRO_0000055023

Regions

Domain124 – 294171Helicase ATP-binding
Domain305 – 473169Helicase C-terminal
Nucleotide binding137 – 1448ATP By similarity
Region2 – 299298N-terminal lobe By similarity
Region54 – 6714N-terminal helix By similarity
Region300 – 478179C-terminal lobe By similarity
Motif91 – 11929Q motif
Motif241 – 2444DEAD box
Compositional bias48 – 536Poly-Glu

Sites

Binding site1181ATP By similarity
Binding site4281ATP By similarity
Binding site4311ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict30 – 323VKA → AKS in AAA53629. Ref.1
Sequence conflict262 – 2632ML → IV in AAA53629. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61655 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 46BDE331544EDA7E

FASTA47853,933
        10         20         30         40         50         60 
MATDSWALAV DEQEAAVKSM SSLQIKEEKV KADTNGVIKT STTAEKTEEE EKEDRAAQSL 

        70         80         90        100        110        120 
LNKLIRSNLV DNTNQVEVLQ RDPSSPLYSV KSFEELRLKP QLLQGVYAMG FNRPSKIQEN 

       130        140        150        160        170        180 
ALPMMLAEPP QNLIAQSQSG TGKTAAFVLA MLSRVEPADR YPQCLCLSPT YELALQTGKV 

       190        200        210        220        230        240 
IEQMGKFHPE LKLAYAVRGN KLERGQKVSE QIVIGTPGTV LDWCSKLKFI DPKKIKVFVL 

       250        260        270        280        290        300 
DEADVMIATQ GHQDQSIRIQ RMLPRNCQML LFSATFEDSV WKFAQKVVPD PNIIKLKREE 

       310        320        330        340        350        360 
ETLDTIKQYY VLCNNREEKF QALCNLYGAI TIAQAMIFCH TRKTASWLAA ELSKEGHQVA 

       370        380        390        400        410        420 
LLSGEMMVEQ RAAVIERFRE GKEKVLVTTN VCARGIDVEQ VSVVINFDLP VDKDGNPDNE 

       430        440        450        460        470 
TYLHRIGRTG RFGKRGLAVN MVDSKHSMNI LNRIQEHFNK KIERLDTDDL DEIEKIAN 

« Hide

References

« Hide 'large scale' references
[1]"Mouse erythroid cells express multiple putative RNA helicase genes exhibiting high sequence conservation from yeast to mammals."
Gee S.L., Conboy J.G.
Gene 140:171-177(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Erythroleukemia.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Stomach.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25125 mRNA. Translation: AAA53629.1.
AK049467 mRNA. Translation: BAC33762.1.
AK146548 mRNA. Translation: BAE27252.1.
CH466525 Genomic DNA. Translation: EDL11480.1.
BC011270 mRNA. Translation: AAH11270.1.
CCDSCCDS22668.1.
PIRI49731.
RefSeqNP_031942.2. NM_007916.2.
UniGeneMm.287901.

3D structure databases

ProteinModelPortalQ61655.
SMRQ61655. Positions 59-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199417. 2 interactions.
IntActQ61655. 1 interaction.

PTM databases

PhosphoSiteQ61655.

2D gel databases

REPRODUCTION-2DPAGEQ61655.

Proteomic databases

MaxQBQ61655.
PaxDbQ61655.
PRIDEQ61655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040416; ENSMUSP00000047898; ENSMUSG00000015023.
GeneID13680.
KEGGmmu:13680.
UCSCuc009nll.2. mouse.

Organism-specific databases

CTD55308.
MGIMGI:99526. Ddx19a.

Phylogenomic databases

eggNOGCOG0513.
GeneTreeENSGT00530000063236.
HOGENOMHOG000268797.
HOVERGENHBG107989.
InParanoidQ543M2.
OMAMMAINTI.
OrthoDBEOG7TMZRJ.
TreeFamTF314957.

Gene expression databases

BgeeQ61655.
CleanExMM_DDX19A.
GenevestigatorQ61655.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX19A. mouse.
NextBio284434.
PROQ61655.
SOURCESearch...

Entry information

Entry nameDD19A_MOUSE
AccessionPrimary (citable) accession number: Q61655
Secondary accession number(s): Q543M2, Q921R0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries