Q61655 (DD19A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › nuclear 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.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Cytoplasm Membrane Nuclear pore complex Nucleus
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	induction of apoptosis Inferred from electronic annotation. Source: Compara mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW response to zinc ion Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 478	478	ATP-dependent RNA helicase DDX19A		PRO_0000055023
Regions
	Domain	124 – 294	171	Helicase ATP-binding
	Domain	305 – 473	169	Helicase C-terminal
	Nucleotide binding	137 – 144	8	ATP By similarity
	Region	1 – 299	299	N-terminal lobe By similarity
	Region	54 – 67	14	N-terminal helix By similarity
	Region	300 – 478	179	C-terminal lobe By similarity
	Motif	91 – 119	29	Q motif
	Motif	241 – 244	4	DEAD box
	Compositional bias	48 – 53	6	Poly-Glu
Sites
	Binding site	118	1	ATP By similarity
	Binding site	428	1	ATP By similarity
	Binding site	431	1	ATP By similarity
Experimental info
	Sequence conflict	30 – 32	3	VKA → AKS in AAA53629. Ref.1
	Sequence conflict	262 – 263	2	ML → IV in AAA53629. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q61655 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 46BDE331544EDA7E	FASTA	478	53,933
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00123651.
PIR	I49731.
RefSeq	NP_031942.2. NM_007916.2.
UniGene	Mm.287901.
3D structure databases
ProteinModelPortal	Q61655.
SMR	Q61655. Positions 59-466.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61655. 1 interaction.
PTM databases
PhosphoSite	Q61655.
2D gel databases
REPRODUCTION-2DPAGE	Q61655.
Proteomic databases
PaxDb	Q61655.
PRIDE	Q61655.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000040416; ENSMUSP00000047898; ENSMUSG00000015023.
GeneID	13680.
KEGG	mmu:13680.
Organism-specific databases
CTD	55308.
MGI	MGI:99526. Ddx19a.
Phylogenomic databases
eggNOG	COG0513.
GeneTree	ENSGT00530000063236.
HOGENOM	HOG000268797.
HOVERGEN	HBG107989.
InParanoid	Q543M2.
OMA	PQAICLA.
OrthoDB	EOG46MBJK.
Gene expression databases
Bgee	Q61655.
CleanEx	MM_DDX19A.
Genevestigator	Q61655.
GermOnline	ENSMUSG00000015023. Mus musculus.
Family and domain databases
InterPro	IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR014014. RNA_helicase_DEAD_Q_motif. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF00271. Helicase_C. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS00039. DEAD_ATP_HELICASE. False negative. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51195. Q_MOTIF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DDX19A. mouse.
NextBio	284434.
SOURCE	Search...

Entry information

Entry name

DD19A_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program