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Protein

ATPase Asna1

Gene

Asna1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741UniRule annotation
Binding sitei251 – 2511ATPUniRule annotation
Binding sitei278 – 2781ATPUniRule annotation
Metal bindingi289 – 2891Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi292 – 2921Zinc; shared with dimeric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 528ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-381038. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase Asna1UniRule annotation (EC:3.6.-.-UniRule annotation)
Alternative name(s):
Arsenical pump-driving ATPaseUniRule annotation
Arsenite-stimulated ATPaseUniRule annotation
Gene namesi
Name:Asna1
Synonyms:Arsa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1928379. Asna1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Endoplasmic reticulum UniRule annotation
  • Nucleusnucleolus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Disruption phenotypei

Causes early embryonic lethality.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 348347ATPase Asna1PRO_0000152254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO54984.
MaxQBiO54984.
PaxDbiO54984.
PRIDEiO54984.

2D gel databases

REPRODUCTION-2DPAGEO54984.

PTM databases

iPTMnetiO54984.
PhosphoSiteiO54984.

Expressioni

Gene expression databases

BgeeiO54984.
CleanExiMM_ARSA.
GenevisibleiO54984. MM.

Interactioni

Subunit structurei

Homodimer. Component of a transmembrane domain recognition complex (TRC). Interacts with SERP1 and SEC61B. Interacts with WRB.UniRule annotation

Protein-protein interaction databases

BioGridi208019. 8 interactions.
IntActiO54984. 6 interactions.
MINTiMINT-4088407.
STRINGi10090.ENSMUSP00000065337.

Structurei

3D structure databases

ProteinModelPortaliO54984.
SMRiO54984. Positions 27-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arsA ATPase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG2825. Eukaryota.
COG0003. LUCA.
GeneTreeiENSGT00390000003817.
HOGENOMiHOG000197637.
InParanoidiO54984.
KOiK01551.
OMAiYEIDTHN.
OrthoDBiEOG79W95W.
PhylomeDBiO54984.
TreeFamiTF300670.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_03112. Asna1_Get3.
InterProiIPR025723. Anion-transp_ATPase-like_dom.
IPR016300. ATPase_ArsA/GET3.
IPR027542. ATPase_ArsA/GET3_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10803. PTHR10803. 1 hit.
PfamiPF02374. ArsA_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00345. GET3_arsA_TRC40. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O54984-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK
60 70 80 90 100
TTCSCSLAVQ LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL
110 120 130 140 150
FAMEIDPSLG VAELPDEFFE EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE
160 170 180 190 200
VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP TIVERGLGRL MQIKNQISPF
210 220 230 240 250
ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE QTTFICVCIA
260 270 280 290 300
EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA
310 320 330 340
KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSTQ
Length:348
Mass (Da):38,823
Last modified:July 11, 2001 - v2
Checksum:iDA4EB4ACC35C7A36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039405 mRNA. Translation: AAB94772.2.
AF061177 Genomic DNA. Translation: AAD15826.2.
BC016453 mRNA. Translation: AAH16453.1.
BC083335 mRNA. Translation: AAH83335.1.
AK171690 mRNA. Translation: BAE42614.1.
CH466525 Genomic DNA. Translation: EDL10985.1.
CCDSiCCDS40417.1.
RefSeqiNP_062626.1. NM_019652.1.
UniGeneiMm.41475.

Genome annotation databases

EnsembliENSMUST00000064314; ENSMUSP00000065337; ENSMUSG00000052456.
GeneIDi56495.
KEGGimmu:56495.
UCSCiuc009mox.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039405 mRNA. Translation: AAB94772.2.
AF061177 Genomic DNA. Translation: AAD15826.2.
BC016453 mRNA. Translation: AAH16453.1.
BC083335 mRNA. Translation: AAH83335.1.
AK171690 mRNA. Translation: BAE42614.1.
CH466525 Genomic DNA. Translation: EDL10985.1.
CCDSiCCDS40417.1.
RefSeqiNP_062626.1. NM_019652.1.
UniGeneiMm.41475.

3D structure databases

ProteinModelPortaliO54984.
SMRiO54984. Positions 27-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208019. 8 interactions.
IntActiO54984. 6 interactions.
MINTiMINT-4088407.
STRINGi10090.ENSMUSP00000065337.

PTM databases

iPTMnetiO54984.
PhosphoSiteiO54984.

2D gel databases

REPRODUCTION-2DPAGEO54984.

Proteomic databases

EPDiO54984.
MaxQBiO54984.
PaxDbiO54984.
PRIDEiO54984.

Protocols and materials databases

DNASUi56495.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064314; ENSMUSP00000065337; ENSMUSG00000052456.
GeneIDi56495.
KEGGimmu:56495.
UCSCiuc009mox.1. mouse.

Organism-specific databases

CTDi439.
MGIiMGI:1928379. Asna1.

Phylogenomic databases

eggNOGiKOG2825. Eukaryota.
COG0003. LUCA.
GeneTreeiENSGT00390000003817.
HOGENOMiHOG000197637.
InParanoidiO54984.
KOiK01551.
OMAiYEIDTHN.
OrthoDBiEOG79W95W.
PhylomeDBiO54984.
TreeFamiTF300670.

Enzyme and pathway databases

ReactomeiR-MMU-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi312786.
PROiO54984.
SOURCEiSearch...

Gene expression databases

BgeeiO54984.
CleanExiMM_ARSA.
GenevisibleiO54984. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_03112. Asna1_Get3.
InterProiIPR025723. Anion-transp_ATPase-like_dom.
IPR016300. ATPase_ArsA/GET3.
IPR027542. ATPase_ArsA/GET3_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10803. PTHR10803. 1 hit.
PfamiPF02374. ArsA_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00345. GET3_arsA_TRC40. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization and chromosomal localization of the Asna1 gene, a mouse homologue of a bacterial arsenic-translocating ATPase gene."
    Bhattacharjee H., Ho Y.-S., Rosen B.P.
    Gene 272:291-299(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Salivary gland.
  3. "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: NOD.
    Tissue: Spleen.
  4. 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].
  5. "Targeted disruption of the mouse Asna1 gene results in embryonic lethality."
    Mukhopadhyay R., Ho Y.S., Swiatek P.J., Rosen B.P., Bhattacharjee H.
    FEBS Lett. 580:3889-3894(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 66-86; 157-185 AND 261-267, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiASNA_MOUSE
AccessioniPrimary (citable) accession number: O54984
Secondary accession number(s): Q3TAQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 11, 2001
Last modified: April 13, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.