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O43681 (ASNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATPase ASNA1

EC=3.6.-.-
Alternative name(s):
Arsenical pump-driving ATPase
Arsenite-stimulated ATPase
Transmembrane domain recognition complex 40 kDa ATPase subunit
hARSA-I
hASNA-I
Gene names
Name:ASNA1
Synonyms:ARSA, TRC40
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. May be involved in insulin signaling. Ref.12 Ref.13

Subunit structure

Homodimer By similarity. Component of a transmembrane domain recognition complex (TRC) By similarity. Interacts with SERP1 and SEC61B By similarity. Interacts with WRB. Ref.12 Ref.13 Ref.16

Subcellular location

Cytoplasm. Endoplasmic reticulum. Nucleusnucleolus Ref.10 Ref.12 Ref.16.

Tissue specificity

Expressed in the epithelial cells of the liver, kidney, and stomach wall, in the adrenal medulla, in the islet cells of the pancreas, in the red pulp of the spleen, and in cardiac and skeletal muscle. Ref.11

Sequence similarities

Belongs to the arsA ATPase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.22 mM for ATP Ref.9

Vmax=16.6 nmol/min/mg enzyme for ATP

Sequence caution

The sequence AAC50731.1 differs from that shown. Reason: Frameshift at position 19.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 348347ATPase ASNA1 HAMAP-Rule MF_03112
PRO_0000152253

Regions

Nucleotide binding45 – 528ATP By similarity

Sites

Active site741 By similarity
Metal binding2891Zinc; shared with dimeric partner By similarity
Metal binding2921Zinc; shared with dimeric partner By similarity
Binding site2511ATP By similarity
Binding site2781ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.14

Natural variations

Natural variant3321N → S. Ref.4
Corresponds to variant rs8177499 [ dbSNP | Ensembl ].
VAR_018844

Experimental info

Mutagenesis461G → R: Abolishes ATPase activity, dominantly inhibits the TA protein insertion pathway. Ref.12
Sequence conflict113 – 1142EL → DV in AAC50731. Ref.8
Sequence conflict2051C → F in AAC03551. Ref.1
Sequence conflict3031L → P in BAD97083. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O43681 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: DA52C4ACC35C7A36

FASTA34838,793
        10         20         30         40         50         60 
MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK TTCSCSLAVQ 

        70         80         90        100        110        120 
LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL FAMEIDPSLG VAELPDEFFE 

       130        140        150        160        170        180 
EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP 

       190        200        210        220        230        240 
TIVERGLGRL MQIKNQISPF ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE 

       250        260        270        280        290        300 
QTTFICVCIA EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA 

       310        320        330        340 
KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSAQ 

« Hide

References

« Hide 'large scale' references
[1]"Human homolog of bacterial and mouse arsenite translocating ATPase gene, ArsA."
Hu G.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Salivary gland.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[4]NIEHS SNPs program
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-332.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Uterus.
[8]"Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter."
Kurdi-Haidar B., Aebi S., Heath D., Enns R.E., Naredi P., Hom D.K., Howell S.B.
Genomics 36:486-491(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-348.
[9]"Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I)."
Kurdi-Haidar B., Heath D., Aebi S., Howell S.B.
J. Biol. Chem. 273:22173-22176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[10]"Dual cytoplasmic and nuclear distribution of the novel arsenite-stimulated human ATPase (hASNA-I)."
Kurdi-Haidar B., Hom D.K., Flittner D.E., Heath D., Fink L., Naredi P., Howell S.B.
J. Cell. Biochem. 71:1-10(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Immunohistochemical analysis of the distribution of the human ATPase (hASNA-I) in normal tissues and its overexpression in breast adenomas and carcinomas."
Kurdi-Haidar B., Heath D., Naredi P., Varki N., Howell S.B.
J. Histochem. Cytochem. 46:1243-1248(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Identification of a targeting factor for posttranslational membrane protein insertion into the ER."
Stefanovic S., Hegde R.S.
Cell 128:1147-1159(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE TRC COMPLEX, MUTAGENESIS OF GLY-46, SUBCELLULAR LOCATION, INTERACTION WITH SEC61B.
[13]"Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins."
Favaloro V., Spasic M., Schwappach B., Dobberstein B.
J. Cell Sci. 121:1832-1840(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SERP1 AND SEC61B.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored proteins into the ER membrane."
Vilardi F., Lorenz H., Dobberstein B.
J. Cell Sci. 124:1301-1307(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WRB, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF047469 mRNA. Translation: AAC03551.1.
AK291855 mRNA. Translation: BAF84544.1.
AK223363 mRNA. Translation: BAD97083.1.
AY304483 Genomic DNA. Translation: AAP45050.1.
AC018761 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84303.1.
BC002651 mRNA. Translation: AAH02651.1.
U60276 mRNA. Translation: AAC50731.1. Frameshift.
RefSeqNP_004308.2. NM_004317.2.
UniGeneHs.465985.

3D structure databases

ProteinModelPortalO43681.
SMRO43681. Positions 27-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106931. 18 interactions.
IntActO43681. 8 interactions.
MINTMINT-4656878.
STRING9606.ENSP00000349887.

Chemistry

DrugBankDB00171. Adenosine triphosphate.

Protein family/group databases

TCDB3.A.19.1.1. the tms recognition/insertion complex (trc) family.

PTM databases

PhosphoSiteO43681.

2D gel databases

OGPO43681.

Proteomic databases

PaxDbO43681.
PRIDEO43681.

Protocols and materials databases

DNASU439.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357332; ENSP00000349887; ENSG00000198356.
ENST00000591090; ENSP00000466379; ENSG00000198356.
GeneID439.
KEGGhsa:439.
UCSCuc002muv.3. human.

Organism-specific databases

CTD439.
GeneCardsGC19P012848.
HGNCHGNC:752. ASNA1.
HPAHPA045951.
HPA048087.
MIM601913. gene.
neXtProtNX_O43681.
PharmGKBPA25051.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0003.
HOGENOMHOG000197637.
InParanoidO43681.
KOK01551.
OMAIPEEMSI.
OrthoDBEOG79W95W.
PhylomeDBO43681.

Gene expression databases

ArrayExpressO43681.
BgeeO43681.
CleanExHS_ARSA.
HS_ASNA1.
GenevestigatorO43681.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_03112. Asna1_Get3.
InterProIPR025723. Anion-transp_ATPase-like_dom.
IPR016300. ATPase_ArsA/GET3.
IPR027542. ATPase_ArsA/GET3_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10803. PTHR10803. 1 hit.
PfamPF02374. ArsA_ATPase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00345. GET3_arsA_TRC40. 1 hit.
ProtoNetSearch...

Other

ChiTaRSASNA1. human.
GeneWikiASNA1.
GenomeRNAi439.
NextBio1839.
PROO43681.
SOURCESearch...

Entry information

Entry nameASNA_HUMAN
AccessionPrimary (citable) accession number: O43681
Secondary accession number(s): A6NHP8 expand/collapse secondary AC list , A8K740, Q53FC6, Q92849
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM