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O43681

- ASNA_HUMAN

UniProt

O43681 - ASNA_HUMAN

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Protein

ATPase ASNA1

Gene

ASNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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 (By similarity). May be involved in insulin signaling.2 PublicationsUniRule annotation

Kineticsi

  1. KM=0.22 mM for ATP1 Publication

Vmax=16.6 nmol/min/mg enzyme for ATP1 Publication

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

  1. arsenite transmembrane transporter activity Source: ProtInc
  2. ATPase activity Source: InterPro
  3. ATP binding Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW
  5. transporter activity Source: ProtInc

GO - Biological processi

  1. inorganic anion transport Source: GOC
  2. protein insertion into ER membrane Source: UniProtKB-HAMAP
  3. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

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

Protein family/group databases

TCDBi3.A.19.1.1. the tms recognition/insertion complex (trc) family.

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
Transmembrane domain recognition complex 40 kDa ATPase subunit
hARSA-I
hASNA-I
Gene namesi
Name:ASNA1UniRule annotation
Synonyms:ARSA, TRC40
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:752. ASNA1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. endoplasmic reticulum Source: UniProtKB-HAMAP
  3. extracellular vesicular exosome Source: UniProt
  4. nucleolus Source: HPA
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461G → R: Abolishes ATPase activity, dominantly inhibits the TA protein insertion pathway. 1 Publication

Organism-specific databases

PharmGKBiPA25051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 348347ATPase ASNA1PRO_0000152253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43681.
PaxDbiO43681.
PRIDEiO43681.

2D gel databases

OGPiO43681.

PTM databases

PhosphoSiteiO43681.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO43681.
CleanExiHS_ARSA.
HS_ASNA1.
ExpressionAtlasiO43681. baseline and differential.
GenevestigatoriO43681.

Organism-specific databases

HPAiHPA045951.
HPA048087.

Interactioni

Subunit structurei

Homodimer (By similarity). Component of a transmembrane domain recognition complex (TRC) (By similarity). Interacts with SERP1 and SEC61B (By similarity). Interacts with WRB.3 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi106931. 26 interactions.
IntActiO43681. 9 interactions.
MINTiMINT-4656878.
STRINGi9606.ENSP00000349887.

Structurei

3D structure databases

ProteinModelPortaliO43681.
SMRiO43681. Positions 27-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arsA ATPase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0003.
GeneTreeiENSGT00390000003817.
HOGENOMiHOG000197637.
InParanoidiO43681.
KOiK01551.
OMAiMYRYLTV.
OrthoDBiEOG79W95W.
PhylomeDBiO43681.

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.

O43681-1 [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 PYKPPSAQ
Length:348
Mass (Da):38,793
Last modified:May 30, 2000 - v2
Checksum:iDA52C4ACC35C7A36
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1142EL → DV in AAC50731. (PubMed:8884272)Curated
Sequence conflicti205 – 2051C → F in AAC03551. 1 PublicationCurated
Sequence conflicti303 – 3031L → P in BAD97083. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti332 – 3321N → S.1 Publication
Corresponds to variant rs8177499 [ dbSNP | Ensembl ].
VAR_018844

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32920.1.
RefSeqiNP_004308.2. NM_004317.2.
UniGeneiHs.465985.

Genome annotation databases

EnsembliENST00000357332; ENSP00000349887; ENSG00000198356.
ENST00000591090; ENSP00000466379; ENSG00000198356.
GeneIDi439.
KEGGihsa:439.
UCSCiuc002muv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS32920.1.
RefSeqi NP_004308.2. NM_004317.2.
UniGenei Hs.465985.

3D structure databases

ProteinModelPortali O43681.
SMRi O43681. Positions 27-342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106931. 26 interactions.
IntActi O43681. 9 interactions.
MINTi MINT-4656878.
STRINGi 9606.ENSP00000349887.

Chemistry

DrugBanki DB00171. Adenosine triphosphate.

Protein family/group databases

TCDBi 3.A.19.1.1. the tms recognition/insertion complex (trc) family.

PTM databases

PhosphoSitei O43681.

2D gel databases

OGPi O43681.

Proteomic databases

MaxQBi O43681.
PaxDbi O43681.
PRIDEi O43681.

Protocols and materials databases

DNASUi 439.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357332 ; ENSP00000349887 ; ENSG00000198356 .
ENST00000591090 ; ENSP00000466379 ; ENSG00000198356 .
GeneIDi 439.
KEGGi hsa:439.
UCSCi uc002muv.3. human.

Organism-specific databases

CTDi 439.
GeneCardsi GC19P012848.
HGNCi HGNC:752. ASNA1.
HPAi HPA045951.
HPA048087.
MIMi 601913. gene.
neXtProti NX_O43681.
PharmGKBi PA25051.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0003.
GeneTreei ENSGT00390000003817.
HOGENOMi HOG000197637.
InParanoidi O43681.
KOi K01551.
OMAi MYRYLTV.
OrthoDBi EOG79W95W.
PhylomeDBi O43681.

Miscellaneous databases

ChiTaRSi ASNA1. human.
GeneWikii ASNA1.
GenomeRNAii 439.
NextBioi 1839.
PROi O43681.
SOURCEi Search...

Gene expression databases

Bgeei O43681.
CleanExi HS_ARSA.
HS_ASNA1.
ExpressionAtlasi O43681. baseline and differential.
Genevestigatori O43681.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
HAMAPi MF_03112. Asna1_Get3.
InterProi IPR025723. Anion-transp_ATPase-like_dom.
IPR016300. ATPase_ArsA/GET3.
IPR027542. ATPase_ArsA/GET3_euk.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10803. PTHR10803. 1 hit.
Pfami PF02374. ArsA_ATPase. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00345. GET3_arsA_TRC40. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiASNA_HUMAN
AccessioniPrimary (citable) accession number: O43681
Secondary accession number(s): A6NHP8
, A8K740, Q53FC6, Q92849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3