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ATPase Cre-asna-1 (EC 3.6.-.-) (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase)

 E3NC86_CAERE            Unreviewed;       342 AA.
E3NC86;
11-JAN-2011, integrated into UniProtKB/TrEMBL.
11-JAN-2011, sequence version 1.
25-OCT-2017, entry version 56.
RecName: Full=ATPase Cre-asna-1 {ECO:0000256|HAMAP-Rule:MF_03112};
EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_03112};
AltName: Full=Arsenical pump-driving ATPase {ECO:0000256|HAMAP-Rule:MF_03112};
AltName: Full=Arsenite-stimulated ATPase {ECO:0000256|HAMAP-Rule:MF_03112};
Name=Cre-asna-1 {ECO:0000313|EMBL:EFO92668.1};
Synonyms=asna-1 {ECO:0000256|HAMAP-Rule:MF_03112};
ORFNames=CRE_16340 {ECO:0000313|EMBL:EFO92668.1};
Caenorhabditis remanei (Caenorhabditis vulgaris).
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
[1] {ECO:0000313|Proteomes:UP000008281}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
Caenorhabditis remanei Sequencing Consortium;
Wilson R.K.;
"PCAP assembly of the Caenorhabditis remanei genome.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
-!- 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. {ECO:0000256|HAMAP-
Rule:MF_03112}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846957}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03112}.
Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03112}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000256|SAAS:SAAS00846961}.
-!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000256|HAMAP-
Rule:MF_03112, ECO:0000256|SAAS:SAAS00846955}.
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EMBL; DS268593; EFO92668.1; -; Genomic_DNA.
RefSeq; XP_003093975.1; XM_003093927.1.
STRING; 31234.CRE16340; -.
EnsemblMetazoa; CRE16340; CRE16340; WBGene00070702.
GeneID; 9811693; -.
CTD; 9811693; -.
eggNOG; KOG2825; Eukaryota.
eggNOG; COG0003; LUCA.
InParanoid; E3NC86; -.
OMA; DQIADLY; -.
OrthoDB; EOG091G0CAR; -.
Proteomes; UP000008281; Unassembled WGS sequence.
GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IEA:EnsemblMetazoa.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0016887; F:ATPase activity; IEA:EnsemblMetazoa.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071722; P:detoxification of arsenic-containing substance; IEA:EnsemblMetazoa.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:EnsemblMetazoa.
GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
CDD; cd02035; ArsA; 1.
HAMAP; MF_03112; Asna1_Get3; 1.
InterPro; IPR025723; Anion-transp_ATPase-like_dom.
InterPro; IPR016300; ATPase_ArsA/GET3.
InterPro; IPR027542; ATPase_ArsA/GET3_euk.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10803; PTHR10803; 1.
PANTHER; PTHR10803:SF3; PTHR10803:SF3; 1.
Pfam; PF02374; ArsA_ATPase; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846966};
Complete proteome {ECO:0000313|Proteomes:UP000008281};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846962};
Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03112};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846968};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846954};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846966};
Reference proteome {ECO:0000313|Proteomes:UP000008281};
Transport {ECO:0000256|HAMAP-Rule:MF_03112,
ECO:0000256|SAAS:SAAS00846958};
Zinc {ECO:0000256|HAMAP-Rule:MF_03112, ECO:0000256|SAAS:SAAS00846960}.
DOMAIN 19 336 ArsA_ATPase. {ECO:0000259|Pfam:PF02374}.
NP_BIND 26 33 ATP. {ECO:0000256|HAMAP-Rule:MF_03112}.
ACT_SITE 55 55 {ECO:0000256|HAMAP-Rule:MF_03112}.
METAL 286 286 Zinc; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_03112}.
METAL 289 289 Zinc; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_03112}.
BINDING 244 244 ATP. {ECO:0000256|HAMAP-Rule:MF_03112}.
BINDING 271 271 ATP. {ECO:0000256|HAMAP-Rule:MF_03112}.
SEQUENCE 342 AA; 37684 MW; AFC8D9A94038D140 CRC64;
MSDQLEGSIK NVLEQKSLKW IFVGGKGGVG KTTCSCSLAA QLSKVRERVL LISTDPAHNI
SDAFCQKFTK TPTLVEGFEN LFAMEIDSNP SGEGVEMANI EEMLQNAAQN ESGSGGGFAM
GKDLLQSFAG GLPGIDEAMS FGEMMKLIDS LDFDVVVFDT APTGHTLRLL QFPTLLEKVF
TKILSLQGMF GPMLNQFGGM FGMGGGSINE MIEKMTTTLE SVKKMNAQFK DPEVTTFVCV
CIAEFLSLYE TERLIQELTK QGIDTHNIIV NQLLFPDTDE NGKVTCRKCG SRQAIQSKYL
SEIDELYEDF HVVKLPLLET EVRGGPEILK FSERMVHPEK NN


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