ASNA_CAEEL
ID ASNA_CAEEL Reviewed; 342 AA.
AC P30632;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ATPase asna-1 {ECO:0000255|HAMAP-Rule:MF_03112};
DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenical pump-driving ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenite-stimulated ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
GN Name=asna-1 {ECO:0000255|HAMAP-Rule:MF_03112}; Synonyms=tag-205;
GN ORFNames=ZK637.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1538779; DOI=10.1038/356037a0;
RA Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA Waterston R.;
RT "The C. elegans genome sequencing project: a beginning.";
RL Nature 356:37-41(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=17289575; DOI=10.1016/j.cell.2006.12.031;
RA Kao G., Nordenson C., Still M., Roennlund A., Tuck S., Naredi P.;
RT "ASNA-1 positively regulates insulin secretion in C. elegans and mammalian
RT cells.";
RL Cell 128:577-587(2007).
CC -!- FUNCTION: ATPase required for the post-translational delivery of tail-
CC anchored (TA) proteins to the endoplasmic reticulum. Recognizes and
CC selectively binds the transmembrane domain of TA proteins in the
CC cytosol. This complex then targets to the endoplasmic reticulum by
CC membrane-bound receptors, where the tail-anchored protein is released
CC for insertion. This process is regulated by ATP binding and hydrolysis.
CC ATP binding drives the homodimer towards the closed dimer state,
CC facilitating recognition of newly synthesized TA membrane proteins. ATP
CC hydrolysis is required for insertion. Subsequently, the homodimer
CC reverts towards the open dimer state, lowering its affinity for the
CC membrane-bound receptor, and returning it to the cytosol to initiate a
CC new round of targeting (By similarity). May be involved in insulin
CC signaling. {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:17289575}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- INTERACTION:
CC P30632; Q19824: cee-1; NbExp=3; IntAct=EBI-318697, EBI-320572;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}.
CC Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
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DR EMBL; Z11115; CAA77452.1; -; Genomic_DNA.
DR PIR; S15791; S15791.
DR RefSeq; NP_498965.1; NM_066564.3.
DR AlphaFoldDB; P30632; -.
DR SMR; P30632; -.
DR BioGRID; 41455; 22.
DR DIP; DIP-26718N; -.
DR IntAct; P30632; 16.
DR STRING; 6239.ZK637.5; -.
DR EPD; P30632; -.
DR PaxDb; P30632; -.
DR PeptideAtlas; P30632; -.
DR EnsemblMetazoa; ZK637.5.1; ZK637.5.1; WBGene00014025.
DR GeneID; 176254; -.
DR KEGG; cel:CELE_ZK637.5; -.
DR CTD; 176254; -.
DR WormBase; ZK637.5; CE00436; WBGene00014025; asna-1.
DR eggNOG; KOG2825; Eukaryota.
DR GeneTree; ENSGT00390000003817; -.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; P30632; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR PhylomeDB; P30632; -.
DR BRENDA; 7.3.2.7; 1045.
DR PRO; PR:P30632; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00014025; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0043529; C:GET complex; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071722; P:detoxification of arsenic-containing substance; IMP:WormBase.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:WormBase.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISS:WormBase.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03112; Asna1_Get3; 1.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR016300; ATPase_ArsA/GET3.
DR InterPro; IPR027542; ATPase_ArsA/GET3_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10803; PTHR10803; 1.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..342
FT /note="ATPase asna-1"
FT /id="PRO_0000152255"
FT ACT_SITE 55
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ SEQUENCE 342 AA; 37554 MW; 5278E924425E18C9 CRC64;
MSDQLEASIK NILEQKTLKW IFVGGKGGVG KTTCSCSLAA QLSKVRERVL LISTDPAHNI
SDAFSQKFTK TPTLVEGFKN LFAMEIDSNP NGEGVEMGNI EEMLQNAAQN EGGSGGFSMG
KDFLQSFAGG LPGIDEAMSF GEMIKLIDSL DFDVVVFDTA PTGHTLRLLQ FPTLLEKVFT
KILSLQGMFG PMMNQFGGMF GMGGGSMNEM IEKMTTTLES VKKMNAQFKD PNCTTFVCVC
IAEFLSLYET ERLIQELSKQ GIDTHNIIVN QLLFPDTDAN GTVSCRKCAS RQAIQSKYLT
DIDELYEDFH VVKLPLLEAE VRGGPAILQF SERMVDPEAN KN
