GenomeNet

Database: UniProt
Entry: W5JQD0_ANODA
LinkDB: W5JQD0_ANODA
Original site: W5JQD0_ANODA 
ID   W5JQD0_ANODA            Unreviewed;       344 AA.
AC   W5JQD0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=ATPase ASNA1 homolog {ECO:0000256|HAMAP-Rule:MF_03112};
DE            EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_03112};
DE   AltName: Full=Arsenical pump-driving ATPase homolog {ECO:0000256|HAMAP-Rule:MF_03112};
DE   AltName: Full=Arsenite-stimulated ATPase {ECO:0000256|HAMAP-Rule:MF_03112};
GN   ORFNames=AND_003310 {ECO:0000313|EMBL:ETN64944.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN64944.1};
RN   [1] {ECO:0000313|EMBL:ETN64944.1, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN64944.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN64944.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA   Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA   Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA   Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA   de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA   Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA   Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA   Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA   de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA   Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA   Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA   Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA   Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA   Camargo E.P., de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC003310-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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. {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03112}.
CC       Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SIMILARITY: Belongs to the arsA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00011040, ECO:0000256|HAMAP-Rule:MF_03112}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ADMH02000830; ETN64944.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5JQD0; -.
DR   STRING; 43151.W5JQD0; -.
DR   EnsemblMetazoa; ADAC003310-RA; ADAC003310-PA; ADAC003310.
DR   VEuPathDB; VectorBase:ADAC003310; -.
DR   VEuPathDB; VectorBase:ADAR2_000674; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   HOGENOM; CLU_040761_0_0_1; -.
DR   OMA; MDAPYEF; -.
DR   OrthoDB; 3135429at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR   CDD; cd02035; ArsA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00345; GET3_arsA_TRC40; 1.
DR   PANTHER; PTHR10803; ARSENICAL PUMP-DRIVING ATPASE ARSENITE-TRANSLOCATING ATPASE; 1.
DR   PANTHER; PTHR10803:SF3; ATPASE GET3; 1.
DR   Pfam; PF02374; ArsA_ATPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03112};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03112}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03112};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_03112}.
FT   DOMAIN          22..324
FT                   /note="Anion-transporting ATPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02374"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   344 AA;  38024 MW;  771EE38355FC8970 CRC64;
     MEEDFEPLEP SIRNVIEQTS LKWVFVGGKG GVGKTTCSCS LAVQLSLKRE SVLIISTDPA
     HNISDAFDQK FTKVPTKVNG FDNLFAMEID PNVGLSELPD EYFEGDSSPL NVGKGVLQEV
     ISTLPGIDEA MSYAEVMKLV KAMNFSVVVF DTAPTGHTLR LLSFPQVVEK GLGKLLRLKM
     KLSPIISQMG ALFGMADFNG DTIATKLEEM LSIIQQVNEQ FHNPQQTTFV CVCIAEFLSL
     YETERLVQEL TKCGIDTHNI IVNQLLFQRK GQQPCTMCSA RCKVQAKYLD QIADLYEDFH
     VTRLPLLDEE VRGVEKVKKF SKNLLVPYTP DTAAPAAPAP APAE
//
DBGET integrated database retrieval system