(data stored in ACNUC30567 zone)

HOGENOM: AEDAE_4401_PE3

ID   AEDAE_4401_PE3                       STANDARD;      PRT;   341 AA.
AC   AEDAE_4401_PE3; Q16MG9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATPase ASNA1 homolog; EC=3.6.- -;AltName: Full=Arsenical
DE   pump-driving ATPase homolog;AltName: Full=Arsenite-stimulated ATPase;
DE   (AEDAE_4401.PE3).
GN   ORFNames=AAEL011136;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_4401.PE3.
CC       Aedes aegypti supercontig supercont1.677 AaegL1 full sequence 1..634724
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:ASNA_AEDAE
CC   -!- FUNCTION: ATPase required for the post-translational delivery of
CC       tail-anchored (TA) proteins to the endoplasmic reticulum.
CC       Recognizes and selectively binds the transmembrane domain of TA
CC       proteins in the cytosol. This complex then targets to the
CC       endoplasmic reticulum by membrane-bound receptors, where the tail-
CC       anchored protein is released for insertion. This process is
CC       regulated by ATP binding and hydrolysis. ATP binding drives the
CC       homodimer towards the closed dimer state, facilitating recognition
CC       of newly synthesized TA membrane proteins. ATP hydolysis is
CC       required for insertion. Subsequently, the homodimer reverts
CC       towards the open dimer state, lowering its affinity for the
CC       membrane-bound receptor, and returning it to the cytosol to
CC       initiate a new round of targeting (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endoplasmic
CC       reticulum (By similarity).
CC   -!- SIMILARITY: Belongs to the arsA ATPase family.
CC   -!- GENE_FAMILY: HOG000197637 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL012316;AAEL012316-RA;AAEL012316-PA.
DR   EMBL; CH477728; - ;
DR   EMBL; CH477862; - ;
DR   UniProtKB/Swiss-Prot; Q16MG9; -.
DR   EMBL; CH477862; EAT35519.1; -; Genomic_DNA.
DR   EMBL; CH477728; EAT36805.1; -; Genomic_DNA.
DR   RefSeq; XP_001661438.1; XM_001661388.1.
DR   RefSeq; XP_001662407.1; XM_001662357.1.
DR   UniGene; Aae.11984; -.
DR   UniGene; Aae.23219; -.
DR   ProteinModelPortal; Q16MG9; -.
DR   EnsemblMetazoa; AAEL011136-RA; AAEL011136-PA; AAEL011136.
DR   EnsemblMetazoa; AAEL012316-RA; AAEL012316-PA; AAEL012316.
DR   GeneID; 5574421; -.
DR   GeneID; 5576083; -.
DR   KEGG; aag:AaeL_AAEL011136; -.
DR   KEGG; aag:AaeL_AAEL012316; -.
DR   VectorBase; AAEL011136; Aedes aegypti.
DR   VectorBase; AAEL012316; Aedes aegypti.
DR   eggNOG; inNOG05495; -.
DR   GeneTree; EMGT00050000017449; -.
DR   OMA; LSCMEID; -.
DR   OrthoDB; EOG4905RN; -.
DR   PhylomeDB; Q16MG9; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0015446; F:arsenite-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:InterPro.
DR   InterPro; IPR016300; Arsenical_pump_ATPase_ArsA.
DR   TIGRFAMs; TIGR00345; ArsA; 1.
DR   HOGENOMDNA; AEDAE_4401.PE3; -.
KW   AAEL0123163; AAEL012316-PA ; Q16MG9; CH477728; CH477862;
KW   ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Transport; Zinc.
SQ   SEQUENCE   341 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDTDFEPLAP SLENIIDQET LKWVFVGGKG GVGKTTCSCS LAVQLAKVRE SVLIISTDPA
     HNISDAFDQK FTKVPTKVNG FNNLFAMEID PNVGLNELPD EYFEGENSAM KLSKGVFQEI
     IGALPGIDEA MSYAEVMKLV KAMNFSVVVF DTAPTGHTLR LLSFPQVVEK GLGKLLMLKM
     KLAPFISQMG SLFGMQDFNA DTLTGKLEEM LTIIRQVNEQ FRNPDQTTFV CVCIAEFLSL
     YETERLVQEL TKCGIDTHNI IVNQLLFRRE GQAPCAMCSA RYKVQGKYLD QIADLYEDFY
     VVKLPLLDKE VRGVENVKKF SEYLIKPYCP NGTNETQEQD K
//

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