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Database: UniProt
Entry: A0A1U8A1R6_NELNU
LinkDB: A0A1U8A1R6_NELNU
Original site: A0A1U8A1R6_NELNU 
ID   A0A1U8A1R6_NELNU        Unreviewed;       358 AA.
AC   A0A1U8A1R6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=ATPase ASNA1 homolog isoform X1 {ECO:0000313|RefSeq:XP_010255567.1, ECO:0000313|RefSeq:XP_010255568.1};
GN   Name=LOC104596199 {ECO:0000313|RefSeq:XP_010255567.1,
GN   ECO:0000313|RefSeq:XP_010255568.1};
OS   Nelumbo nucifera (Sacred lotus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010255568.1};
RN   [1] {ECO:0000313|RefSeq:XP_010255567.1, ECO:0000313|RefSeq:XP_010255568.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03112}.
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DR   RefSeq; XP_010255567.1; XM_010257265.1.
DR   RefSeq; XP_010255568.1; XM_010257266.1.
DR   STRING; 4432.A0A1U8A1R6; -.
DR   GeneID; 104596199; -.
DR   KEGG; nnu:104596199; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   OrthoDB; 3135429at2759; -.
DR   Proteomes; UP000189703; Unplaced.
DR   GO; GO:0043529; C:GET complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03112}.
FT   DOMAIN          22..313
FT                   /note="Anion-transporting ATPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02374"
FT   COILED          327..358
FT                   /evidence="ECO:0000256|SAM:Coils"
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         227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   358 AA;  40475 MW;  9A71AEE8469CD007 CRC64;
     MATDQGIPEG TVQNILDQES LKWVFVGGKG GVGKTTCSSV LSILLSRVRS SVLIISTDPA
     HNLSDAFQQR FTKMPTLVNG FTNLYAMEVD PNVENEDLTN MEEMDSFVSE LANAIPGIDE
     AMSFAEMLKL VQTMDYSVIV FDTAPTGHTL RLLQFPSTLE KGLAKMMSLK NRFGGILSQM
     SRIFGVDDFG EDAVLGKLEG MKDVIEKVNK QFKDPDLTTF VCVCIPEFLS LYETERLVQE
     LTKFEIDTHN IIINQVLFNE EAVESKLLKA RMRMQQKYLD QFYMLYDDFH ITKLPLLPEE
     VCGVEALNKF SHNFITPYQP SITRGTAEEL EQRVSILRQQ LEDAEAELDR LRKGKQIL
//
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