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
//