GET3_ASPFU
ID GET3_ASPFU Reviewed; 340 AA.
AC Q4WY07;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATPase get3 {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};
DE AltName: Full=Golgi to ER traffic protein 3 {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Guided entry of tail-anchored proteins 3 {ECO:0000255|HAMAP-Rule:MF_03112};
GN Name=get3; ORFNames=AFUA_3G11350;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT, AND
RP MUTAGENESIS OF GLY-38.
RX PubMed=19706470; DOI=10.1073/pnas.0907522106;
RA Suloway C.J.M., Chartron J.W., Zaslaver M., Clemons W.M. Jr.;
RT "Model for eukaryotic tail-anchored protein binding based on the structure
RT of Get3.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14849-14854(2009).
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:0000255|HAMAP-Rule:MF_03112}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- INTERACTION:
CC Q4WY07; Q4WY07: get3; NbExp=2; IntAct=EBI-15800715, EBI-15800715;
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; AAHF01000002; EAL92446.2; -; Genomic_DNA.
DR RefSeq; XP_754484.2; XM_749391.2.
DR PDB; 3IBG; X-ray; 3.20 A; A/B/C/D/E/F=3-340.
DR PDBsum; 3IBG; -.
DR AlphaFoldDB; Q4WY07; -.
DR SMR; Q4WY07; -.
DR DIP; DIP-48950N; -.
DR STRING; 746128.CADAFUBP00003705; -.
DR EnsemblFungi; EAL92446; EAL92446; AFUA_3G11350.
DR GeneID; 3512551; -.
DR KEGG; afm:AFUA_3G11350; -.
DR VEuPathDB; FungiDB:Afu3g11350; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; Q4WY07; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR EvolutionaryTrace; Q4WY07; -.
DR Proteomes; UP000002530; Chromosome 3.
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:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044183; F:protein folding chaperone; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
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 GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR GO; GO:0010038; P:response to metal ion; IEA:EnsemblFungi.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:EnsemblFungi.
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 3D-structure; ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..340
FT /note="ATPase get3"
FT /id="PRO_0000388189"
FT ACT_SITE 63
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 283
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 286
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 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 38
FT /note="G->R: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:19706470"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3IBG"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:3IBG"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 284..303
FT /evidence="ECO:0007829|PDB:3IBG"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3IBG"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:3IBG"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:3IBG"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:3IBG"
SQ SEQUENCE 340 AA; 37440 MW; 9F6B277957FFE461 CRC64;
MSSTAVVHGD DLMEPTLQSI LSQKTLRWIF VGGKGGVGKT TTSCSLAIQL AKVRKSVLLI
STDPAHNLSD AFGQKFGKEA RLVDGYSNLS AMEIDPNGSI QDLLASGDSQ GDDPLAGLGM
GNMMQDLAFS IPGVDEAMSF AEVLKQVKSL SYEVIVFDTA PTGHTLRFLQ FPTVLEKALA
KLSQLSSQFG PMLNSILGAR GGLPGGQNID ELLQKMESLR ETISEVNTQF KNPDMTTFVC
VCIAEFLSLY ETERMIQELT SYGIDTHAIV VNQLLFPKEG SGCEQCNARR KMQKKYLEQI
EELYEDFNVV RMPLLVEEVR GKEKLEKFSE MLVHPYVPPQ
