GET3_CRYNJ
ID GET3_CRYNJ Reviewed; 325 AA.
AC P0CM24; Q55K96; Q5K9A4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 {ECO:0000255|HAMAP-Rule:MF_03112}; OrderedLocusNames=CNK02640;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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 -!- 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}.
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; AE017351; AAW46346.1; -; Genomic_DNA.
DR RefSeq; XP_567863.1; XM_567863.1.
DR AlphaFoldDB; P0CM24; -.
DR SMR; P0CM24; -.
DR STRING; 5207.AAW46346; -.
DR PaxDb; P0CM24; -.
DR EnsemblFungi; AAW46346; AAW46346; CNK02640.
DR GeneID; 3254436; -.
DR KEGG; cne:CNK02640; -.
DR VEuPathDB; FungiDB:CNK02640; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; P0CM24; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR Proteomes; UP000002149; Chromosome 11.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..325
FT /note="ATPase GET3"
FT /id="PRO_0000388205"
FT ACT_SITE 57
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 267
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 270
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"
SQ SEQUENCE 325 AA; 36179 MW; 17FA8C1334549024 CRC64;
MSDLEPLDPT LQNILDQKSL KWIFCGGKGG VGKTTTSCSL AVQLAACRES VLLISTDPAH
NLSDAFSQKF GKDATKVNGF DNLYAMEIDP NGSLQEMIES SDQTGGMGGM MQDLAFAIPG
VDEAMGFAEI MKHVKSMEFS VIVFDTAPTG HTLRFLSFPS VLEKALGKLS TLGGKFGPMI
QQMQSMFGGG APQEDMFAKL ESMREIITEV NNQFKDPEKT TFVCVCISEF LSLYETERLI
QELTSYEIDT HNIVVNQLLF PKAGDNCEQC SVRHNMQQKY LKEAYDLYED EFHIVKLPLL
TEEVRGVEKI KEFSKMLTQP YTPPQ
