GET3_LACTC
ID GET3_LACTC Reviewed; 349 AA.
AC C5DL53;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=KLTH0F10098g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(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 GET1 and GET2, where the tail-anchored protein
CC is released for insertion. This process is regulated by ATP binding and
CC hydrolysis. ATP binding drives the homodimer towards the closed dimer
CC state, facilitating recognition of newly synthesized TA membrane
CC proteins. ATP hydrolysis is required for insertion. Subsequently, the
CC homodimer reverts towards the open dimer state, lowering its affinity
CC for the GET1-GET2 receptor, and returning it to the cytosol to initiate
CC a new round of targeting. Cooperates with the HDEL receptor ERD2 to
CC mediate the ATP-dependent retrieval of resident ER proteins that
CC contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
CC Involved in low-level resistance to the oxyanions arsenite and
CC arsenate, and in heat tolerance. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SUBUNIT: Homodimer. Component of the Golgi to ER traffic (GET) complex,
CC which is composed of GET1, GET2 and GET3. Within the complex, GET1 and
CC GET2 form a heterotetramer which is stabilized by phosphatidylinositol
CC binding and which binds to the GET3 homodimer. Interacts with the
CC chloride channel protein GEF1. {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}. Golgi
CC apparatus {ECO:0000255|HAMAP-Rule:MF_03112}. Note=GET1 and GET2 are
CC required for targeting GET3 to the endoplasmic reticulum.
CC {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; CU928170; CAR24204.1; -; Genomic_DNA.
DR RefSeq; XP_002554641.1; XM_002554595.1.
DR AlphaFoldDB; C5DL53; -.
DR SMR; C5DL53; -.
DR STRING; 559295.C5DL53; -.
DR EnsemblFungi; CAR24204; CAR24204; KLTH0F10098g.
DR GeneID; 8292851; -.
DR KEGG; lth:KLTH0F10098g; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; C5DL53; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR Proteomes; UP000002036; Chromosome F.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Golgi apparatus; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..349
FT /note="ATPase GET3"
FT /id="PRO_0000388210"
FT ACT_SITE 57
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 280
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 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"
SQ SEQUENCE 349 AA; 39124 MW; 52B129166D51B243 CRC64;
MDLIAEPNLK ELINSTTHKW IFVGGKGGVG KTTSSCSISI QMALAQPKKQ FLLISTDPAH
NLSDAFGEKF GKDARKVTGM DNLSCMEIDP SAALKDMNDM SVAQNDKNDG FSDLLQGGGL
AELTGSIPGI DEALSFMEVM KHIKRQEEGE GEKYDTVIFD TAPTGHTLRF LQLPQTLSQL
LQKFGEIAGR FGPMLNSLTG GGQNMDIMGK VDELKANVEK IREQFTNPDM TTFVCVCISE
FLSLYETERL IQELMSYEMD VNSIIVNQLL FADDDAEHNC RRCQARWNMQ KKYLDQIGEL
YDDFHVVKMP LCAGEIRGLN NLKKFSQFLN KEYDPVADNK IIYELEEQK
