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GET3_KOMPG
ID   GET3_KOMPG              Reviewed;         344 AA.
AC   C4R7S9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=PAS_chr4_0405;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(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; FN392322; CAY71654.1; -; Genomic_DNA.
DR   RefSeq; XP_002493833.1; XM_002493788.1.
DR   AlphaFoldDB; C4R7S9; -.
DR   SMR; C4R7S9; -.
DR   STRING; 644223.C4R7S9; -.
DR   PRIDE; C4R7S9; -.
DR   EnsemblFungi; CAY71654; CAY71654; PAS_chr4_0405.
DR   GeneID; 8200688; -.
DR   KEGG; ppa:PAS_chr4_0405; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   HOGENOM; CLU_040761_0_0_1; -.
DR   InParanoid; C4R7S9; -.
DR   OMA; MDAPYEF; -.
DR   Proteomes; UP000000314; Chromosome 4.
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:0042802; F:identical protein binding; IEA:EnsemblFungi.
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..344
FT                   /note="ATPase GET3"
FT                   /id="PRO_0000388224"
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         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         276
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         279
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   344 AA;  38785 MW;  6D95D4B472F69F5B CRC64;
     MDIEAEPSLR SIVNHESLKW IFVGGKGGVG KTTTSSSISI QLALHNPNKK YLLISTDPAH
     NLSDAFNQKF GKDARQVEGL PNLSCMEIDP DSTLENLQKN NESTFGSAGG NDPLKSMMGD
     ITGSIPGIDE AFSFMEVLKH IGETKENQIK YDTVIFDTAP TGHTLRFLQL PSTLEKLLGK
     VNELSGRFGP MLNNLLGSQG GQSIDFASKI KEIQVQVTEV NKQFQDPELT TFVCVCISEF
     LSLYETERLI QELMSYNMDV NSIVINQLLF SDDSECRRCN ARWRMQKKYL DQMDELYEDY
     HLVKMPLLAM EVRGLENLKK FSKYLIEPYN SETDGHVVFD LEEQ
 
 
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