GET3_SCHPO
ID GET3_SCHPO Reviewed; 329 AA.
AC Q9P7F8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=SPAC1142.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS), AND SUBUNIT.
RX PubMed=19675567; DOI=10.1038/nature08319;
RA Mateja A., Szlachcic A., Downing M.E., Dobosz M., Mariappan M., Hegde R.S.,
RA Keenan R.J.;
RT "The structural basis of tail-anchored membrane protein recognition by
RT Get3.";
RL Nature 461:361-366(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 Q9P7F8; Q9P7F8: get3; NbExp=2; IntAct=EBI-15798909, EBI-15798909;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000255|HAMAP-
CC Rule:MF_03112}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
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DR EMBL; CU329670; CAB77013.1; -; Genomic_DNA.
DR RefSeq; NP_594270.1; NM_001019693.2.
DR PDB; 2WOO; X-ray; 3.01 A; A/B/C/D/E/F=1-329.
DR PDBsum; 2WOO; -.
DR AlphaFoldDB; Q9P7F8; -.
DR SMR; Q9P7F8; -.
DR BioGRID; 279369; 24.
DR DIP; DIP-59296N; -.
DR IntAct; Q9P7F8; 3.
DR STRING; 4896.SPAC1142.06.1; -.
DR iPTMnet; Q9P7F8; -.
DR MaxQB; Q9P7F8; -.
DR PaxDb; Q9P7F8; -.
DR PRIDE; Q9P7F8; -.
DR EnsemblFungi; SPAC1142.06.1; SPAC1142.06.1:pep; SPAC1142.06.
DR GeneID; 2542928; -.
DR KEGG; spo:SPAC1142.06; -.
DR PomBase; SPAC1142.06; get3.
DR VEuPathDB; FungiDB:SPAC1142.06; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; Q9P7F8; -.
DR OMA; MDAPYEF; -.
DR PhylomeDB; Q9P7F8; -.
DR EvolutionaryTrace; Q9P7F8; -.
DR PRO; PR:Q9P7F8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043529; C:GET complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032977; F:membrane insertase activity; IC:PomBase.
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:0071816; P:tail-anchored membrane protein insertion into ER membrane; IC:PomBase.
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; Nucleus; Reference proteome; Transport;
KW Zinc.
FT CHAIN 1..329
FT /note="ATPase get3"
FT /id="PRO_0000317079"
FT ACT_SITE 56
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2WOO"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:2WOO"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 269..288
FT /evidence="ECO:0007829|PDB:2WOO"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:2WOO"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:2WOO"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:2WOO"
SQ SEQUENCE 329 AA; 36548 MW; B0EEEE7019E7F4E8 CRC64;
MSFDPLPGTL ENLLEQTSLK WIFVGGKGGV GKTTTSCSLA IQMSKVRSSV LLISTDPAHN
LSDAFGTKFG KDARKVPGFD NLSAMEIDPN LSIQEMTEQA DQQNPNNPLS GMMQDLAFTI
PGIDEALAFA EILKQIKSME FDCVIFDTAP TGHTLRFLNF PTVLEKALGK LGGLSSRFGP
MINQMGSIMG VNANEQDLFG KMESMRANIS EVNKQFKNPD LTTFVCVCIS EFLSLYETER
MIQELTSYEI DTHNIVVNQL LLDPNTTCPQ CMARRKMQQK YLAQIEELYE DFHVVKVPQV
PAEVRGTEAL KSFSEMLVKP YVYPTSGKE
