GET3_HUMAN
ID GET3_HUMAN Reviewed; 348 AA.
AC O43681; A6NHP8; A8K740; Q53FC6; Q92849;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 198.
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=Guided entry of tail-anchored proteins factor 3, ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Transmembrane domain recognition complex 40 kDa ATPase subunit;
DE AltName: Full=hARSA-I;
DE AltName: Full=hASNA-I;
GN Name=GET3 {ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000312|HGNC:HGNC:752};
GN Synonyms=ARSA {ECO:0000312|HGNC:HGNC:752},
GN ASNA1 {ECO:0000255|HAMAP-Rule:MF_03112}, TRC40 {ECO:0000312|HGNC:HGNC:752};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hu G.;
RT "Human homolog of bacterial and mouse arsenite translocating ATPase gene,
RT ArsA.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-332.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-348.
RX PubMed=8884272; DOI=10.1006/geno.1996.0494;
RA Kurdi-Haidar B., Aebi S., Heath D., Enns R.E., Naredi P., Hom D.K.,
RA Howell S.B.;
RT "Isolation of the ATP-binding human homolog of the arsA component of the
RT bacterial arsenite transporter.";
RL Genomics 36:486-491(1996).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9712828; DOI=10.1074/jbc.273.35.22173;
RA Kurdi-Haidar B., Heath D., Aebi S., Howell S.B.;
RT "Biochemical characterization of the human arsenite-stimulated ATPase
RT (hASNA-I).";
RL J. Biol. Chem. 273:22173-22176(1998).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=9736449;
RX DOI=10.1002/(sici)1097-4644(19981001)71:1<1::aid-jcb1>3.0.co;2-#;
RA Kurdi-Haidar B., Hom D.K., Flittner D.E., Heath D., Fink L., Naredi P.,
RA Howell S.B.;
RT "Dual cytoplasmic and nuclear distribution of the novel arsenite-stimulated
RT human ATPase (hASNA-I).";
RL J. Cell. Biochem. 71:1-10(1998).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=9774623; DOI=10.1177/002215549804601104;
RA Kurdi-Haidar B., Heath D., Naredi P., Varki N., Howell S.B.;
RT "Immunohistochemical analysis of the distribution of the human ATPase
RT (hASNA-I) in normal tissues and its overexpression in breast adenomas and
RT carcinomas.";
RL J. Histochem. Cytochem. 46:1243-1248(1998).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE TRC COMPLEX, MUTAGENESIS OF GLY-46,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SEC61B.
RX PubMed=17382883; DOI=10.1016/j.cell.2007.01.036;
RA Stefanovic S., Hegde R.S.;
RT "Identification of a targeting factor for posttranslational membrane
RT protein insertion into the ER.";
RL Cell 128:1147-1159(2007).
RN [13]
RP FUNCTION, AND INTERACTION WITH SERP1 AND SEC61B.
RX PubMed=18477612; DOI=10.1242/jcs.020321;
RA Favaloro V., Spasic M., Schwappach B., Dobberstein B.;
RT "Distinct targeting pathways for the membrane insertion of tail-anchored
RT (TA) proteins.";
RL J. Cell Sci. 121:1832-1840(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP INTERACTION WITH GET1, AND SUBCELLULAR LOCATION.
RX PubMed=21444755; DOI=10.1242/jcs.084277;
RA Vilardi F., Lorenz H., Dobberstein B.;
RT "WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored
RT proteins into the ER membrane.";
RL J. Cell Sci. 124:1301-1307(2011).
RN [17]
RP FUNCTION, IDENTIFICATION IN GET COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23041287; DOI=10.1016/j.molcel.2012.08.028;
RA Yamamoto Y., Sakisaka T.;
RT "Molecular machinery for insertion of tail-anchored membrane proteins into
RT the endoplasmic reticulum membrane in mammalian cells.";
RL Mol. Cell 48:387-397(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INTERACTION WITH CAMLG AND GET1.
RX PubMed=24392163; DOI=10.1371/journal.pone.0085033;
RA Vilardi F., Stephan M., Clancy A., Janshoff A., Schwappach B.;
RT "WRB and CAML are necessary and sufficient to mediate tail-anchored protein
RT targeting to the ER membrane.";
RL PLoS ONE 9:e85033-e85033(2014).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF LYS-86.
RX PubMed=25535373; DOI=10.1073/pnas.1402745112;
RA Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.;
RT "Bag6 complex contains a minimal tail-anchor-targeting module and a mock
RT BAG domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF THE GET COMPLEX.
RX PubMed=32910895; DOI=10.1016/j.molcel.2020.08.012;
RA McDowell M.A., Heimes M., Fiorentino F., Mehmood S., Farkas A.,
RA Coy-Vergara J., Wu D., Bolla J.R., Schmid V., Heinze R., Wild K.,
RA Flemming D., Pfeffer S., Schwappach B., Robinson C.V., Sinning I.;
RT "Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET
RT Insertase Complex.";
RL Mol. Cell 80:72-86(2020).
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/WRB and CAMLG/GET2, where the tail-
CC anchored protein is released for insertion. This process is regulated
CC by ATP binding and hydrolysis. ATP binding drives the homodimer towards
CC the closed dimer state, facilitating recognition of newly synthesized
CC TA membrane proteins. ATP hydrolysis is required for insertion.
CC Subsequently, the homodimer reverts towards the open dimer state,
CC lowering its affinity for the GET1-CAMLG receptor, and returning it to
CC the cytosol to initiate a new round of targeting. May be involved in
CC insulin signaling. {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:18477612,
CC ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:25535373}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for ATP {ECO:0000269|PubMed:9712828};
CC Vmax=16.6 nmol/min/mg enzyme for ATP {ECO:0000269|PubMed:9712828};
CC -!- SUBUNIT: Homodimer (By similarity). Component of the Golgi to ER
CC traffic (GET) complex, which is composed of GET1/WRB, CAMLG/GET2 and
CC GET3/TRC40 (PubMed:21444755, PubMed:23041287, PubMed:24392163,
CC PubMed:32910895). Within the complex, CAMLG and GET1 form a
CC heterotetramer which is stabilized by phosphatidylinositol binding and
CC which binds to the GET3 homodimer (PubMed:32910895). Interacts with
CC CAMLG (via N-terminus) (By similarity). GET3 shows a higher affinity
CC for CAMLG than for GET1 (PubMed:24392163). Interacts with SERP1 and
CC SEC61B (PubMed:17382883, PubMed:18477612).
CC {ECO:0000250|UniProtKB:G3V9T7, ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:18477612,
CC ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:23041287,
CC ECO:0000269|PubMed:24392163, ECO:0000269|PubMed:32910895}.
CC -!- INTERACTION:
CC O43681; O95994: AGR2; NbExp=7; IntAct=EBI-2515857, EBI-712648;
CC O43681; Q12797: ASPH; NbExp=3; IntAct=EBI-2515857, EBI-2967294;
CC O43681; Q12797-6: ASPH; NbExp=3; IntAct=EBI-2515857, EBI-12092171;
CC O43681; P49069: CAMLG; NbExp=5; IntAct=EBI-2515857, EBI-1748958;
CC O43681; Q8TEY5: CREB3L4; NbExp=3; IntAct=EBI-2515857, EBI-3925424;
CC O43681; O95196-2: CSPG5; NbExp=3; IntAct=EBI-2515857, EBI-18400097;
CC O43681; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-2515857, EBI-742054;
CC O43681; Q7Z589-5: EMSY; NbExp=3; IntAct=EBI-2515857, EBI-11989522;
CC O43681; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-2515857, EBI-11793142;
CC O43681; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2515857, EBI-18304435;
CC O43681; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2515857, EBI-3918971;
CC O43681; Q7L5D6: GET4; NbExp=4; IntAct=EBI-2515857, EBI-711823;
CC O43681; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-2515857, EBI-712073;
CC O43681; Q96SL4: GPX7; NbExp=6; IntAct=EBI-2515857, EBI-749411;
CC O43681; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2515857, EBI-11721746;
CC O43681; Q9Y5L2: HILPDA; NbExp=3; IntAct=EBI-2515857, EBI-8803836;
CC O43681; P24592: IGFBP6; NbExp=3; IntAct=EBI-2515857, EBI-947015;
CC O43681; Q8WWG9: KCNE4; NbExp=3; IntAct=EBI-2515857, EBI-11750916;
CC O43681; Q9UJ90: KCNE5; NbExp=3; IntAct=EBI-2515857, EBI-11981259;
CC O43681; O15165-2: LDLRAD4; NbExp=3; IntAct=EBI-2515857, EBI-13302279;
CC O43681; Q15084: PDIA6; NbExp=3; IntAct=EBI-2515857, EBI-1043087;
CC O43681; O75381: PEX14; NbExp=3; IntAct=EBI-2515857, EBI-594898;
CC O43681; O00264: PGRMC1; NbExp=3; IntAct=EBI-2515857, EBI-1045534;
CC O43681; O15173: PGRMC2; NbExp=3; IntAct=EBI-2515857, EBI-1050125;
CC O43681; Q04118: PRB3; NbExp=3; IntAct=EBI-2515857, EBI-13360404;
CC O43681; Q16378: PRR4; NbExp=3; IntAct=EBI-2515857, EBI-738624;
CC O43681; Q15293: RCN1; NbExp=5; IntAct=EBI-2515857, EBI-948278;
CC O43681; Q6ZWK4: RHEX; NbExp=3; IntAct=EBI-2515857, EBI-18304046;
CC O43681; Q96E16: SMIM19; NbExp=3; IntAct=EBI-2515857, EBI-17657124;
CC O43681; P10451: SPP1; NbExp=3; IntAct=EBI-2515857, EBI-723648;
CC O43681; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2515857, EBI-17280858;
CC O43681; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-2515857, EBI-18196631;
CC O43681; Q6P9G4: TMEM154; NbExp=3; IntAct=EBI-2515857, EBI-13329239;
CC O43681; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-2515857, EBI-726044;
CC O43681; Q9H3N1: TMX1; NbExp=3; IntAct=EBI-2515857, EBI-1051115;
CC O43681; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-2515857, EBI-11957238;
CC O43681; Q8IUB2: WFDC3; NbExp=3; IntAct=EBI-2515857, EBI-7963932;
CC O43681; Q56975: yscD; Xeno; NbExp=2; IntAct=EBI-2515857, EBI-6413916;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17382883,
CC ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:9736449}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:21444755}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:21444755,
CC ECO:0000269|PubMed:9736449}.
CC -!- TISSUE SPECIFICITY: Expressed in the epithelial cells of the liver,
CC kidney, and stomach wall, in the adrenal medulla, in the islet cells of
CC the pancreas, in the red pulp of the spleen, and in cardiac and
CC skeletal muscle. {ECO:0000269|PubMed:9774623}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50731.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/asna1/";
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DR EMBL; AF047469; AAC03551.1; -; mRNA.
DR EMBL; AK291855; BAF84544.1; -; mRNA.
DR EMBL; AK223363; BAD97083.1; -; mRNA.
DR EMBL; AY304483; AAP45050.1; -; Genomic_DNA.
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84303.1; -; Genomic_DNA.
DR EMBL; BC002651; AAH02651.1; -; mRNA.
DR EMBL; U60276; AAC50731.1; ALT_FRAME; mRNA.
DR CCDS; CCDS32920.1; -.
DR RefSeq; NP_004308.2; NM_004317.3.
DR PDB; 6SO5; EM; 4.20 A; A/B=1-348.
DR PDBsum; 6SO5; -.
DR AlphaFoldDB; O43681; -.
DR SMR; O43681; -.
DR BioGRID; 106931; 108.
DR ComplexPortal; CPX-6464; GET complex.
DR IntAct; O43681; 58.
DR MINT; O43681; -.
DR STRING; 9606.ENSP00000466379; -.
DR DrugBank; DB00171; ATP.
DR TCDB; 3.A.19.1.1; the guided entry of tail anchored protein (get) family.
DR CarbonylDB; O43681; -.
DR iPTMnet; O43681; -.
DR MetOSite; O43681; -.
DR PhosphoSitePlus; O43681; -.
DR SwissPalm; O43681; -.
DR BioMuta; ASNA1; -.
DR OGP; O43681; -.
DR EPD; O43681; -.
DR jPOST; O43681; -.
DR MassIVE; O43681; -.
DR MaxQB; O43681; -.
DR PaxDb; O43681; -.
DR PeptideAtlas; O43681; -.
DR PRIDE; O43681; -.
DR ProteomicsDB; 49111; -.
DR Antibodypedia; 26148; 361 antibodies from 37 providers.
DR DNASU; 439; -.
DR Ensembl; ENST00000357332.8; ENSP00000349887.3; ENSG00000198356.12.
DR Ensembl; ENST00000591090.5; ENSP00000466379.1; ENSG00000198356.12.
DR GeneID; 439; -.
DR KEGG; hsa:439; -.
DR MANE-Select; ENST00000357332.8; ENSP00000349887.3; NM_004317.4; NP_004308.2.
DR UCSC; uc002muv.3; human.
DR CTD; 439; -.
DR DisGeNET; 439; -.
DR GeneCards; GET3; -.
DR HGNC; HGNC:752; GET3.
DR HPA; ENSG00000198356; Low tissue specificity.
DR MIM; 601913; gene.
DR neXtProt; NX_O43681; -.
DR OpenTargets; ENSG00000198356; -.
DR PharmGKB; PA25051; -.
DR VEuPathDB; HostDB:ENSG00000198356; -.
DR eggNOG; KOG2825; Eukaryota.
DR GeneTree; ENSGT00390000003817; -.
DR InParanoid; O43681; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR PhylomeDB; O43681; -.
DR BRENDA; 7.3.2.7; 2681.
DR PathwayCommons; O43681; -.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SABIO-RK; O43681; -.
DR SignaLink; O43681; -.
DR BioGRID-ORCS; 439; 531 hits in 1093 CRISPR screens.
DR ChiTaRS; ASNA1; human.
DR GeneWiki; ASNA1; -.
DR GenomeRNAi; 439; -.
DR Pharos; O43681; Tbio.
DR PRO; PR:O43681; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43681; protein.
DR Bgee; ENSG00000198356; Expressed in monocyte and 203 other tissues.
DR Genevisible; O43681; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043529; C:GET complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0015105; F:arsenite transmembrane transporter activity; TAS:ProtInc.
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; IC:ComplexPortal.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
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; Acetylation; ATP-binding; Cytoplasm; Endoplasmic reticulum;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..348
FT /note="ATPase GET3"
FT /id="PRO_0000152253"
FT ACT_SITE 74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 289
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 292
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VARIANT 332
FT /note="N -> S (in dbSNP:rs8177499)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018844"
FT MUTAGEN 46
FT /note="G->R: Abolishes ATPase activity, dominantly inhibits
FT the TA protein insertion pathway."
FT /evidence="ECO:0000269|PubMed:17382883"
FT MUTAGEN 86
FT /note="K->D: Reduces TA protein insertion pathway."
FT /evidence="ECO:0000269|PubMed:25535373"
FT CONFLICT 113..114
FT /note="EL -> DV (in Ref. 8; AAC50731)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="C -> F (in Ref. 1; AAC03551)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="L -> P (in Ref. 3; BAD97083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38793 MW; DA52C4ACC35C7A36 CRC64;
MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK TTCSCSLAVQ
LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL FAMEIDPSLG VAELPDEFFE
EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP
TIVERGLGRL MQIKNQISPF ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE
QTTFICVCIA EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA
KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSAQ
