OAS1A_MOUSE
ID OAS1A_MOUSE Reviewed; 367 AA.
AC P11928; F2Z419; Q3UEC1; Q64440; Q91VI0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=2'-5'-oligoadenylate synthase 1A;
DE Short=(2-5')oligo(A) synthase 1A;
DE Short=2-5A synthase 1A;
DE EC=2.7.7.84 {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:2171206, ECO:0000305|PubMed:27663720};
DE AltName: Full=p42 OAS;
GN Name=Oas1a; Synonyms=Oias1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3808949; DOI=10.1093/nar/14.24.10117;
RA Ichii Y., Fukunaga R., Shiojiri S., Sokawa Y.;
RT "Mouse 2-5A synthetase cDNA: nucleotide sequence and comparison to human 2-
RT 5A synthetase.";
RL Nucleic Acids Res. 14:10117-10117(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=2171206; DOI=10.1016/0042-6822(90)90292-y;
RA Coccia E.M., Romeo G., Nissim A., Marziali G., Albertini R., Affabris E.,
RA Battistini A., Fiorucci G., Orsatti R., Rossi G.B., Chebath J.;
RT "A full-length murine 2-5A synthetase cDNA transfected in NIH-3T3 cells
RT impairs EMCV but not VSV replication.";
RL Virology 179:228-233(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=12396720; DOI=10.1089/10799900260286696;
RA Kakuta S., Shibata S., Iwakura Y.;
RT "Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene
RT family.";
RL J. Interferon Cytokine Res. 22:981-993(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 14-367, AND INDUCTION.
RX PubMed=1709495; DOI=10.1093/nar/19.8.1917;
RA Rutherford M.N., Kumar A., Nissim A., Chebath J., Williams B.R.G.;
RT "The murine 2-5A synthetase locus: three distinct transcripts from two
RT linked genes.";
RL Nucleic Acids Res. 19:1917-1924(1991).
RN [9]
RP CATALYTIC ACTIVITY, INTERACTION WITH OAS1D, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15899864; DOI=10.1128/mcb.25.11.4615-4624.2005;
RA Yan W., Ma L., Stein P., Pangas S.A., Burns K.H., Bai Y., Schultz R.M.,
RA Matzuk M.M.;
RT "Mice deficient in oocyte-specific oligoadenylate synthetase-like protein
RT OAS1D display reduced fertility.";
RL Mol. Cell. Biol. 25:4615-4624(2005).
RN [10]
RP REVIEW.
RX PubMed=17024523; DOI=10.1007/s00239-006-0073-3;
RA Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.;
RT "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for
RT concerted evolution of paralogous Oas1 genes in Rodentia and
RT Artiodactyla.";
RL J. Mol. Evol. 63:562-576(2006).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=21142819; DOI=10.1089/jir.2010.0107;
RA Kristiansen H., Gad H.H., Eskildsen-Larsen S., Despres P., Hartmann R.;
RT "The oligoadenylate synthetase family: an ancient protein family with
RT multiple antiviral activities.";
RL J. Interferon Cytokine Res. 31:41-47(2011).
RN [12]
RP INDUCTION.
RX PubMed=22305621; DOI=10.1016/j.virol.2011.11.025;
RA Pulit-Penaloza J.A., Scherbik S.V., Brinton M.A.;
RT "Activation of Oas1a gene expression by type I IFN requires both STAT1 and
RT STAT2 while only STAT2 is required for Oas1b activation.";
RL Virology 425:71-81(2012).
RN [13]
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=27663720; DOI=10.1016/j.meegid.2016.09.018;
RA Elkhateeb E., Tag-El-Din-Hassan H.T., Sasaki N., Torigoe D., Morimatsu M.,
RA Agui T.;
RT "The role of mouse 2',5'-oligoadenylate synthetase 1 paralogs.";
RL Infect. Genet. Evol. 45:393-401(2016).
RN [14]
RP FUNCTION, AND ISOPRENYLATION AT CYS-364.
RX PubMed=34581622; DOI=10.1126/science.abj3624;
RG ISARIC4C Investigators;
RA Wickenhagen A., Sugrue E., Lytras S., Kuchi S., Noerenberg M.,
RA Turnbull M.L., Loney C., Herder V., Allan J., Jarmson I., Cameron-Ruiz N.,
RA Varjak M., Pinto R.M., Lee J.Y., Iselin L., Palmalux N., Stewart D.G.,
RA Swingler S., Greenwood E.J.D., Crozier T.W.M., Gu Q., Davies E.L.,
RA Clohisey S., Wang B., Trindade Maranhao Costa F., Freire Santana M.,
RA de Lima Ferreira L.C., Murphy L., Fawkes A., Meynert A., Grimes G.,
RA Da Silva Filho J.L., Marti M., Hughes J., Stanton R.J., Wang E.C.Y., Ho A.,
RA Davis I., Jarrett R.F., Castello A., Robertson D.L., Semple M.G.,
RA Openshaw P.J.M., Palmarini M., Lehner P.J., Baillie J.K., Rihn S.J.,
RA Wilson S.J.;
RT "A prenylated dsRNA sensor protects against severe COVID-19.";
RL Science 374:eabj3624-eabj3624(2021).
CC -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which
CC plays a critical role in cellular innate antiviral response. In
CC addition, it may also play a role in other cellular processes such as
CC apoptosis, cell growth, differentiation and gene regulation.
CC Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP
CC which then bind to the inactive monomeric form of ribonuclease L (RNase
CC L) leading to its dimerization and subsequent activation. Activation of
CC RNase L leads to degradation of cellular as well as viral RNA,
CC resulting in the inhibition of protein synthesis, thus terminating
CC viral replication. Can mediate the antiviral effect via the classical
CC RNase L-dependent pathway or an alternative antiviral pathway
CC independent of RNase L. {ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:34581622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84;
CC Evidence={ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864,
CC ECO:0000269|PubMed:2171206, ECO:0000305|PubMed:27663720};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00973};
CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC dsRNA generated during the course of viral infection. The dsRNA
CC activator must be at least 15 nucleotides long, and no modification of
CC the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as
CC activators.
CC -!- SUBUNIT: Monomer (By similarity). Homotetramer (By similarity).
CC Interacts with OAS1D; the interaction inhibits OAS1A catalytic activity
CC (PubMed:15899864). {ECO:0000250|UniProtKB:P00973,
CC ECO:0000269|PubMed:15899864}.
CC -!- INTERACTION:
CC P11928; O89168; Xeno; NbExp=5; IntAct=EBI-9352099, EBI-10107989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}.
CC Mitochondrion {ECO:0000250|UniProtKB:P00973}. Nucleus
CC {ECO:0000250|UniProtKB:P00973}. Microsome
CC {ECO:0000250|UniProtKB:P00973}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P00973}. Note=Associated with different
CC subcellular fractions such as mitochondrial, nuclear, and rough/smooth
CC microsomal fractions. {ECO:0000250|UniProtKB:P00973}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes and granulosa cells of ovary,
CC in intestine, stomach, spleen and uterus (at protein level)
CC (PubMed:15899864). Expressed at high levels in the digestive tract and
CC lymphoid organs (PubMed:12396720). Expressed in ovary and spleen
CC (PubMed:27663720). {ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:27663720}.
CC -!- DEVELOPMENTAL STAGE: Detected 5 weeks after birth in developing ovary
CC and spleen (PubMed:27663720). Expressed in fully grown, germinal
CC vesicle (GV)-intact oocytes, in oocytes at the metaphase II stage and
CC in the 2- to 8-cell embryos (PubMed:15899864).
CC {ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:27663720}.
CC -!- INDUCTION: Up-regulated in response to the type I interferon IFNB1, in
CC a STAT1 and STAT2-dependent manner (PubMed:1709495, PubMed:22305621).
CC Induced by polyinosinic:polycytidylic acid (poly I:C) (PubMed:15899864,
CC PubMed:27663720). {ECO:0000269|PubMed:15899864,
CC ECO:0000269|PubMed:1709495, ECO:0000269|PubMed:22305621,
CC ECO:0000269|PubMed:27663720}.
CC -!- PTM: C-terminal prenylated. {ECO:0000305|PubMed:34581622}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; X04958; CAA28620.1; -; mRNA.
DR EMBL; M33863; AAA37116.1; -; mRNA.
DR EMBL; AK149613; BAE28990.1; -; mRNA.
DR EMBL; AC015535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19743.1; -; Genomic_DNA.
DR EMBL; BC013715; AAH13715.1; -; mRNA.
DR EMBL; BC057878; AAH57878.1; -; mRNA.
DR EMBL; X58077; CAA41105.1; -; mRNA.
DR CCDS; CCDS19630.1; -.
DR PIR; A24725; SYMSO1.
DR PIR; S15660; S15660.
DR RefSeq; NP_660212.2; NM_145211.2.
DR AlphaFoldDB; P11928; -.
DR SMR; P11928; -.
DR BioGRID; 232938; 3.
DR IntAct; P11928; 1.
DR STRING; 10090.ENSMUSP00000079198; -.
DR PhosphoSitePlus; P11928; -.
DR SwissPalm; P11928; -.
DR EPD; P11928; -.
DR MaxQB; P11928; -.
DR PaxDb; P11928; -.
DR PeptideAtlas; P11928; -.
DR PRIDE; P11928; -.
DR ProteomicsDB; 293916; -.
DR DNASU; 246730; -.
DR Ensembl; ENSMUST00000080322; ENSMUSP00000079198; ENSMUSG00000052776.
DR GeneID; 246730; -.
DR KEGG; mmu:246730; -.
DR UCSC; uc008zij.2; mouse.
DR CTD; 246730; -.
DR MGI; MGI:2180860; Oas1a.
DR VEuPathDB; HostDB:ENSMUSG00000052776; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_0_0_1; -.
DR InParanoid; P11928; -.
DR OMA; VGRRHYT; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; P11928; -.
DR TreeFam; TF329749; -.
DR BRENDA; 2.7.7.84; 3474.
DR BioGRID-ORCS; 246730; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Oas1a; mouse.
DR PRO; PR:P11928; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P11928; protein.
DR Bgee; ENSMUSG00000052776; Expressed in granulocyte and 65 other tissues.
DR Genevisible; P11928; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0071659; P:negative regulation of IP-10 production; ISO:MGI.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0048525; P:negative regulation of viral process; IDA:MGI.
DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0060700; P:regulation of ribonuclease activity; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:MGI.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISO:MGI.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR InterPro; IPR026774; 2-5A_synthase.
DR InterPro; IPR006117; 2-5OAS_C_CS.
DR InterPro; IPR043518; 2-5OAS_N_CS.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR11258; PTHR11258; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Cytoplasm; Endoplasmic reticulum; Immunity;
KW Innate immunity; Lipoprotein; Magnesium; Metal-binding; Microsome;
KW Mitochondrion; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Prenylation; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..367
FT /note="2'-5'-oligoadenylate synthase 1A"
FT /id="PRO_0000160260"
FT REGION 14..61
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT REGION 201..211
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT LIPID 364
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:34581622"
FT CONFLICT 74
FT /note="K -> R (in Ref. 1; CAA28620 and 2; AAA37116)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> W (in Ref. 8; CAA41105)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="F -> Y (in Ref. 8; CAA41105)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="Y -> N (in Ref. 8; CAA41105)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="Q -> K (in Ref. 8; CAA41105)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="L -> V (in Ref. 7; AAH57878/AAH13715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 42429 MW; AE5946D5807776A4 CRC64;
MEHGLRSIPA WTLDKFIEDY LLPDTTFGAD VKSAVNVVCD FLKERCFQGA AHPVRVSKVV
KGGSSGKGTT LKGKSDADLV VFLNNLTSFE DQLNRRGEFI KEIKKQLYEV QHERRFRVKF
EVQSSWWPNA RSLSFKLSAP HLHQEVEFDV LPAFDVLGHV NTSSKPDPRI YAILIEECTS
LGKDGEFSTC FTELQRNFLK QRPTKLKSLI RLVKHWYQLC KEKLGKPLPP QYALELLTVF
AWEQGNGCYE FNTAQGFRTV LELVINYQHL RIYWTKYYDF QHQEVSKYLH RQLRKARPVI
LDPADPTGNV AGGNPEGWRR LAEEADVWLW YPCFIKKDGS RVSSWDVPTV VPVPFEQVEE
NWTCILL
