SELO_MOUSE
ID SELO_MOUSE Reviewed; 667 AA.
AC Q9DBC0; E9QPP4; Q80ZK3;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein adenylyltransferase SelO, mitochondrial {ECO:0000305};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q9BVL4};
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:Q9BVL4};
DE AltName: Full=Selenoprotein O {ECO:0000250|UniProtKB:Q9BVL4};
DE Short=SelO {ECO:0000250|UniProtKB:Q9BVL4};
DE Flags: Precursor;
GN Name=Selenoo {ECO:0000312|MGI:MGI:1919007};
GN Synonyms=Selo {ECO:0000312|MGI:MGI:1919007};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-667.
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Ser, Thr and Tyr residues of target proteins (AMPylation). May be a
CC redox-active mitochondrial selenoprotein which interacts with a redox
CC target protein. {ECO:0000250|UniProtKB:Q9BVL4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC Evidence={ECO:0000250|UniProtKB:Q9BVL4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC Evidence={ECO:0000250|UniProtKB:Q9BVL4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein]
CC + diphosphate; Xref=Rhea:RHEA:58120, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15073, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:142516; Evidence={ECO:0000250|UniProtKB:Q9BVL4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q87VB1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BVL4}.
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48849.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB23774.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005048; BAB23774.1; ALT_SEQ; mRNA.
DR EMBL; AC113069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048849; AAH48849.1; ALT_SEQ; mRNA.
DR CCDS; CCDS27738.1; -.
DR RefSeq; NP_082181.2; NM_027905.3.
DR BioGRID; 230195; 11.
DR STRING; 10090.ENSMUSP00000081020; -.
DR iPTMnet; Q9DBC0; -.
DR PhosphoSitePlus; Q9DBC0; -.
DR SwissPalm; Q9DBC0; -.
DR EPD; Q9DBC0; -.
DR jPOST; Q9DBC0; -.
DR MaxQB; Q9DBC0; -.
DR PaxDb; Q9DBC0; -.
DR PeptideAtlas; Q9DBC0; -.
DR PRIDE; Q9DBC0; -.
DR ProteomicsDB; 257118; -.
DR Antibodypedia; 76483; 3 antibodies from 3 providers.
DR DNASU; 223776; -.
DR Ensembl; ENSMUST00000082439; ENSMUSP00000081020; ENSMUSG00000035757.
DR GeneID; 223776; -.
DR KEGG; mmu:223776; -.
DR UCSC; uc007xff.1; mouse.
DR CTD; 83642; -.
DR MGI; MGI:1919007; Selenoo.
DR VEuPathDB; HostDB:ENSMUSG00000035757; -.
DR eggNOG; KOG2542; Eukaryota.
DR GeneTree; ENSGT00390000005508; -.
DR HOGENOM; CLU_010245_4_0_1; -.
DR InParanoid; Q9DBC0; -.
DR OMA; RVQMLDY; -.
DR OrthoDB; 454947at2759; -.
DR PhylomeDB; Q9DBC0; -.
DR TreeFam; TF323296; -.
DR BioGRID-ORCS; 223776; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Selenoo; mouse.
DR PRO; PR:Q9DBC0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DBC0; protein.
DR Bgee; ENSMUSG00000035757; Expressed in left lobe of liver and 222 other tissues.
DR ExpressionAtlas; Q9DBC0; baseline and differential.
DR Genevisible; Q9DBC0; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; ISO:MGI.
DR GO; GO:0018117; P:protein adenylylation; ISO:MGI.
DR HAMAP; MF_00692; SelO; 1.
DR InterPro; IPR003846; SelO.
DR Pfam; PF02696; SelO; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Selenocysteine;
KW Transferase; Transit peptide.
FT TRANSIT 1..6
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 7..667
FT /note="Protein adenylyltransferase SelO, mitochondrial"
FT /id="PRO_0000121400"
FT REGION 58..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 154..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 189..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT NON_STD 665
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 635
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVL4"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVL4"
FT CONFLICT 619
FT /note="R -> L (in Ref. 1; BAB23774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 74221 MW; 5B5E772FDB8D9026 CRC64;
MASVRAAVGA SLAVARTRPR CVGLALPSSA PRSAWAAAME PTPRWLAGLR FDNRALRELP
VETPPPGPED SLATPRPVPG ACFSRARPAP LRRPRLVALS EPALALLGLE ASEEAEVEAE
AALFFSGNAL LPGTEPAAHC YCGHQFGQFA GQLGDGAAMY LGEVCTAAGE RWELQLKGAG
PTPFSRQADG RKVLRSSIRE FLCSEAMFHL GIPTTRAGAC VTSESTVMRD VFYDGNPKYE
KCTVVLRIAP TFIRFGSFEI FKPPDEHTGR AGPSVGRDDI RVQLLDYVIS SFYPEIQAAH
TCDTDNIQRN AAFFREVTQR TARMVAEWQC VGFCHGVLNT DNMSIVGLTI DYGPFGFLDR
YDPDHICNAS DNAGRYTYSK QPQVCKWNLQ KLAEALEPEL PLALAEAILK EEFDTEFQRH
YLQKMRKKLG LIRVEKEEDG TLVAKLLETM HLTGADFTNT FCVLSSFPAD LSDSAEFLSR
LTSQCASLEE LRLAFRPQMD PRQLSMMLML AQSNPQLFAL IGTQANVTKE LERVEHQSRL
EQLSPSDLQR KNRDHWEAWL QEYRDRLDKE KEGVGDTAAW QAERVRVMRA NNPKYVLRNY
IAQKAIEAAE NGDFSEVRRV LKLLESPYHS EEEATGPEAV ARSTEEQSSY SNRPPLWAAE
LCVTUSS
