SELO_HUMAN
ID SELO_HUMAN Reviewed; 669 AA.
AC Q9BVL4; Q2TAL2; Q5JZ81; Q8WUI0;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein adenylyltransferase SelO, mitochondrial {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:30270044};
DE EC=2.7.7.n1 {ECO:0000269|PubMed:30270044};
DE AltName: Full=Selenoprotein O {ECO:0000303|PubMed:27645994};
DE Short=SelO {ECO:0000303|PubMed:12775843, ECO:0000303|PubMed:24751718, ECO:0000303|PubMed:27645994};
DE Flags: Precursor;
GN Name=SELENOO {ECO:0000312|HGNC:HGNC:30395};
GN Synonyms=SELO {ECO:0000303|PubMed:12775843, ECO:0000303|PubMed:24751718,
GN ECO:0000303|PubMed:27645994};
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].
RX PubMed=12775843; DOI=10.1126/science.1083516;
RA Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O.,
RA Guigo R., Gladyshev V.N.;
RT "Characterization of mammalian selenoproteomes.";
RL Science 300:1439-1443(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-3 AND ASN-167.
RC TISSUE=Brain, Colon, and Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-635 AND SER-653, AND
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 664-CYS--SEC-667; CYS-664 AND SEC-667.
RX PubMed=24751718; DOI=10.1371/journal.pone.0095518;
RA Han S.J., Lee B.C., Yim S.H., Gladyshev V.N., Lee S.R.;
RT "Characterization of mammalian selenoprotein o: a redox-active
RT mitochondrial protein.";
RL PLoS ONE 9:E95518-E95518(2014).
RN [6]
RP NOMENCLATURE.
RX PubMed=27645994; DOI=10.1074/jbc.m116.756155;
RA Gladyshev V.N., Arner E.S., Berry M.J., Brigelius-Flohe R., Bruford E.A.,
RA Burk R.F., Carlson B.A., Castellano S., Chavatte L., Conrad M.,
RA Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A., Flohe L.,
RA Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J., Hoffmann P.R.,
RA Holmgren A., Hondal R.J., Howard M.T., Huang K., Kim H.Y., Kim I.Y.,
RA Koehrle J., Krol A., Kryukov G.V., Lee B.J., Lee B.C., Lei X.G., Liu Q.,
RA Lescure A., Lobanov A.V., Loscalzo J., Maiorino M., Mariotti M.,
RA Sandeep Prabhu K., Rayman M.P., Rozovsky S., Salinas G., Schmidt E.E.,
RA Schomburg L., Schweizer U., Simonovic M., Sunde R.A., Tsuji P.A.,
RA Tweedie S., Ursini F., Whanger P.D., Zhang Y.;
RT "Selenoprotein gene nomenclature.";
RL J. Biol. Chem. 291:24036-24040(2016).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-348.
RX PubMed=30270044; DOI=10.1016/j.cell.2018.08.046;
RA Sreelatha A., Yee S.S., Lopez V.A., Park B.C., Kinch L.N., Pilch S.,
RA Servage K.A., Zhang J., Jiou J., Karasiewicz-Urbanska M., Lobocka M.,
RA Grishin N.V., Orth K., Kucharczyk R., Pawlowski K., Tomchick D.R.,
RA Tagliabracci V.S.;
RT "Protein AMPylation by an Evolutionarily Conserved Pseudokinase.";
RL Cell 175:809-821(2018).
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Ser, Thr and Tyr residues of target proteins (AMPylation)
CC (PubMed:30270044). May be a redox-active mitochondrial selenoprotein
CC which interacts with a redox target protein (PubMed:24751718).
CC {ECO:0000269|PubMed:24751718, ECO:0000269|PubMed:30270044}.
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:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC Evidence={ECO:0000269|PubMed:30270044};
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:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54293;
CC Evidence={ECO:0000269|PubMed:30270044};
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:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58121;
CC Evidence={ECO:0000269|PubMed:30270044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q87VB1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24751718}.
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01099.3; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH20510.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY324823; AAP85540.1; -; mRNA.
DR EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001099; AAH01099.3; ALT_SEQ; mRNA.
DR EMBL; BC020510; AAH20510.1; ALT_SEQ; mRNA.
DR EMBL; BC110866; AAI10867.1; -; mRNA.
DR CCDS; CCDS43034.1; -.
DR RefSeq; NP_113642.1; NM_031454.1.
DR BioGRID; 123706; 39.
DR IntAct; Q9BVL4; 16.
DR MINT; Q9BVL4; -.
DR STRING; 9606.ENSP00000370288; -.
DR iPTMnet; Q9BVL4; -.
DR PhosphoSitePlus; Q9BVL4; -.
DR SwissPalm; Q9BVL4; -.
DR BioMuta; SELENOO; -.
DR DMDM; 172045770; -.
DR EPD; Q9BVL4; -.
DR jPOST; Q9BVL4; -.
DR MassIVE; Q9BVL4; -.
DR MaxQB; Q9BVL4; -.
DR PaxDb; Q9BVL4; -.
DR PeptideAtlas; Q9BVL4; -.
DR PRIDE; Q9BVL4; -.
DR ProteomicsDB; 79218; -.
DR Antibodypedia; 76483; 3 antibodies from 3 providers.
DR DNASU; 83642; -.
DR Ensembl; ENST00000380903.7; ENSP00000370288.2; ENSG00000073169.15.
DR GeneID; 83642; -.
DR KEGG; hsa:83642; -.
DR MANE-Select; ENST00000380903.7; ENSP00000370288.2; NM_031454.2; NP_113642.1.
DR CTD; 83642; -.
DR DisGeNET; 83642; -.
DR GeneCards; SELENOO; -.
DR HGNC; HGNC:30395; SELENOO.
DR HPA; ENSG00000073169; Tissue enhanced (liver).
DR MIM; 607917; gene.
DR neXtProt; NX_Q9BVL4; -.
DR OpenTargets; ENSG00000073169; -.
DR VEuPathDB; HostDB:ENSG00000073169; -.
DR eggNOG; KOG2542; Eukaryota.
DR GeneTree; ENSGT00390000005508; -.
DR InParanoid; Q9BVL4; -.
DR OMA; RVQMLDY; -.
DR OrthoDB; 454947at2759; -.
DR PhylomeDB; Q9BVL4; -.
DR PathwayCommons; Q9BVL4; -.
DR SignaLink; Q9BVL4; -.
DR BioGRID-ORCS; 83642; 8 hits in 1029 CRISPR screens.
DR ChiTaRS; SELENOO; human.
DR GenomeRNAi; 83642; -.
DR Pharos; Q9BVL4; Tdark.
DR PRO; PR:Q9BVL4; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9BVL4; protein.
DR Bgee; ENSG00000073169; Expressed in pancreatic ductal cell and 183 other tissues.
DR ExpressionAtlas; Q9BVL4; baseline and differential.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA: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; IDA:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
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..115
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 116..669
FT /note="Protein adenylyltransferase SelO, mitochondrial"
FT /id="PRO_0000121399"
FT REGION 58..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 153..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 188..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:30270044"
FT NON_STD 667
FT /note="Selenocysteine"
FT MOD_RES 635
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 3
FT /note="V -> A (in dbSNP:rs5771225)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059952"
FT VARIANT 167
FT /note="T -> N (in dbSNP:rs2272846)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059953"
FT VARIANT 630
FT /note="E -> K (in dbSNP:rs2272852)"
FT /id="VAR_059954"
FT VARIANT 638
FT /note="E -> K (in dbSNP:rs17013238)"
FT /id="VAR_059955"
FT MUTAGEN 348
FT /note="D->A: Loss of catalytic activity. Loss of ATP
FT binding."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 664..667
FT /note="CVTU->SVTC: Enhances redox complex formation."
FT /evidence="ECO:0000269|PubMed:24751718"
FT MUTAGEN 664..667
FT /note="CVTU->SVTS: Abolishes redox complex formation."
FT /evidence="ECO:0000269|PubMed:24751718"
FT MUTAGEN 664
FT /note="C->S: No effect on redox complex formation."
FT /evidence="ECO:0000269|PubMed:24751718"
FT MUTAGEN 667
FT /note="U->C: Slightly enhances redox complex formation."
FT /evidence="ECO:0000269|PubMed:24751718"
FT MUTAGEN 667
FT /note="U->S: No effect on redox complex formation."
FT /evidence="ECO:0000269|PubMed:24751718"
FT CONFLICT 253
FT /note="R -> RGWGQVWPVDASGLPSR (in Ref. 3; AAH20510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73489 MW; F2242E25B2E0EE68 CRC64;
MAVYRAALGA SLAAARLLPL GRCSPSPAPR STLSGAAMEP APRWLAGLRF DNRALRALPV
EAPPPGPEGA PSAPRPVPGA CFTRVQPTPL RQPRLVALSE PALALLGLGA PPAREAEAEA
ALFFSGNALL PGAEPAAHCY CGHQFGQFAG QLGDGAAMYL GEVCTATGER WELQLKGAGP
TPFSRQADGR KVLRSSIREF LCSEAMFHLG VPTTRAGACV TSESTVVRDV FYDGNPKYEQ
CTVVLRVAST FIRFGSFEIF KSADEHTGRA GPSVGRNDIR VQLLDYVISS FYPEIQAAHA
SDSVQRNAAF FREVTRRTAR MVAEWQCVGF CHGVLNTDNM SILGLTIDYG PFGFLDRYDP
DHVCNASDNT GRYAYSKQPE VCRWNLRKLA EALQPELPLE LGEAILAEEF DAEFQRHYLQ
KMRRKLGLVQ VELEEDGALV SKLLETMHLT GADFTNTFYL LSSFPVELES PGLAEFLARL
MEQCASLEEL RLAFRPQMDP RQLSMMLMLA QSNPQLFALM GTRAGIAREL ERVEQQSRLE
QLSAAELQSR NQGHWADWLQ AYRARLDKDL EGAGDAAAWQ AEHVRVMHAN NPKYVLRNYI
AQNAIEAAER GDFSEVRRVL KLLETPYHCE AGAATDAEAT EADGADGRQR SYSSKPPLWA
AELCVTUSS
