PSTK_MOUSE
ID PSTK_MOUSE Reviewed; 359 AA.
AC Q8BP74; Q0D2I7; Q14C09;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=L-seryl-tRNA(Sec) kinase;
DE EC=2.7.1.164 {ECO:0000269|PubMed:15317934};
DE AltName: Full=O-phosphoseryl-tRNA(Sec) kinase;
GN Name=Pstk;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 MRNA] (ISOFORM 1).
RC STRAIN=Mix FVB/N; 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 [3]
RP FUNCTION, COFACTOR, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=15317934; DOI=10.1073/pnas.0402636101;
RA Carlson B.A., Xu X.M., Kryukov G.V., Rao M., Berry M.J., Gladyshev V.N.,
RA Hatfield D.L.;
RT "Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12848-12853(2004).
CC -!- FUNCTION: Specifically phosphorylates seryl-tRNA(Sec) to O-
CC phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine
CC biosynthesis. No activity with other tRNAs has been detected.
CC {ECO:0000269|PubMed:15317934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec);
CC Xref=Rhea:RHEA:25037, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:78533, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:456216; EC=2.7.1.164;
CC Evidence={ECO:0000269|PubMed:15317934};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15317934};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (archaeal/eukaryal route): step 1/2. {ECO:0000305|PubMed:15317934}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BP74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BP74-2; Sequence=VSP_024860;
CC -!- SIMILARITY: Belongs to the L-seryl-tRNA(Sec) kinase family.
CC {ECO:0000305}.
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DR EMBL; AK077585; BAC36878.1; -; mRNA.
DR EMBL; BC110381; AAI10382.1; -; mRNA.
DR EMBL; BC115503; AAI15504.2; -; mRNA.
DR CCDS; CCDS21914.1; -. [Q8BP74-1]
DR RefSeq; NP_001034623.1; NM_001039534.1. [Q8BP74-1]
DR AlphaFoldDB; Q8BP74; -.
DR STRING; 10090.ENSMUSP00000075037; -.
DR PhosphoSitePlus; Q8BP74; -.
DR EPD; Q8BP74; -.
DR MaxQB; Q8BP74; -.
DR PaxDb; Q8BP74; -.
DR PeptideAtlas; Q8BP74; -.
DR PRIDE; Q8BP74; -.
DR ProteomicsDB; 291579; -. [Q8BP74-1]
DR ProteomicsDB; 291580; -. [Q8BP74-2]
DR Antibodypedia; 46364; 66 antibodies from 15 providers.
DR DNASU; 214580; -.
DR Ensembl; ENSMUST00000075610; ENSMUSP00000075037; ENSMUSG00000063179. [Q8BP74-1]
DR Ensembl; ENSMUST00000145114; ENSMUSP00000118636; ENSMUSG00000063179. [Q8BP74-2]
DR GeneID; 214580; -.
DR KEGG; mmu:214580; -.
DR UCSC; uc009kbh.1; mouse. [Q8BP74-1]
DR CTD; 118672; -.
DR MGI; MGI:2685945; Pstk.
DR VEuPathDB; HostDB:ENSMUSG00000063179; -.
DR eggNOG; KOG4622; Eukaryota.
DR GeneTree; ENSGT00390000017554; -.
DR HOGENOM; CLU_060632_0_0_1; -.
DR InParanoid; Q8BP74; -.
DR OMA; VHLCYDD; -.
DR OrthoDB; 1322551at2759; -.
DR PhylomeDB; Q8BP74; -.
DR TreeFam; TF321264; -.
DR BioCyc; MetaCyc:MON-14957; -.
DR BRENDA; 2.7.1.164; 3474.
DR UniPathway; UPA00906; UER00897.
DR BioGRID-ORCS; 214580; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Pstk; mouse.
DR PRO; PR:Q8BP74; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BP74; protein.
DR Bgee; ENSMUSG00000063179; Expressed in hindlimb stylopod muscle and 249 other tissues.
DR ExpressionAtlas; Q8BP74; baseline and differential.
DR Genevisible; Q8BP74; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0043915; F:L-seryl-tRNA(Sec) kinase activity; IDA:MGI.
DR GO; GO:0000049; F:tRNA binding; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IDA:MGI.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR013641; KTI12/PSTK.
DR InterPro; IPR020028; L-seryl-tRNA_Sec_kinase_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08433; KTI12; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03575; selen_PSTK_euk; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="L-seryl-tRNA(Sec) kinase"
FT /id="PRO_0000097081"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 263..359
FT /note="ETDRIICSTNILHKADETLRRTVSQTMREAKDEQIPLNNLKHLAEELNKLKA
FT DVLEDLRQGNRKYLCFQQTTDLSDIISSFCKERDTIVQKYFSKQH -> NYLFY (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024860"
SQ SEQUENCE 359 AA; 40763 MW; E43BED6554DFFB2E CRC64;
MKTAAARGAT RRDGQPKLGL CVLCGLPAAG KSTFARALAL RLRRERGWAV GVLSYDDVLP
LALPDCDGTQ PRPSQWKMFR QELLKHLECF LVAVISGAQM SAPPNRTEAV WEDFITCLKS
QDLMIFPTAL EAQPCHLLAK PAVSRPLFLV LDDNFYYQSM RYEVYQLARK YSLGFCQLFL
DCPLETCLKR NGERSQPLPD ETIQLMGRKI EKPNPEKNAW EHNSLIIQSS ACSLEASLEV
TGLLLTALEN PIKCVEDNTE QKETDRIICS TNILHKADET LRRTVSQTMR EAKDEQIPLN
NLKHLAEELN KLKADVLEDL RQGNRKYLCF QQTTDLSDII SSFCKERDTI VQKYFSKQH
