SYPM_MOUSE
ID SYPM_MOUSE Reviewed; 475 AA.
AC Q8CFI5; A2AVQ8; Q8R0C4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable proline--tRNA ligase, mitochondrial;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
DE Flags: Precursor;
GN Name=Pars2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Eye, and 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, and Spleen;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL929585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027073; AAH27073.1; -; mRNA.
DR EMBL; BC038817; AAH38817.1; -; mRNA.
DR CCDS; CCDS18423.1; -.
DR RefSeq; NP_001272713.1; NM_001285784.1.
DR RefSeq; NP_758476.2; NM_172272.2.
DR AlphaFoldDB; Q8CFI5; -.
DR SMR; Q8CFI5; -.
DR BioGRID; 230971; 9.
DR STRING; 10090.ENSMUSP00000102393; -.
DR iPTMnet; Q8CFI5; -.
DR PhosphoSitePlus; Q8CFI5; -.
DR EPD; Q8CFI5; -.
DR MaxQB; Q8CFI5; -.
DR PaxDb; Q8CFI5; -.
DR PRIDE; Q8CFI5; -.
DR ProteomicsDB; 254744; -.
DR Antibodypedia; 33219; 62 antibodies from 19 providers.
DR DNASU; 230577; -.
DR Ensembl; ENSMUST00000058905; ENSMUSP00000053160; ENSMUSG00000043572.
DR GeneID; 230577; -.
DR KEGG; mmu:230577; -.
DR UCSC; uc008typ.1; mouse.
DR CTD; 25973; -.
DR MGI; MGI:2386296; Pars2.
DR VEuPathDB; HostDB:ENSMUSG00000043572; -.
DR eggNOG; KOG2324; Eukaryota.
DR GeneTree; ENSGT00390000010922; -.
DR HOGENOM; CLU_016739_4_1_1; -.
DR InParanoid; Q8CFI5; -.
DR BioGRID-ORCS; 230577; 28 hits in 79 CRISPR screens.
DR PRO; PR:Q8CFI5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CFI5; protein.
DR Bgee; ENSMUSG00000043572; Expressed in cortical plate and 186 other tissues.
DR ExpressionAtlas; Q8CFI5; baseline and differential.
DR Genevisible; Q8CFI5; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..475
FT /note="Probable proline--tRNA ligase, mitochondrial"
FT /id="PRO_0000035819"
FT CONFLICT 240
FT /note="Q -> R (in Ref. 2; AAH38817)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="S -> G (in Ref. 2; AAH38817)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="I -> V (in Ref. 2; AAH38817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 53518 MW; 184D4DCA2B226549 CRC64;
MEGLLTRCRT LSALAACSLR HCRYIIHKCY HRAPGRGQRL VLSRMFQPQN LREDQVLSLE
GRASDLTCKS QRLMLQVGLI LPASPGCYHL MPYTVRAVEK LVRVIDQEMQ AIGGQKINMP
SLSPAELWRA TSRWDLMGRE LLRLRDRHGK EYCLGPTHEE AVTALVASQK KLSYKQLPLL
LYQVTRKFRD EPRPRFGLLR GREFYMKDMY TFDSSSEAAQ ETYGLVCDAY CRLFDRLGLQ
WMKARADVGS IGGTMSHEFQ LPVDIGEDRL VVCPSCHFSA NTEILDLSQK ICPDCQGPLT
ETKGIEVGHT FYLSTKYSSI FNALFTNAHG ESLLAEMGCY GLGVTRILAA AIEVLSTEDC
IRWPRLLAPY QVCVIPPKKG SKETAATEIV EKLYDDIMEA VPQLRGEVLL DDRTHLTIGN
RLKDANKLGY PFVIIAGKRA LEDPAHFEVW SQNTGEVVFL TKEGVMELLT GVHVV
