##gff-version 3 Q8CGC7 UniProtKB Chain 1 1512 . . . ID=PRO_0000119744;Note=Bifunctional glutamate/proline--tRNA ligase Q8CGC7 UniProtKB Domain 749 805 . . . Note=WHEP-TRS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00531 Q8CGC7 UniProtKB Domain 822 878 . . . Note=WHEP-TRS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00531 Q8CGC7 UniProtKB Domain 900 956 . . . Note=WHEP-TRS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00531 Q8CGC7 UniProtKB Region 164 759 . . . Note=Glutamate--tRNA ligase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28668 Q8CGC7 UniProtKB Region 294 315 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Region 709 742 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Region 760 956 . . . Note=3 X 57 AA approximate repeats;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Region 795 819 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Region 869 898 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Region 956 1011 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Region 1007 1512 . . . Note=Proline--tRNA ligase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28668 Q8CGC7 UniProtKB Motif 204 214 . . . Note='HIGH' region;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28668 Q8CGC7 UniProtKB Motif 432 436 . . . Note='KMSKS' region;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28668 Q8CGC7 UniProtKB Compositional bias 710 732 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Compositional bias 804 819 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Compositional bias 875 892 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Compositional bias 956 981 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Compositional bias 982 1000 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8CGC7 UniProtKB Binding site 1121 1123 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1152 1152 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1152 1152 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1154 1154 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1163 1163 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1164 1164 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1237 1237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1237 1237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1240 1240 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1242 1242 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1276 1276 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1278 1278 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1448 1448 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1453 1453 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1495 1495 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Binding site 1497 1497 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 300 300 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8CGC7 UniProtKB Modified residue 300 300 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 355 355 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 417 417 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 498 498 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 535 535 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 542 542 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 637 637 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 788 788 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8CGC7 UniProtKB Modified residue 861 861 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8CGC7 UniProtKB Modified residue 872 872 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 885 885 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 998 998 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 999 999 . . . Note=Phosphoserine%3B by RPS6KB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23071094;Dbxref=PMID:23071094 Q8CGC7 UniProtKB Modified residue 1152 1152 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 1350 1350 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Modified residue 1503 1503 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07814 Q8CGC7 UniProtKB Mutagenesis 999 999 . . . Note=Loss of function in translation inhibition. Loss of interaction with SLC27A1. Mutant mice have no apparent developmental defect but display reduced adiposity associated with decreased insulin levels and adipocytes size. They also display increased lipolysis and fatty acid beta-oxidation and an extended lifespan. Adipocytes display decreased insulin-stimulated long-chain fatty acid uptake. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23071094,ECO:0000269|PubMed:28178239;Dbxref=PMID:23071094,PMID:28178239 Q8CGC7 UniProtKB Mutagenesis 999 999 . . . Note=Constitutively active in translation inhibition (phosphomimetic). Mutant mice have no apparent developmental defect and do not display overt phenotype related to adiposity or lifespan. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23071094,ECO:0000269|PubMed:28178239;Dbxref=PMID:23071094,PMID:28178239 Q8CGC7 UniProtKB Sequence conflict 94 94 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8CGC7 UniProtKB Sequence conflict 172 172 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8CGC7 UniProtKB Sequence conflict 618 618 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8CGC7 UniProtKB Sequence conflict 986 986 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8CGC7 UniProtKB Sequence conflict 1290 1290 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305