PYM1_XENTR
ID PYM1_XENTR Reviewed; 200 AA.
AC B1WB17; B7ZSP7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804};
DE AltName: Full=PYM homolog 1 exon junction complex-associated factor {ECO:0000250|UniProtKB:Q9BRP8};
DE AltName: Full=Protein wibg homolog;
GN Name=pym1 {ECO:0000250|UniProtKB:Q9BRP8}; Synonyms=pym, wibg;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key regulator of the exon junction complex (EJC), a
CC multiprotein complex that associates immediately upstream of the exon-
CC exon junction on mRNAs and serves as a positional landmark for the
CC intron exon structure of genes and directs post-transcriptional
CC processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA
CC decay (NMD) or translation. Acts as an EJC disassembly factor, allowing
CC translation-dependent EJC removal and recycling by disrupting mature
CC EJC from spliced mRNAs. Its association with the 40S ribosomal subunit
CC probably prevents a translation-independent disassembly of the EJC from
CC spliced mRNAs, by restricting its activity to mRNAs that have been
CC translated. Interferes with NMD and enhances translation of spliced
CC mRNAs, probably by antagonizing EJC functions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with magoh and rbm8a; the
CC interaction is direct. Associates (eIF2A-like region) with the 40S
CC ribosomal subunit and the 48S preinitiation complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRP8}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BRP8}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9BRP8}. Note=Shuttles between the nucleus and
CC the cytoplasm. Nuclear export is mediated by XPO1/CRM1.
CC {ECO:0000250|UniProtKB:Q9BRP8}.
CC -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR EMBL; BC161580; AAI61580.1; -; mRNA.
DR EMBL; BC170597; AAI70597.1; -; mRNA.
DR EMBL; BC170601; AAI70601.1; -; mRNA.
DR RefSeq; NP_001016274.1; NM_001016274.2.
DR AlphaFoldDB; B1WB17; -.
DR SMR; B1WB17; -.
DR STRING; 8364.ENSXETP00000047260; -.
DR PaxDb; B1WB17; -.
DR GeneID; 549028; -.
DR KEGG; xtr:549028; -.
DR CTD; 84305; -.
DR Xenbase; XB-GENE-943122; pym1.
DR eggNOG; KOG4325; Eukaryota.
DR HOGENOM; CLU_074603_3_0_1; -.
DR InParanoid; B1WB17; -.
DR OrthoDB; 1545729at2759; -.
DR TreeFam; TF324615; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035145; C:exon-exon junction complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1903259; P:exon-exon junction complex disassembly; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR InterPro; IPR039333; PYM1.
DR InterPro; IPR015362; WIBG_mago-bd.
DR InterPro; IPR036348; WIBG_N_sf.
DR PANTHER; PTHR22959; PTHR22959; 1.
DR Pfam; PF09282; Mago-bind; 1.
DR SMART; SM01273; Mago-bind; 1.
DR SUPFAM; SSF101931; SSF101931; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW Reference proteome; Translation regulation.
FT CHAIN 1..200
FT /note="Partner of Y14 and mago"
FT /id="PRO_0000378158"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 84..200
FT /evidence="ECO:0000255"
FT COMPBIAS 60..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 146
FT /note="K -> R (in Ref. 1; AAI70601/AAI70597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22854 MW; 8BEA0CE8FA904C53 CRC64;
MATPYVTDES GKYIAATQRP DGSWRKQRKV KEGYVPQEEV PVYENKYVKF FKSKPSLPPG
LSETDASTGK TQQPSKPDAD TTLSKTAKRN MKRKEKRKQE KGEREQVEDA RQDLERVNIS
ETPVQKNLTS AHKNGSASSD NPAAEKAKKI KNLRKKLRQV EELQQKIDSG EIKEPSKEQL
EKLSRRKALE EEIEDLELDL