PYM1_BOVIN
ID PYM1_BOVIN Reviewed; 203 AA.
AC A6QPH1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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 -!- DOMAIN: The eIF2A-like region shares sequence similarity with eIF2A and
CC mediates the interaction with the 40S ribosomal subunit and the 48S
CC preinitiation complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR EMBL; BC149320; AAI49321.1; -; mRNA.
DR RefSeq; NP_001095814.1; NM_001102344.1.
DR AlphaFoldDB; A6QPH1; -.
DR SMR; A6QPH1; -.
DR STRING; 9913.ENSBTAP00000041588; -.
DR PaxDb; A6QPH1; -.
DR PeptideAtlas; A6QPH1; -.
DR PRIDE; A6QPH1; -.
DR Ensembl; ENSBTAT00000044075; ENSBTAP00000041588; ENSBTAG00000031146.
DR GeneID; 787259; -.
DR KEGG; bta:787259; -.
DR CTD; 84305; -.
DR VEuPathDB; HostDB:ENSBTAG00000031146; -.
DR VGNC; VGNC:33592; PYM1.
DR eggNOG; KOG4325; Eukaryota.
DR GeneTree; ENSGT00730000111107; -.
DR HOGENOM; CLU_074603_3_0_1; -.
DR InParanoid; A6QPH1; -.
DR OMA; IPGCADS; -.
DR OrthoDB; 1545729at2759; -.
DR TreeFam; TF324615; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000031146; Expressed in anterior segment of eyeball and 104 other tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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 Phosphoprotein; Reference proteome; Translation regulation.
FT CHAIN 1..203
FT /note="Partner of Y14 and mago"
FT /id="PRO_0000378155"
FT REGION 1..32
FT /note="Required for interaction with MAGOH and RBM8A"
FT /evidence="ECO:0000250"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..203
FT /note="eIF2A-like"
FT /evidence="ECO:0000250"
FT COILED 81..116
FT /evidence="ECO:0000255"
FT COILED 144..203
FT /evidence="ECO:0000255"
FT COMPBIAS 115..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRP8"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRP8"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRP8"
SQ SEQUENCE 203 AA; 22663 MW; 2B579363CD97F45A CRC64;
MATPYVTDET GGKYIASTQR PDGTWRKQRR VKEGYVPQEE VPVYENKYVK FFKSKPELPP
GLSPEATAPI TASRPEGGEP ALSKTAKRNL KRKEKRRQQQ EKGEAEALSR TLEKVSLGET
AQVPSAPQAS RAAPTAASDQ PDSAATTEKA KKIKNLKKKL RQVEELQQRI QAGEISQPSK
EQLEKLARRR ALEEELEDLE LGL
