ID   PYM1A_SALSA             Reviewed;         202 AA.
AC   B5XDD3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Partner of Y14 and mago A {ECO:0000250|UniProtKB:P82804};
DE   AltName: Full=PYM homolog 1 exon junction complex-associated factor A {ECO:0000250|UniProtKB:Q9BRP8};
DE   AltName: Full=Protein wibg homolog A;
GN   Name=pym1a {ECO:0000250|UniProtKB:Q9BRP8}; Synonyms=pyma, wibga;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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; BT049052; ACI68853.1; -; mRNA.
DR   AlphaFoldDB; B5XDD3; -.
DR   SMR; B5XDD3; -.
DR   STRING; 8030.ENSSSAP00000040163; -.
DR   Ensembl; ENSSSAT00000066364; ENSSSAP00000040163; ENSSSAG00000044441.
DR   Proteomes; UP000087266; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:1903259; P:exon-exon junction complex disassembly; IEA:InterPro.
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..202
FT                   /note="Partner of Y14 and mago A"
FT                   /id="PRO_0000378156"
FT   REGION          54..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          142..200
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        125..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   202 AA;  22397 MW;  A8FD28465F385D02 CRC64;
     MATPYVEDQS GKYIAATQRP DGTWRKPRRV KDGYTPQEEV PVYENKFVKF FKGKPDLPPG
     MSPGNAAQAR QQQGIPGIAE NEIAGLSKTA KRNMKRKEKR KQQGPDSNVE LLTNAVETMT
     FAEDGDNVTP ASNPAGATYD PSSAIAEKAK KIKNIKKKLR QVEELQQKLD SGEIKQATKE
     QQEKLGRAKA LQGELLQLEE DS