PYM_AEDAE
ID PYM_AEDAE Reviewed; 253 AA.
AC Q16LW2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804};
DE AltName: Full=Protein wibg homolog;
GN Name=Pym {ECO:0000250|UniProtKB:P82804}; Synonyms=wibg;
GN ORFNames=AAEL012503;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Regulator of the exon junction complex (EJC), a multiprotein
CC complex that associates immediately upstream of the exon-exon junction
CC on mRNAs and serves as a positional landmarks for the intron exon
CC structure of genes and directs post-transcriptional processes in the
CC cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or
CC translation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with mago and tsu/Y14; the
CC interaction is direct. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is
CC mediated by emb/Crm1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH477889; EAT35312.1; -; Genomic_DNA.
DR RefSeq; XP_001656113.1; XM_001656063.1.
DR AlphaFoldDB; Q16LW2; -.
DR SMR; Q16LW2; -.
DR STRING; 7159.AAEL012503-PA; -.
DR GeneID; 5576411; -.
DR KEGG; aag:5576411; -.
DR VEuPathDB; VectorBase:AAEL012503; -.
DR eggNOG; KOG4325; Eukaryota.
DR HOGENOM; CLU_074603_3_0_1; -.
DR InParanoid; Q16LW2; -.
DR OMA; MAKLESW; -.
DR OrthoDB; 1363113at2759; -.
DR PhylomeDB; Q16LW2; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035145; C:exon-exon junction complex; 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 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 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..253
FT /note="Partner of Y14 and mago"
FT /id="PRO_0000378159"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..156
FT /evidence="ECO:0000255"
FT COILED 189..221
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 29140 MW; AD36B822C6A0F1B8 CRC64;
MTTYATDSQG KFIPSTQRPD GTWRKPRRVR DGYVPQEEVP LYESKGKLFA QKPLLPPGMS
PEMAQKSREK REREQRIKQQ READANRRPP QNPVPGLLIL NGDSKINQPQ QRAAKSAKPK
KKAVELPDVL LEQKQKEEQK QVRQQQQQQK SQKDHKNTKP HHQERIEEVA KAMNGLQLTN
NHVASASAAD ALQTDLSKKL RKLRKKIREI EIIEERLRST DGGPRPDKDQ IDKAKRKPEI
LKEIEELEKG IAK