ID PYM_DROME Reviewed; 207 AA.
AC P82804;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 142.
DE RecName: Full=Partner of Y14 and mago {ECO:0000312|FlyBase:FBgn0034918};
DE Short=DmPYM;
DE AltName: Full=Protein within the bgcn gene intron;
GN Name=Pym {ECO:0000312|FlyBase:FBgn0034918};
GN Synonyms=wibg {ECO:0000312|FlyBase:FBgn0034918};
GN ORFNames=CG30176 {ECO:0000312|FlyBase:FBgn0034918};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAG00610.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=10924476; DOI=10.1093/genetics/155.4.1809;
RA Ohlstein B., Lavoie C.A., Vef O., Gateff E., McKearin D.M.;
RT "The Drosophila cystoblast differentiation factor, benign gonial cell
RT neoplasm, is related to DExH-box proteins and interacts genetically with
RT bag-of-marbles.";
RL Genetics 155:1809-1819(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH MAGO AND TSU.
RX PubMed=12483225; DOI=10.1038/nbt773;
RA Forler D., Kocher T., Rode M., Gentzel M., Izaurralde E., Wilm M.;
RT "An efficient protein complex purification method for functional proteomics
RT in higher eukaryotes.";
RL Nat. Biotechnol. 21:89-92(2003).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH MAGO AND TSU.
RX PubMed=24967911; DOI=10.1371/journal.pgen.1004455;
RA Ghosh S., Obrdlik A., Marchand V., Ephrussi A.;
RT "The EJC binding and dissociating activity of PYM is regulated in
RT Drosophila.";
RL PLoS Genet. 10:E1004455-E1004455(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-58 IN COMPLEX WITH MAGO AND TSU,
RP AND SUBCELLULAR LOCATION.
RX PubMed=14968132; DOI=10.1038/sj.embor.7400091;
RA Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.;
RT "Molecular insights into the interaction of PYM with the Mago-Y14 core of
RT the exon junction complex.";
RL EMBO Rep. 5:304-310(2004).
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 landmark 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. Acts as an EJC disassembly factor by disrupting mature EJC
CC from spliced mRNAs. Required for normal localization of osk mRNA to the
CC posterior pole of the developing oocyte. Does not interact with the
CC small ribosomal unit or components of the translation initiation
CC complex. May not function in cap-dependent translation regulation.
CC {ECO:0000269|PubMed:24967911}.
CC -!- SUBUNIT: Interacts (via N-terminus) with mago and tsu/RBM8A; the
CC interaction is direct. {ECO:0000269|PubMed:12483225,
CC ECO:0000269|PubMed:14968132, ECO:0000269|PubMed:24967911}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14968132,
CC ECO:0000269|PubMed:24967911}. Nucleus {ECO:0000269|PubMed:14968132}.
CC Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is
CC mediated by emb/Crm1. {ECO:0000269|PubMed:14968132,
CC ECO:0000269|PubMed:24967911}.
CC -!- TISSUE SPECIFICITY: Expression detected in the ovary. In the oocyte
CC expressed in the germarium, nurse cell and follicle cell.
CC {ECO:0000269|PubMed:24967911}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile. No visible phenotype.
CC {ECO:0000269|PubMed:24967911}.
CC -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR EMBL; AF293388; AAG00610.1; -; mRNA.
DR EMBL; AJ459405; CAD30676.1; -; mRNA.
DR EMBL; AE013599; AAM68273.1; -; Genomic_DNA.
DR EMBL; AY070957; AAL48579.1; -; mRNA.
DR EMBL; AY071704; AAL49326.1; -; mRNA.
DR RefSeq; NP_726372.1; NM_166627.3.
DR PDB; 1RK8; X-ray; 1.90 A; C=1-58.
DR PDBsum; 1RK8; -.
DR AlphaFoldDB; P82804; -.
DR SMR; P82804; -.
DR BioGRID; 63373; 3.
DR ComplexPortal; CPX-3147; PYM-mago-Y14 complex.
DR IntAct; P82804; 3.
DR STRING; 7227.FBpp0072142; -.
DR PaxDb; 7227-FBpp0072142; -.
DR DNASU; 37780; -.
DR EnsemblMetazoa; FBtr0072233; FBpp0072142; FBgn0034918.
DR GeneID; 37780; -.
DR KEGG; dme:Dmel_CG30176; -.
DR AGR; FB:FBgn0034918; -.
DR CTD; 37780; -.
DR FlyBase; FBgn0034918; Pym.
DR VEuPathDB; VectorBase:FBgn0034918; -.
DR eggNOG; KOG4325; Eukaryota.
DR GeneTree; ENSGT00730000111107; -.
DR HOGENOM; CLU_074603_3_0_1; -.
DR InParanoid; P82804; -.
DR OMA; IPGCADS; -.
DR OrthoDB; 1216579at2759; -.
DR PhylomeDB; P82804; -.
DR SignaLink; P82804; -.
DR BioGRID-ORCS; 37780; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P82804; -.
DR GenomeRNAi; 37780; -.
DR PRO; PR:P82804; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034918; Expressed in adult abdomen and 20 other cell types or tissues.
DR Genevisible; P82804; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
DR GO; GO:1990448; F:exon-exon junction complex binding; IPI:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:1903259; P:exon-exon junction complex disassembly; IMP:FlyBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR DisProt; DP02384; -.
DR InterPro; IPR039333; PYM1.
DR InterPro; IPR015362; WIBG_mago-bd.
DR InterPro; IPR036348; WIBG_N_sf.
DR PANTHER; PTHR22959:SF0; PARTNER OF Y14 AND MAGO; 1.
DR PANTHER; PTHR22959; PYM PROTEIN; 1.
DR Pfam; PF09282; Mago-bind; 1.
DR SMART; SM01273; Mago-bind; 1.
DR SUPFAM; SSF101931; Pym (Within the bgcn gene intron protein, WIBG), N-terminal domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..207
FT /note="Partner of Y14 and mago"
FT /id="PRO_0000065972"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..91
FT /evidence="ECO:0000255"
FT COILED 152..184
FT /evidence="ECO:0000255"
FT COMPBIAS 67..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1RK8"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1RK8"
SQ SEQUENCE 207 AA; 23450 MW; F7E6B7C98A2961DE CRC64;
MSTYLQSSEG KFIPATKRPD GTWRKARRVK DGYVPQEEVP LYESKGKQFV AQRQAGVPPG
MCPLLAAESK KEREKQERTR AKKQEKESGR QPKAPAPGVL VMPPSTCPPP KVSQQQQQQQ
QQPSGSRDIN SISKTLEDTL KLDAAQEVVD PAKQLKKLRK KIREIEQIES RIQAGEQKKL
DKDQLDKVKK KSEILRQIKD LESTPRS
//
