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PYM_DROME
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   03-AUG-2022, entry version 138.
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; P82804; -.
DR   PRIDE; P82804; -.
DR   DNASU; 37780; -.
DR   EnsemblMetazoa; FBtr0072233; FBpp0072142; FBgn0034918.
DR   GeneID; 37780; -.
DR   KEGG; dme:Dmel_CG30176; -.
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; 1545729at2759; -.
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 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; PTHR22959; 1.
DR   Pfam; PF09282; Mago-bind; 1.
DR   SMART; SM01273; Mago-bind; 1.
DR   SUPFAM; SSF101931; SSF101931; 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
 
 
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