PCID2_DROME
ID PCID2_DROME Reviewed; 395 AA.
AC Q9VTL1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=PCI domain-containing protein 2 homolog {ECO:0000303|PubMed:27016737};
DE AltName: Full=CSN12-like protein;
GN Name=PCID2 {ECO:0000303|PubMed:27016737, ECO:0000312|FlyBase:FBgn0036184};
GN ORFNames=CG7351 {ECO:0000312|FlyBase:FBgn0036184};
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;
RN [1]
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 [2]
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 [3]
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 [4]
RP FUNCTION, INTERACTION WITH SBR, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=18086857; DOI=10.1101/gad.1616008;
RA Farny N.G., Hurt J.A., Silver P.A.;
RT "Definition of global and transcript-specific mRNA export pathways in
RT metazoans.";
RL Genes Dev. 22:66-78(2008).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE AMEX COMPLEX, INTERACTION WITH ORC3 AND
RP ORC4, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=27016737; DOI=10.1093/nar/gkw192;
RA Kopytova D., Popova V., Kurshakova M., Shidlovskii Y., Nabirochkina E.,
RA Brechalov A., Georgiev G., Georgieva S.;
RT "ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association
RT with mRNP and mRNA export in Drosophila.";
RL Nucleic Acids Res. 44:4920-4933(2016).
RN [6]
RP FUNCTION, AND INTERACTION WITH MOE.
RX PubMed=28554770; DOI=10.1016/j.bbamcr.2017.05.020;
RA Kristo I., Bajusz C., Borsos B.N., Pankotai T., Dopie J., Jankovics F.,
RA Vartiainen M.K., Erdelyi M., Vilmos P.;
RT "The actin binding cytoskeletal protein Moesin is involved in nuclear mRNA
RT export.";
RL Biochim. Biophys. Acta 1864:1589-1604(2017).
RN [7]
RP FUNCTION, INTERACTION WITH NUDC, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=33602059; DOI=10.1080/15476286.2021.1885198;
RA Glukhova A.A., Kurshakova M.M., Nabirochkina E.N., Georgieva S.G.,
RA Kopytova D.V.;
RT "PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is
RT essential for both mRNA nuclear export and its subsequent cytoplasmic
RT trafficking.";
RL RNA Biol. 18:1969-1980(2021).
CC -!- FUNCTION: Required for the export of nuclear mRNAs and involved in mRNA
CC trafficking in the cytoplasm (PubMed:27016737, PubMed:28554770,
CC PubMed:33602059). Component of the nuclear pore complex (NPC)-
CC associated TREX-2/AMEX complex (anchoring and mRNA export complex)
CC which functions in docking export-competent ribonucleoprotein particles
CC (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear
CC basket), thereby enabling the export of mRNAs to the cytoplasm through
CC the nuclear pores (PubMed:27016737, PubMed:28554770, PubMed:33602059).
CC Within the complex, specifically promotes the association of factors
CC involved in regulating nuclear mRNA export, such as Moe, sbr/NXF1 and
CC the ORC complex, to the mRNPs particles (PubMed:27016737,
CC PubMed:28554770, PubMed:33602059). In the cytoplasm, functions
CC independently of its role in the TREX-2/AMEX complex, to promote
CC cytoplasmic mRNA trafficking together with nudC (PubMed:33602059).
CC Associates with translationally active polysomes (PubMed:18086857).
CC {ECO:0000269|PubMed:18086857, ECO:0000269|PubMed:27016737,
CC ECO:0000269|PubMed:28554770, ECO:0000269|PubMed:33602059}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-
CC 2/AMEX complex (anchoring and mRNA export complex), composed of e(y)2,
CC xmas and PCID2 (PubMed:27016737). Interaction between the TREX-2/AMEX
CC complex and the ORC complex is required for ORC localization to mRNPs,
CC and consequently mRNA export (PubMed:27016737). Within the TREX-2/AMEX-
CC ORC complex, interacts with Orc3 and Orc4 (PubMed:27016737). Interacts
CC with sbr/NXF1 (PubMed:18086857). Interacts with Moe (PubMed:28554770).
CC Interacts with nudC; required to maintain stability in the cytoplasm
CC (PubMed:33602059). {ECO:0000269|PubMed:18086857,
CC ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:28554770,
CC ECO:0000269|PubMed:33602059}.
CC -!- INTERACTION:
CC Q9VTL1; Q9VM46: Sem1; NbExp=3; IntAct=EBI-123918, EBI-101834;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18086857,
CC ECO:0000269|PubMed:27016737}. Cytoplasm {ECO:0000269|PubMed:18086857,
CC ECO:0000269|PubMed:33602059}. Nucleus membrane
CC {ECO:0000269|PubMed:33602059}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:33602059}. Note=Shuttles in and out of the nucleus
CC by a emb/Crm1-dependent mechanism (PubMed:18086857). The ubiquitinated
CC forms are localized to the cytoplasm, the nonubiquitinated forms are
CC localized to the nucleus, and both forms are associated with the
CC nuclear membrane (PubMed:33602059). Associated with cytoplasmic
CC microtubules (PubMed:33602059). Associates with mRNA in the nucleus and
CC cytoplasm (PubMed:33602059). {ECO:0000269|PubMed:18086857,
CC ECO:0000269|PubMed:33602059}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:27016737}.
CC -!- DOMAIN: PCI domain is required for interaction with polysomes but not
CC the interaction with sbr. {ECO:0000269|PubMed:18086857}.
CC -!- PTM: Mono- and poly-ubiquitinated. {ECO:0000269|PubMed:33602059}.
CC -!- SIMILARITY: Belongs to the CSN12 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF50037.2; -; Genomic_DNA.
DR EMBL; AY058688; AAL13917.1; -; mRNA.
DR RefSeq; NP_648486.1; NM_140229.3.
DR AlphaFoldDB; Q9VTL1; -.
DR SMR; Q9VTL1; -.
DR BioGRID; 64668; 13.
DR IntAct; Q9VTL1; 2.
DR STRING; 7227.FBpp0075833; -.
DR PaxDb; Q9VTL1; -.
DR PRIDE; Q9VTL1; -.
DR DNASU; 39306; -.
DR EnsemblMetazoa; FBtr0076102; FBpp0075833; FBgn0036184.
DR GeneID; 39306; -.
DR KEGG; dme:Dmel_CG7351; -.
DR UCSC; CG7351-RA; d. melanogaster.
DR CTD; 55795; -.
DR FlyBase; FBgn0036184; PCID2.
DR VEuPathDB; VectorBase:FBgn0036184; -.
DR eggNOG; KOG2688; Eukaryota.
DR GeneTree; ENSGT00390000001101; -.
DR HOGENOM; CLU_031567_2_0_1; -.
DR InParanoid; Q9VTL1; -.
DR OMA; TYLIPCH; -.
DR OrthoDB; 706700at2759; -.
DR PhylomeDB; Q9VTL1; -.
DR BioGRID-ORCS; 39306; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 39306; -.
DR PRO; PR:Q9VTL1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036184; Expressed in eye disc (Drosophila) and 20 other tissues.
DR Genevisible; Q9VTL1; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:0070390; C:transcription export complex 2; IDA:FlyBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045114; Csn12-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12732; PTHR12732; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Membrane; mRNA transport; Nucleus;
KW Protein transport; Reference proteome; Translation regulation; Transport;
KW Ubl conjugation.
FT CHAIN 1..395
FT /note="PCI domain-containing protein 2 homolog"
FT /id="PRO_0000121035"
FT DOMAIN 208..389
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 395 AA; 45180 MW; F7B95BA88C8034EB CRC64;
MFGTVNNYLS GVLHAAQDLD GESLATYLSL RDVHVQNHNL YIAQPEKLVD RFLKPPLDEV
VSAHLKVLYH LAQEPPGYME AYTQQSAACG AVVRLLQQLK DENWCLPLMY RVCLDLRYLA
QACEKHCQGF TPGHVLEKAA DCIMACFRVC AADGRASEED TKRLGMMNLV NQLFKIYFRI
NKLHLCKPLI RAIDNCIFKD SFPLPEQITY KYFVGRRAMF DSNYQAAVQY LSYAFSNCPD
RFASNKRLIL IYLVPVKMLL GYLPSKSLLQ RYDLLLFLDL AMAMKAGNVN RFDEIVRDQE
LVLIRSGIYL LVEKLKFLVY RNLFKKVFVI RKSHQLDMGD FLSALHFVGL TDVSLDETHC
IVANLIYDGK IKGYISHAHN KLVVSKQNPF PSVSL
