GEMI2_DROME
ID GEMI2_DROME Reviewed; 245 AA.
AC Q9VVX0; Q7K0M0;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein Gemin2 {ECO:0000312|EMBL:AAF49187.1};
GN Name=Gem2 {ECO:0000312|EMBL:AAF49187.1, ECO:0000312|FlyBase:FBgn0036850};
GN ORFNames=CG10419;
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] {ECO:0000312|EMBL:AAF49187.1}
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] {ECO:0000312|EMBL:AAF49187.1}
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] {ECO:0000312|EMBL:AAL39848.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39848.2};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, INTERACTION WITH THE
RP SPLICEOSOME USNRNP PROTEINS SNRNP-U1-70K, U2A, SNF/U1A AND U5-116KD,
RP INTERACTION WITH THE SNRNP SM PROTEINS, AND SUBCELLULAR LOCATION.
RX PubMed=18621711; DOI=10.1073/pnas.0802287105;
RA Kroiss M., Schultz J., Wiesner J., Chari A., Sickmann A., Fischer U.;
RT "Evolution of an RNP assembly system: a minimal SMN complex facilitates
RT formation of UsnRNPs in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10045-10050(2008).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20452345; DOI=10.1016/j.yexcr.2010.05.001;
RA Cauchi R.J., Sanchez-Pulido L., Liu J.L.;
RT "Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are components
RT of U bodies.";
RL Exp. Cell Res. 316:2354-2364(2010).
RN [6] {ECO:0000312|PDB:4V98}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009;
RA Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K.,
RA Stark H., Schindelin H., Fischer U.;
RT "Structural basis of assembly chaperone-mediated snRNP formation.";
RL Mol. Cell 49:692-703(2013).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs (PubMed:18621711, PubMed:23333303). Most spliceosomal snRNPs
CC contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on
CC the Sm site of the small nuclear RNA to form the core snRNP (Sm core)
CC (By similarity). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE,
CC SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by
CC the chaperone CLNS1A that controls the assembly of the core snRNP (By
CC similarity). To assemble core snRNPs, the SMN complex accepts the
CC trapped 5Sm proteins from CLNS1A (By similarity). Binding of snRNA
CC inside 5Sm ultimately triggers eviction of the SMN complex, thereby
CC allowing binding of SNRPD3 and SNRPB to complete assembly of the core
CC snRNP (By similarity). Within the SMN complex, GEMIN2 constrains the
CC conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing
CC the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus
CC preventing progression of assembly until a cognate substrate is bound
CC (By similarity). {ECO:0000250|UniProtKB:O14893,
CC ECO:0000269|PubMed:18621711, ECO:0000269|PubMed:23333303}.
CC -!- SUBUNIT: Part of the core SMN complex, at least composed of Smn and
CC Gem2. The SMN complex associates with the entire set of spliceosomal
CC snRNP Sm proteins, SmB, SmD1, SmD2, SmD3, SmE, SmF and SmG, and with
CC the snRNP-specific proteins snRNP-U1-70K, U2A, snf/U1A and U5-116KD.
CC {ECO:0000269|PubMed:18621711, ECO:0000269|PubMed:23333303}.
CC -!- INTERACTION:
CC Q9VVX0; Q9VV74: Smn; NbExp=5; IntAct=EBI-108834, EBI-185315;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18621711,
CC ECO:0000269|PubMed:20452345}. Note=Component of U bodies.
CC {ECO:0000269|PubMed:18621711, ECO:0000269|PubMed:20452345}.
CC -!- TISSUE SPECIFICITY: Expressed in nurse cells and oocytes.
CC {ECO:0000269|PubMed:20452345}.
CC -!- SIMILARITY: Belongs to the gemin-2 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39848.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF49187.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94727.1; -; Genomic_DNA.
DR EMBL; AY069703; AAL39848.2; ALT_INIT; mRNA.
DR RefSeq; NP_001262034.1; NM_001275105.1.
DR RefSeq; NP_649092.1; NM_140835.4.
DR PDB; 4V98; X-ray; 3.10 A; A2/AF/AN/AV/Ad/Al/At/B2/BF/BN/BV/Bd/Bl/Bt/CF/CN/CV/Cd/Cl/Ct=1-245.
DR PDBsum; 4V98; -.
DR AlphaFoldDB; Q9VVX0; -.
DR SASBDB; Q9VVX0; -.
DR SMR; Q9VVX0; -.
DR BioGRID; 65364; 8.
DR IntAct; Q9VVX0; 10.
DR STRING; 7227.FBpp0303126; -.
DR PaxDb; Q9VVX0; -.
DR DNASU; 40087; -.
DR EnsemblMetazoa; FBtr0075032; FBpp0074799; FBgn0036850.
DR EnsemblMetazoa; FBtr0330093; FBpp0303126; FBgn0036850.
DR GeneID; 40087; -.
DR KEGG; dme:Dmel_CG10419; -.
DR UCSC; CG10419-RA; d. melanogaster.
DR CTD; 40087; -.
DR FlyBase; FBgn0036850; Gem2.
DR VEuPathDB; VectorBase:FBgn0036850; -.
DR eggNOG; ENOG502QPK4; Eukaryota.
DR GeneTree; ENSGT00390000013814; -.
DR HOGENOM; CLU_053222_0_0_1; -.
DR InParanoid; Q9VVX0; -.
DR OMA; PTPEWRD; -.
DR OrthoDB; 1235594at2759; -.
DR PhylomeDB; Q9VVX0; -.
DR BioGRID-ORCS; 40087; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40087; -.
DR PRO; PR:Q9VVX0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036850; Expressed in egg cell and 32 other tissues.
DR Genevisible; Q9VVX0; DM.
DR GO; GO:0071254; C:cytoplasmic U snRNP body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034730; C:SmD-containing SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0032797; C:SMN complex; IDA:FlyBase.
DR GO; GO:0034718; C:SMN-Gemin2 complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IDA:FlyBase.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR InterPro; IPR017364; GEMIN2.
DR InterPro; IPR035426; Gemin2/Brr1.
DR Pfam; PF04938; SIP1; 1.
DR PIRSF; PIRSF038038; SMN_Gemin2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing;
KW Reference proteome; Spliceosome.
FT CHAIN 1..245
FT /note="Protein Gemin2"
FT /id="PRO_0000424375"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:4V98"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 85..111
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:4V98"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 194..212
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:4V98"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4V98"
SQ SEQUENCE 245 AA; 28751 MW; 1E9A700ADD97EDFF CRC64;
MQHEPEDQTF QLQALEICEP DSSFDPQKPP ESGEEYLMHM FYERKRCPAV VTKRSSKIRN
NTGNTTLEML DNPELPPFKC LLPTPEWRDE QVKSFQAARS QVLVLRKELA NNNYDQSGEP
PLTSDQEKWK EFCRNQQPLL STLLHLTQND LELLLEMLSK WLQDPNTTVD LLHDVWLARW
LYATLVCLHL PLEPHVFSTL RYIARTCIHL RNQLKEDEVQ RAAPYNLLLT LTVQVFAQND
FKDYI
