GEMI2_DICDI
ID GEMI2_DICDI Reviewed; 331 AA.
AC Q54KN2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Gem-associated protein 2;
DE Short=Gemin-2;
DE AltName: Full=Component of gems protein 2;
GN Name=gemin2; ORFNames=DDB_G0287253;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 (By similarity). Most spliceosomal snRNPs contain a common set of
CC Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP (Sm core) (By similarity). In the
CC cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm)
CC are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A
CC that controls the assembly of the core snRNP (By similarity). To
CC assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins
CC from CLNS1A (By similarity). Binding of snRNA inside 5Sm ultimately
CC triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP (By
CC similarity). Within the SMN complex, GEMIN2 constrains the conformation
CC of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP
CC code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing
CC progression of assembly until a cognate substrate is bound (By
CC similarity). {ECO:0000250|UniProtKB:O14893}.
CC -!- FUNCTION: May play an essential role in spliceosomal snRNP assembly in
CC the cytoplasm and may be required for pre-mRNA splicing in the nucleus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000305}. Cytoplasm
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the gemin-2 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; AAFI02000099; EAL63828.1; -; Genomic_DNA.
DR RefSeq; XP_637325.1; XM_632233.1.
DR AlphaFoldDB; Q54KN2; -.
DR SMR; Q54KN2; -.
DR STRING; 44689.DDB0302536; -.
DR PaxDb; Q54KN2; -.
DR EnsemblProtists; EAL63828; EAL63828; DDB_G0287253.
DR GeneID; 8626022; -.
DR KEGG; ddi:DDB_G0287253; -.
DR dictyBase; DDB_G0287253; gemin2.
DR eggNOG; ENOG502R0G7; Eukaryota.
DR HOGENOM; CLU_053222_0_0_1; -.
DR InParanoid; Q54KN2; -.
DR OMA; PHINDKR; -.
DR PhylomeDB; Q54KN2; -.
DR PRO; PR:Q54KN2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR InterPro; IPR035426; Gemin2/Brr1.
DR Pfam; PF04938; SIP1; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..331
FT /note="Gem-associated protein 2"
FT /id="PRO_0000371341"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..224
FT /evidence="ECO:0000255"
FT COMPBIAS 166..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 39320 MW; A6F24739490C3F56 CRC64;
MDEFQSKAFE VGEEIEPDDN EPLTGEEYLQ RVKWHSNRCP SVVVADIDYS KIKVTIPSNS
YFTLPPSITK CKKELLPTPT WEKEFLNDFS EFRQKLQYIK SNRPSNNNNN NNNNNNNNNN
NNNNNNLIPQ LPHINDKRYW YIFCFGSNGN NNNNNNDIKM KDFNDNQEDD DDDENNEDYE
YNENKEEEEE EEEEEEEEEE VEEEEEEEEE EEEVVDYSTK KPTLGNKPTM DILCRLDHVL
TVALVNYHIE WLEKREFTQE RSYWLYMLLS LLEKPIDPDT CSNLRSCIRR LSVFRSKITN
LNDPNLPSIN ILFTIIAKYF DQLEPSDILY L
