GEMI7_MOUSE
ID GEMI7_MOUSE Reviewed; 129 AA.
AC Q9CWY4;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Gem-associated protein 7;
DE Short=Gemin-7;
GN Name=Gemin7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP (By
CC similarity). {ECO:0000250|UniProtKB:Q9H840}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (By similarity). Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG (By similarity). Interacts with GEMIN6; the interaction
CC is direct (By similarity). Interacts with STRAP/UNRIP; the interaction
CC is direct (By similarity). Interacts with GEMIN8; the interaction is
CC direct (By similarity). Interacts with SNRPB, SNRPD2, SNRPD3 and SNRPE;
CC the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q9H840}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9H840}. Nucleus, gem
CC {ECO:0000250|UniProtKB:Q9H840}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H840}. Note=Found both in the nucleoplasm and
CC in nuclear bodies called gems (Gemini of Cajal bodies) that are often
CC in proximity to Cajal (coiled) bodies. Also found in the cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gemin-7 family. {ECO:0000305}.
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DR EMBL; AK010303; BAB26836.1; -; mRNA.
DR EMBL; BC028527; AAH28527.1; -; mRNA.
DR CCDS; CCDS20907.1; -.
DR RefSeq; NP_081465.1; NM_027189.2.
DR AlphaFoldDB; Q9CWY4; -.
DR SMR; Q9CWY4; -.
DR BioGRID; 213643; 1.
DR IntAct; Q9CWY4; 1.
DR MINT; Q9CWY4; -.
DR STRING; 10090.ENSMUSP00000113266; -.
DR iPTMnet; Q9CWY4; -.
DR PhosphoSitePlus; Q9CWY4; -.
DR EPD; Q9CWY4; -.
DR MaxQB; Q9CWY4; -.
DR PaxDb; Q9CWY4; -.
DR PRIDE; Q9CWY4; -.
DR ProteomicsDB; 272954; -.
DR Antibodypedia; 31264; 159 antibodies from 22 providers.
DR DNASU; 69731; -.
DR Ensembl; ENSMUST00000051364; ENSMUSP00000055844; ENSMUSG00000044709.
DR Ensembl; ENSMUST00000117222; ENSMUSP00000113266; ENSMUSG00000044709.
DR Ensembl; ENSMUST00000119912; ENSMUSP00000112742; ENSMUSG00000044709.
DR Ensembl; ENSMUST00000122055; ENSMUSP00000113583; ENSMUSG00000044709.
DR Ensembl; ENSMUST00000122127; ENSMUSP00000113709; ENSMUSG00000044709.
DR GeneID; 69731; -.
DR KEGG; mmu:69731; -.
DR UCSC; uc009fmi.1; mouse.
DR CTD; 79760; -.
DR MGI; MGI:1916981; Gemin7.
DR VEuPathDB; HostDB:ENSMUSG00000044709; -.
DR eggNOG; ENOG502S59N; Eukaryota.
DR GeneTree; ENSGT00390000018039; -.
DR HOGENOM; CLU_2031900_0_0_1; -.
DR InParanoid; Q9CWY4; -.
DR OMA; FQMYENV; -.
DR OrthoDB; 1517114at2759; -.
DR PhylomeDB; Q9CWY4; -.
DR TreeFam; TF328578; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR BioGRID-ORCS; 69731; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Gemin7; mouse.
DR PRO; PR:Q9CWY4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CWY4; protein.
DR Bgee; ENSMUSG00000044709; Expressed in interventricular septum and 242 other tissues.
DR ExpressionAtlas; Q9CWY4; baseline and differential.
DR Genevisible; Q9CWY4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0120114; C:Sm-like protein family complex; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR CDD; cd11677; Gemin7; 1.
DR InterPro; IPR020338; SMN_gemin7.
DR InterPro; IPR024642; SUZ-C.
DR PANTHER; PTHR14679; PTHR14679; 1.
DR Pfam; PF11095; Gemin7; 1.
DR Pfam; PF12901; SUZ-C; 1.
DR PROSITE; PS51938; SUZ_C; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome.
FT CHAIN 1..129
FT /note="Gem-associated protein 7"
FT /id="PRO_0000087463"
FT DOMAIN 1..31
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H840"
SQ SEQUENCE 129 AA; 14251 MW; 23F108FA3961A8B8 CRC64;
MQSPLTIPVP VPVLRLPRGP DGFSRGFASD GRRTILRPEV GEGHIQDPPE SQEQRARATL
RERYLRSLLA MVGHPVSFTL HEGVHVTAQF GATDLDVANF YVSQLQTPIG VQAEALLRCS
DIISYSFKL