GEMI7_BOVIN
ID GEMI7_BOVIN Reviewed; 125 AA.
AC Q17QA0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Gem-associated protein 7;
DE Short=Gemin-7;
GN Name=GEMIN7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC118472; AAI18473.1; -; mRNA.
DR RefSeq; NP_001069957.1; NM_001076489.1.
DR AlphaFoldDB; Q17QA0; -.
DR SMR; Q17QA0; -.
DR STRING; 9913.ENSBTAP00000014112; -.
DR PaxDb; Q17QA0; -.
DR Ensembl; ENSBTAT00000014112; ENSBTAP00000014112; ENSBTAG00000010668.
DR GeneID; 618024; -.
DR KEGG; bta:618024; -.
DR CTD; 79760; -.
DR VEuPathDB; HostDB:ENSBTAG00000010668; -.
DR VGNC; VGNC:29320; GEMIN7.
DR eggNOG; ENOG502S59N; Eukaryota.
DR GeneTree; ENSGT00390000018039; -.
DR HOGENOM; CLU_2031900_0_0_1; -.
DR InParanoid; Q17QA0; -.
DR OMA; FQMYENV; -.
DR OrthoDB; 1517114at2759; -.
DR TreeFam; TF328578; -.
DR Reactome; R-BTA-191859; snRNP Assembly.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000010668; Expressed in blood and 108 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; 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 Phosphoprotein; Reference proteome.
FT CHAIN 1..125
FT /note="Gem-associated protein 7"
FT /id="PRO_0000271401"
FT DOMAIN 1..29
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H840"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H840"
SQ SEQUENCE 125 AA; 13851 MW; 091367563B26A9FB CRC64;
MQTPLATPVP VLRLPRGPDG SNRGFAPDGR RAPPKPEVPE PPESRESWEQ QARASLRERY
LRSLLAMVGR PVCFTLHEGV QVIAHFGATD LDVANFYVSQ LQTPIGIQAE ALLRCSDIIS
YTFKP