ID   GEMI2_XENLA             Reviewed;         259 AA.
AC   O42260;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, 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 2;
DE   AltName: Full=Survival of motor neuron protein-interacting protein 1;
DE            Short=SMN-interacting protein 1;
GN   Name=gemin2; Synonyms=sip1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9323129; DOI=10.1016/s0092-8674(00)80367-0;
RA   Liu Q., Fischer U., Wang F., Dreyfuss G.;
RT   "The spinal muscular atrophy disease gene product, SMN, and its associated
RT   protein SIP1 are in a complex with spliceosomal snRNP proteins.";
RL   Cell 90:1013-1021(1997).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Ovary;
RX   PubMed=9323130; DOI=10.1016/s0092-8674(00)80368-2;
RA   Fischer U., Liu Q., Dreyfuss G.;
RT   "The SMN-SIP1 complex has an essential role in spliceosomal snRNP
RT   biogenesis.";
RL   Cell 90:1023-1029(1997).
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:9323130). Most spliceosomal snRNPs contain a common set
CC       of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG
CC       that 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       ECO:0000269|PubMed:9323130}.
CC   -!- SUBUNIT: Forms a stable heteromeric complex with survival of motor
CC       neuron protein (SMN), GEMIN3 and GEMIN4. The SMN complex is associated
CC       with the spliceosomal snRNAs U1 and U5 in the cytoplasm of oocytes.
CC   -!- SUBCELLULAR LOCATION: Nucleus, gem. Cytoplasm. Note=Localized in
CC       subnuclear structures next to coiled bodies, called gems, which are
CC       highly enriched in spliceosomal snRNPs. Also found in the cytoplasm.
CC   -!- SIMILARITY: Belongs to the gemin-2 family. {ECO:0000305}.
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DR   EMBL; AF027151; AAB82298.1; -; mRNA.
DR   AlphaFoldDB; O42260; -.
DR   SMR; O42260; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR   GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR   GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR   InterPro; IPR017364; GEMIN2.
DR   InterPro; IPR035426; Gemin2/Brr1.
DR   Pfam; PF04938; SIP1; 1.
DR   PIRSF; PIRSF038038; SMN_Gemin2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT   CHAIN           1..259
FT                   /note="Gem-associated protein 2"
FT                   /id="PRO_0000087458"
SQ   SEQUENCE   259 AA;  29525 MW;  D13F08733DAF4AB0 CRC64;
     MPRLLPVEAC DLPEDYDPSV PPRTPQEYLR RVQIEAARCP DVVIAQIDPK KLRKKQTVSI
     SLSGCQPAPD GYSPSLRWQQ QQVAQFSAVR QSLHKHRGHW RSQPLDSNVT MPSTEDEESW
     KKFCLGERLY SDLAAALNSE SQHPGIDYIK VGFPPLLSIV SRMSQATVTS VLEYLVNWFE
     ERNFTPELGR WLYALLACLE KPLLPEAHSL IRQLARRCSQ IRAGVEHKED DRVSPLNLFI
     CLVGRYFEQR DLADCGDPS