SNRPA_PIG
ID SNRPA_PIG Reviewed; 282 AA.
AC Q06AA4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=U1 small nuclear ribonucleoprotein A;
DE Short=U1 snRNP A;
DE Short=U1-A;
DE Short=U1A;
GN Name=SNRPA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the spliceosomal U1 snRNP, which is essential
CC for recognition of the pre-mRNA 5' splice-site and the subsequent
CC assembly of the spliceosome. U1 snRNP is the first snRNP to interact
CC with pre-mRNA. This interaction is required for the subsequent binding
CC of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1
CC snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA
CC splicing and polyadenylation process. May bind preferentially to the
CC 5'-UGCAC-3' motif on RNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1,
CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric
CC protein ring on the Sm site of the small nuclear RNA to form the core
CC snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K,
CC SNRPA/U1-A and SNRPC/U1-C. Interacts with SFPQ; component of a snRNP-
CC free complex with SFPQ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM U1 A/B'' 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; DQ972960; ABI96196.1; -; mRNA.
DR RefSeq; NP_001070690.1; NM_001077222.1.
DR RefSeq; XP_005655899.1; XM_005655842.2.
DR RefSeq; XP_005655900.1; XM_005655843.2.
DR RefSeq; XP_005655901.1; XM_005655844.2.
DR PDB; 4PKD; X-ray; 2.50 A; B=2-111.
DR PDBsum; 4PKD; -.
DR AlphaFoldDB; Q06AA4; -.
DR SMR; Q06AA4; -.
DR STRING; 9823.ENSSSCP00000003248; -.
DR PaxDb; Q06AA4; -.
DR PeptideAtlas; Q06AA4; -.
DR PRIDE; Q06AA4; -.
DR Ensembl; ENSSSCT00005074361; ENSSSCP00005046696; ENSSSCG00005045937.
DR Ensembl; ENSSSCT00015105994; ENSSSCP00015044483; ENSSSCG00015078150.
DR Ensembl; ENSSSCT00025062644; ENSSSCP00025026632; ENSSSCG00025046097.
DR Ensembl; ENSSSCT00030101951; ENSSSCP00030047036; ENSSSCG00030072757.
DR Ensembl; ENSSSCT00035001235; ENSSSCP00035000361; ENSSSCG00035001021.
DR Ensembl; ENSSSCT00040037684; ENSSSCP00040015700; ENSSSCG00040028027.
DR Ensembl; ENSSSCT00045041183; ENSSSCP00045028585; ENSSSCG00045024127.
DR Ensembl; ENSSSCT00050012236; ENSSSCP00050005125; ENSSSCG00050009001.
DR Ensembl; ENSSSCT00055023836; ENSSSCP00055018857; ENSSSCG00055012095.
DR Ensembl; ENSSSCT00060009582; ENSSSCP00060003496; ENSSSCG00060007518.
DR Ensembl; ENSSSCT00065092986; ENSSSCP00065040686; ENSSSCG00065067725.
DR Ensembl; ENSSSCT00070004974; ENSSSCP00070004044; ENSSSCG00070002681.
DR Ensembl; ENSSSCT00070004987; ENSSSCP00070004053; ENSSSCG00070002681.
DR GeneID; 768109; -.
DR KEGG; ssc:768109; -.
DR CTD; 6626; -.
DR eggNOG; KOG4206; Eukaryota.
DR HOGENOM; CLU_041869_1_3_1; -.
DR InParanoid; Q06AA4; -.
DR OrthoDB; 1608132at2759; -.
DR TreeFam; TF313834; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
DR Genevisible; Q06AA4; SS.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12477; RRM1_U1A; 1.
DR CDD; cd12480; RRM2_U1A; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034407; U1A_RRM1.
DR InterPro; IPR034409; U1A_RRM2.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09012"
FT CHAIN 2..282
FT /note="U1 small nuclear ribonucleoprotein A"
FT /id="PRO_0000273978"
FT DOMAIN 10..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 208..282
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 100..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P09012"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09012"
FT MOD_RES 152
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P09012"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4PKD"
FT TURN 49..53
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:4PKD"
SQ SEQUENCE 282 AA; 31280 MW; CF296FDF03E475AC CRC64;
MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK MRGQAFVIFK
EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT FVERDRKREK RKPKSQETPA
SKKAVQGGAA APVVGAVQGP VPGMPPMTQT PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI
PPGAMPPQQL MPGQMPPAQP LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV
PGRHDIAFVE FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK
