ID   SNRPA_BOVIN             Reviewed;         282 AA.
AC   Q2KIR1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=U1 small nuclear ribonucleoprotein A;
DE            Short=U1 snRNP A;
DE            Short=U1-A;
DE            Short=U1A;
GN   Name=SNRPA;
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=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-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}.
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DR   EMBL; BC112544; AAI12545.1; -; mRNA.
DR   RefSeq; NP_001039504.1; NM_001046039.2.
DR   AlphaFoldDB; Q2KIR1; -.
DR   SMR; Q2KIR1; -.
DR   STRING; 9913.ENSBTAP00000011963; -.
DR   PaxDb; Q2KIR1; -.
DR   PeptideAtlas; Q2KIR1; -.
DR   PRIDE; Q2KIR1; -.
DR   Ensembl; ENSBTAT00000011963; ENSBTAP00000011963; ENSBTAG00000009077.
DR   GeneID; 509802; -.
DR   KEGG; bta:509802; -.
DR   CTD; 6626; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009077; -.
DR   VGNC; VGNC:35074; SNRPA.
DR   eggNOG; KOG4206; Eukaryota.
DR   GeneTree; ENSGT00390000007046; -.
DR   HOGENOM; CLU_041869_1_3_1; -.
DR   InParanoid; Q2KIR1; -.
DR   OMA; NQTIYVN; -.
DR   OrthoDB; 1608132at2759; -.
DR   TreeFam; TF313834; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000009077; Expressed in retropharyngeal lymph node and 107 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; 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_0000273977"
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          101..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..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"
SQ   SEQUENCE   282 AA;  31264 MW;  18B94F970C4BBEC5 CRC64;
     MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK MRGQAFVIFK
     EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT FVERDRKREK RKPKSQETPA
     AKKAVQGGAA APVVGTVQGP VPGMPPMTQA PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQL
     PPGAMPPQQL MPGQMPPAQP LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV
     PGRHDIAFVE FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK