RU1C2_PUCGT
ID RU1C2_PUCGT Reviewed; 188 AA.
AC E3KIY6;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=U1 small nuclear ribonucleoprotein C-2 {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1 snRNP C-2 {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1-C-2 {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1C-2 {ECO:0000255|HAMAP-Rule:MF_03153};
GN ORFNames=PGTG_10639;
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL;
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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-C is directly involved in initial 5'
CC splice-site recognition for both constitutive and regulated alternative
CC splicing. The interaction with the 5' splice-site seems to precede
CC base-pairing between the pre-mRNA and the U1 snRNA. Stimulates
CC commitment or early (E) complex formation by stabilizing the base
CC pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins B/B', D1, D2,
CC D3, E, F and G that assemble in a heptameric protein ring on the Sm
CC site of the small nuclear RNA to form the core snRNP, and at least 3 U1
CC snRNP-specific proteins U1-70K, U1-A and U1-C. U1-C interacts with U1
CC snRNA and the 5' splice-site region of the pre-mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; DS178289; EFP84261.1; -; Genomic_DNA.
DR RefSeq; XP_003328680.1; XM_003328632.2.
DR AlphaFoldDB; E3KIY6; -.
DR SMR; E3KIY6; -.
DR STRING; 418459.E3KIY6; -.
DR EnsemblFungi; EFP84261; EFP84261; PGTG_10639.
DR GeneID; 10545523; -.
DR KEGG; pgr:PGTG_10639; -.
DR VEuPathDB; FungiDB:PGTG_10639; -.
DR HOGENOM; CLU_079697_1_0_1; -.
DR InParanoid; E3KIY6; -.
DR OrthoDB; 1594407at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030627; F:pre-mRNA 5'-splice site binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03153; U1_C; 1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR InterPro; IPR017340; U1_snRNP-C.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR31148; PTHR31148; 1.
DR Pfam; PF06220; zf-U1; 1.
DR PIRSF; PIRSF037969; U1_snRNP-C; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..188
FT /note="U1 small nuclear ribonucleoprotein C-2"
FT /id="PRO_0000414293"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 57..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 19652 MW; 29206FFF3396824E CRC64;
MGKYYCDYCD VFLVSESPSV RKAHNSGRNH LTNVRDYYSS LGHDKAQSYI DEITRMFETG
GGNSTSNRGP GGNPPGSQPG PPNAGMSGPM RPPFSNSTAG PNMPPLPPAM LALMNGQNGM
SSPGSGPPPM RFAGPPIPNN MPPGMMQPPH VNGYSSGPLP PQPQPASGGQ GAPPLTARMN
PDRARQLG
