RU1C_VITVI
ID RU1C_VITVI Reviewed; 213 AA.
AC F6HQ26;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=U1 small nuclear ribonucleoprotein C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1 snRNP C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1-C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1C {ECO:0000255|HAMAP-Rule:MF_03153};
GN OrderedLocusNames=VIT_07s0104g01170;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN596005; CCB56782.1; -; Genomic_DNA.
DR EMBL; FN597025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002270246.1; XM_002270210.3.
DR AlphaFoldDB; F6HQ26; -.
DR SMR; F6HQ26; -.
DR STRING; 29760.VIT_07s0104g01170.t01; -.
DR PRIDE; F6HQ26; -.
DR EnsemblPlants; Vitvi07g00234_t001; Vitvi07g00234_P001; Vitvi07g00234.
DR GeneID; 100263028; -.
DR Gramene; Vitvi07g00234_t001; Vitvi07g00234_P001; Vitvi07g00234.
DR KEGG; vvi:100263028; -.
DR eggNOG; KOG3454; Eukaryota.
DR HOGENOM; CLU_079697_1_0_1; -.
DR InParanoid; F6HQ26; -.
DR OrthoDB; 1594407at2759; -.
DR Proteomes; UP000009183; Chromosome 7.
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..213
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000414272"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 143..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 22779 MW; 48B94936F3AA0B91 CRC64;
MPRYYCDYCD TYLTHDSPSV RKQHNAGYKH KANVRSYYQQ FEEQQTQSLI DQRIKEHLGQ
TAAFQQVGAA YNQHLVSFPG NPPRPRLPVL PTPGMPVAGS APLPMNSPLV PGMRPPVLPR
PVPGAPGYMP APGMPSMMAP PGAPSMPMPP LNSLPRPPTM NVPPAVPGST STPTSGGAPS
MMTQPMYQAN PAGPTSGGFD SFNINAQGPE ANH
