位置:首页 > 蛋白库 > RU1C_FUSV7
RU1C_FUSV7
ID   RU1C_FUSV7              Reviewed;         204 AA.
AC   C7YRT4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
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   ORFNames=NECHADRAFT_80502;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
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}.
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; GG698899; EEU45129.1; -; Genomic_DNA.
DR   RefSeq; XP_003050842.1; XM_003050796.1.
DR   AlphaFoldDB; C7YRT4; -.
DR   SMR; C7YRT4; -.
DR   STRING; 140110.NechaP80502; -.
DR   EnsemblFungi; NechaT80502; NechaP80502; NechaG80502.
DR   GeneID; 9668001; -.
DR   KEGG; nhe:NECHADRAFT_80502; -.
DR   eggNOG; KOG3454; Eukaryota.
DR   HOGENOM; CLU_079697_2_0_1; -.
DR   InParanoid; C7YRT4; -.
DR   OMA; FLTHDST; -.
DR   OrthoDB; 1594407at2759; -.
DR   Proteomes; UP000005206; Unassembled WGS sequence.
DR   GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005685; C:U1 snRNP; IEA:UniProtKB-UniRule.
DR   GO; GO:0071004; C:U2-type prespliceosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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..204
FT                   /note="U1 small nuclear ribonucleoprotein C"
FT                   /id="PRO_0000414289"
FT   ZN_FING         4..36
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT   REGION          65..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..195
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  20666 MW;  304E264C3FA807A7 CRC64;
     MPKFFCDYCD VYLTHDSMSV RKAHNSGRNH LRNVVDYYQQ IGHEKAQSVI DSITSSYAAE
     GQAHANPMLP QNQPGQGFPP PPFGFPGGIP PPFPGMPGAP PGQFPQGMPP PPGGGRGMPP
     MPPFPPGPNG MPVPPNGLPF PPPGGFPFPP PGAPGAPGAP GASGGAPPPF PGLPGMPPPG
     QGFPPGGPPG FAPPGAGAPG HEKR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024