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RU1C_COPC7
ID   RU1C_COPC7              Reviewed;         209 AA.
AC   A8NYM5;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 56.
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=CC1G_01380;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000005; EAU84384.1; -; Genomic_DNA.
DR   RefSeq; XP_001837468.1; XM_001837416.1.
DR   AlphaFoldDB; A8NYM5; -.
DR   SMR; A8NYM5; -.
DR   STRING; 5346.XP_001837468.1; -.
DR   EnsemblFungi; EAU84384; EAU84384; CC1G_01380.
DR   GeneID; 6014024; -.
DR   KEGG; cci:CC1G_01380; -.
DR   VEuPathDB; FungiDB:CC1G_01380; -.
DR   eggNOG; KOG3454; Eukaryota.
DR   HOGENOM; CLU_079697_1_0_1; -.
DR   InParanoid; A8NYM5; -.
DR   OMA; FLTHDST; -.
DR   OrthoDB; 1594407at2759; -.
DR   Proteomes; UP000001861; 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..209
FT                   /note="U1 small nuclear ribonucleoprotein C"
FT                   /id="PRO_0000414286"
FT   ZN_FING         4..36
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT   REGION          72..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..194
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   209 AA;  21170 MW;  C992D47F23171876 CRC64;
     MPKHYCDYCD VFLTHDSASV RKAHNSGRNH LANVRDYYAS LGHDKAQSII DQITSAFESG
     QGPPPGGFGF GPQHLQAPPQ GGFAPPMGGF PPGGFPPGPR PPFPPGPGFP PMMPPGAPPF
     PPNAMPPPGA FGGPPPFPPN GPPGAPPFPP NASQQGGPPG APSFPPPPGG FNGPPPPSGQ
     NSQGPPPPTN PGPGGMHPDR ARMMGPGGR
 
 
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