RU1C_SCHPO
ID RU1C_SCHPO Reviewed; 182 AA.
AC Q9P794;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
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 Name=usp103; Synonyms=yhc1; ORFNames=SPBP35G2.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, IDENTIFICATION IN U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17264129; DOI=10.1093/nar/gkl1144;
RA Newo A.N.S., Luetzelberger M., Bottner C.A., Wehland J., Wissing J.,
RA Jaensch L., Kaeufer N.F.;
RT "Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals
RT three essential organism-specific proteins.";
RL Nucleic Acids Res. 35:1391-1401(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. usp103/U1-C is directly involved in
CC initial 5' splice-site recognition for both constitutive and regulated
CC alternative splicing. The interaction with the 5' splice-site seems to
CC precede 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:0000269|PubMed:17264129}.
CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins smb1, smd1,
CC smd2, smd3, sme1, smf1 and smg1 (Sm proteins B, D1, D2, D3, E, F and G,
CC respectively) that assemble in a heptameric protein ring on the Sm site
CC of the small nuclear RNA to form the core snRNP, and at least 9 U1
CC snRNP-specific proteins usp101/U1-70K, usp102/U1-A, usp103/U1-C,
CC usp106/LUC7, usp105/PRP39, usp104/PRP40, usp107/U1-H, usp108/U1-J and
CC usp109/U1-L. usp103/U1-C interacts with U1 snRNA and the 5' splice-site
CC region of the pre-mRNA. {ECO:0000269|PubMed:17264129}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; CU329671; CAB87371.1; -; Genomic_DNA.
DR RefSeq; NP_595384.1; NM_001021291.2.
DR AlphaFoldDB; Q9P794; -.
DR SMR; Q9P794; -.
DR BioGRID; 277802; 13.
DR STRING; 4896.SPBP35G2.09.1; -.
DR MaxQB; Q9P794; -.
DR PaxDb; Q9P794; -.
DR EnsemblFungi; SPBP35G2.09.1; SPBP35G2.09.1:pep; SPBP35G2.09.
DR GeneID; 2541289; -.
DR KEGG; spo:SPBP35G2.09; -.
DR PomBase; SPBP35G2.09; usp103.
DR VEuPathDB; FungiDB:SPBP35G2.09; -.
DR eggNOG; KOG3454; Eukaryota.
DR HOGENOM; CLU_079697_4_0_1; -.
DR InParanoid; Q9P794; -.
DR PRO; PR:Q9P794; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000243; C:commitment complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005685; C:U1 snRNP; IDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR GO; GO:0003729; F:mRNA binding; ISO:PomBase.
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 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..182
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000363373"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 129..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 20479 MW; 029E661EF603EB35 CRC64;
MPRYLCDYCQ VWLTHDSQSV RKAHNAGRAH IQNVQDYYTK VAQEEAQKQL EERASSGFLK
KGNGSLDLPY AYAFPPKYNV FNLGCPPPPY IVSANTYMAP KGMNAMNAAA FVPMMPAVNL
TNQVAFSAPQ TTASSNTQLT QQQQSLPQTN EHQRARTHSN ANNHFTKTHH QGQRSHQRFV
RA
