ID   CCNL1_XENLA             Reviewed;         496 AA.
AC   Q6GN15; Q52L35;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Cyclin-L1;
GN   Name=ccnl1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing.
CC       {ECO:0000250|UniProtKB:Q9UK58}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9UK58}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in
CC       nuclear intrachromatin granules clusters (IGC), also called nuclear
CC       speckles, which are storage compartments for nuclear proteins involved
CC       in mRNA processing. {ECO:0000250|UniProtKB:Q9UK58}.
CC   -!- DOMAIN: Contains a RS region (arginine-serine dipeptide repeat) within
CC       the C-terminal domain which is the hallmark of the SR family of
CC       splicing factors. This region probably plays a role in protein-protein
CC       interactions (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH73707.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH94084.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC073707; AAH73707.1; ALT_INIT; mRNA.
DR   EMBL; BC094084; AAH94084.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6GN15; -.
DR   SMR; Q6GN15; -.
DR   PRIDE; Q6GN15; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR015431; Cyclin_L1.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; PTHR10026; 1.
DR   PANTHER; PTHR10026:SF64; PTHR10026:SF64; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
PE   2: Evidence at transcript level;
KW   Cyclin; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..496
FT                   /note="Cyclin-L1"
FT                   /id="PRO_0000080486"
FT   REGION          68..170
FT                   /note="Cyclin-like 1"
FT   REGION          183..267
FT                   /note="Cyclin-like 2"
FT   REGION          301..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..406
FT                   /note="RS"
FT   COMPBIAS        323..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..396
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..422
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..445
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..496
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  57226 MW;  5CA03BCFBE4DE493 CRC64;
     MAAVPQLSAP SAPARSADGI LIGDRQYSEV YLTIDYSLIP EERLSPTPSM SDGLDLNTET
     DLRILGCELI QSAGILLRLP QVAMATGQVL FHRFFYSKSF VKHSFEIIAM ACINLASKIE
     EAPRRIRDVI NVCHHLRQIR AKRTPSPLIL DQSYINTKNH VIKAERRILK ELGFCVHVKH
     PHKIIVMYLQ VLECERNQTL VQTAWNYMND CLRTNVFVRF DAETIACACI YLAARALQLS
     LPNRPHWFLL FGATEENIQD ICITTLRLYS RIKPNYEFLE KEVDKRKVAL QEAKLKAKGL
     NPDGTPAILS MGGFSPASKP SSPRDVKTEE KSPNFAKVKR EMDDKQSSKS PYNGLRKENK
     RSRSVSRSRS RTKSRSRSHS PRRHYNNRRR SRSGTYSSRS RSRSRSHSES PRRHHNHGSP
     HMKLKHRVED LRGRHAHKRK KSHSPSKSRE PSELAKKHRH EHGHHRERRE RSRSFERSHK
     NKHHGSSHSG HGRHRR