CCNL1_DANRE
ID CCNL1_DANRE Reviewed; 498 AA.
AC Q7ZVX0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cyclin-L1;
GN Name=ccnl1; ORFNames=zgc:55544;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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}.
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DR EMBL; BC045378; AAH45378.1; -; mRNA.
DR RefSeq; NP_956034.1; NM_199740.1.
DR AlphaFoldDB; Q7ZVX0; -.
DR SMR; Q7ZVX0; -.
DR STRING; 7955.ENSDARP00000021380; -.
DR iPTMnet; Q7ZVX0; -.
DR PaxDb; Q7ZVX0; -.
DR PRIDE; Q7ZVX0; -.
DR GeneID; 326088; -.
DR KEGG; dre:326088; -.
DR CTD; 326088; -.
DR ZFIN; ZDB-GENE-030131-4813; ccnl1b.
DR eggNOG; KOG0835; Eukaryota.
DR InParanoid; Q7ZVX0; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q7ZVX0; -.
DR PRO; PR:Q7ZVX0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
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; IBA:GO_Central.
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; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Cyclin; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..498
FT /note="Cyclin-L1"
FT /id="PRO_0000080485"
FT REGION 68..169
FT /note="Cyclin-like 1"
FT REGION 182..266
FT /note="Cyclin-like 2"
FT REGION 294..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..396
FT /note="RS"
FT COMPBIAS 302..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..498
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 498 AA; 57405 MW; D529EAE038599BA4 CRC64;
MSLGMLSPHL NTPPPNNQGI LIGDKVYSEV FLAIDNSIIP EDRLSTTPSM LDGLDHETET
DLRILGCERI QSAGILLRLP QVAMATGQVI FQRFFFSKSF VKHNFEIVAM ACVNLASKIE
ESPRRVRDVI NVFHHLKQGK GKKSTPLILD QNYINTKNQV IKAERRILKE LGFCVHVKHP
HKIIVMYLQV LECEKNQMLV QTAWNYMNDA LRTSAFVRFE PETIACACIY LAARVLQIPL
PSKPHWFLLF GATKEDIKEI CINTMKLYSR EKPHSEQLER QVEKRKIFLE EARLKARGQN
PNGTPALASI NGFSPASKPS SPRDVKMDDK SPNSKLKEPE NRQLFAKSPL NGSIKKEDGK
VFQNGKNHSR SRSRSTSRSP HRHRRSHSGT YSSHSSHSPS PRQKARRPSP ISQLRTDRDR
PSETSRHSNK RRRSRSRSRS NSRERVRDRD HIKHKQERSG SGHHWDHRDR ERDRSRDHGR
NKRQSRSHSG HSHSRHRR
