CCNL1_RAT
ID CCNL1_RAT Reviewed; 527 AA.
AC Q9R1Q2; Q5U364;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cyclin-L1;
DE Short=Cyclin-L;
DE AltName: Full=Cyclin Ania-6a;
GN Name=Ccnl1; Synonyms=Ania6a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=9651213; DOI=10.1523/jneurosci.18-14-05301.1998;
RA Berke J.D., Paletzki R.F., Aronson G.J., Hyman S.E., Gerfen C.R.;
RT "A complex program of striatal gene expression induced by dopaminergic
RT stimulation.";
RL J. Neurosci. 18:5301-5310(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INDUCTION, AND INTERACTION WITH POLR2A; CDC2L
RP AND SFRS2.
RX PubMed=11683997; DOI=10.1016/s0896-6273(01)00465-2;
RA Berke J.D., Sgambato V., Zhu P.-P., Lavoie B., Vincent M., Krause M.,
RA Hyman S.E.;
RT "Dopamine and glutamate induce distinct striatal splice forms of Ania-6, an
RT RNA polymerase II-associated cyclin.";
RL Neuron 32:277-287(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INDUCTION.
RX PubMed=12807435; DOI=10.1046/j.1471-4159.2003.01816.x;
RA Sgambato V., Minassian R., Nairn A.C., Hyman S.E.;
RT "Regulation of ania-6 splice variants by distinct signaling pathways in
RT striatal neurons.";
RL J. Neurochem. 86:153-164(2003).
RN [5]
RP INTERACTION WITH CDK12.
RX PubMed=16537916; DOI=10.1128/mcb.26.7.2736-2745.2006;
RA Chen H.-H., Wang Y.-C., Fann M.-J.;
RT "Identification and characterization of the CDK12/cyclin L1 complex
RT involved in alternative splicing regulation.";
RL Mol. Cell. Biol. 26:2736-2745(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-339 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in pre-mRNA splicing (PubMed:11683997). Functions in
CC association with cyclin-dependent kinases (CDKs). May play a role in
CC the regulation of RNA polymerase II (pol II). Inhibited by the CDK-
CC specific inhibitor CDKN1A/p21 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UK58, ECO:0000269|PubMed:11683997}.
CC -!- SUBUNIT: Interacts with POLR2A via its hyperphosphorylated C-terminal
CC domain (CTD). Interacts with CDK11A, CDK11B, CDK12 and CDK13. May form
CC a ternary complex with CDK11B and casein kinase II (CKII). Interacts
CC with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND
CC SRSF7/SLU7. {ECO:0000250|UniProtKB:Q9UK58, ECO:0000269|PubMed:11683997,
CC ECO:0000269|PubMed:16537916}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11683997,
CC ECO:0000269|PubMed:9651213}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in nuclear intrachromatin
CC granules clusters (IGC), also called nuclear speckles, which are
CC storage compartments for nuclear proteins involved in mRNA processing.
CC {ECO:0000269|PubMed:11683997, ECO:0000269|PubMed:9651213}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Ccnl1 is an immediate-early gene with independently regulated
CC isoforms.;
CC Name=1;
CC IsoId=Q9R1Q2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R1Q2-2; Sequence=VSP_016128, VSP_016129;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher level in liver; expressed in
CC striatal neurons. {ECO:0000269|PubMed:11683997}.
CC -!- INDUCTION: By anisomycin (activator of MAP kinase pathway) and by
CC dopamine and cocaine in dopamine D1 receptor-expressing striatal
CC neurons and by EGF/epidermal growth factor or NGF/nerve growth factor
CC in PC12 pheochromocytoma cells. Isoform 1 also is specifically induced
CC by cycloheximide, potassium chloride (KCl) and forskolin or brain
CC neurotrophic factor (BDNF). Isoform 2 is induced by glutamate.
CC {ECO:0000269|PubMed:11683997, ECO:0000269|PubMed:12807435,
CC ECO:0000269|PubMed:9651213}.
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; AF030091; AAD45558.1; -; mRNA.
DR EMBL; BC085686; AAH85686.1; -; mRNA.
DR RefSeq; NP_446114.1; NM_053662.3. [Q9R1Q2-1]
DR RefSeq; XP_003749343.1; XM_003749295.4. [Q9R1Q2-2]
DR AlphaFoldDB; Q9R1Q2; -.
DR SMR; Q9R1Q2; -.
DR STRING; 10116.ENSRNOP00000016016; -.
DR iPTMnet; Q9R1Q2; -.
DR PhosphoSitePlus; Q9R1Q2; -.
DR jPOST; Q9R1Q2; -.
DR PaxDb; Q9R1Q2; -.
DR PRIDE; Q9R1Q2; -.
DR Ensembl; ENSRNOT00000016016; ENSRNOP00000016016; ENSRNOG00000011586. [Q9R1Q2-1]
DR GeneID; 114121; -.
DR KEGG; rno:114121; -.
DR UCSC; RGD:620864; rat. [Q9R1Q2-1]
DR CTD; 57018; -.
DR RGD; 620864; Ccnl1.
DR eggNOG; KOG0835; Eukaryota.
DR GeneTree; ENSGT00940000159135; -.
DR HOGENOM; CLU_022000_6_1_1; -.
DR InParanoid; Q9R1Q2; -.
DR OMA; RCHMVQE; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q9R1Q2; -.
DR TreeFam; TF101011; -.
DR PRO; PR:Q9R1Q2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011586; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q9R1Q2; baseline and differential.
DR Genevisible; Q9R1Q2; RN.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:0043484; P:regulation of RNA splicing; ISO:RGD.
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 Alternative splicing; Cyclin; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..527
FT /note="Cyclin-L1"
FT /id="PRO_0000080482"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..191
FT /note="Cyclin-like 1"
FT REGION 204..288
FT /note="Cyclin-like 2"
FT REGION 327..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..433
FT /note="RS"
FT COMPBIAS 344..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..417
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT VAR_SEQ 164..173
FT /note="RTPSPLILDQ -> SDQLHLPKPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11683997,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016128"
FT VAR_SEQ 174..527
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11683997,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016129"
SQ SEQUENCE 527 AA; 59791 MW; 444F5D632B15BC43 CRC64;
MASGPHPTST AAAASASSAA PSAGGSSSGT TTTTTTTTGG ILIGDRLYSE VSLTIDHSVI
PEERLSPTPS MQDGLDLPSE TDLRILGCEL IQAAGILLRL PQVAMATGQV LFHRFFYSKS
FVKHSFEIVA MACINLASKI EEAPRRIRDV INVFHHLRQL RGKRTPSPLI LDQNYINTKN
QVIKAERRVL KELGFCVHVK HPHKIIVMYL QVLECERNQT LVQTAWNYMN DSLRTNVFVR
FQPETIACAC IYLAARALQI PLPTRPHWFL LFGTTEEEIQ EICIETLRLY TRKKPNYELL
EKEVEKRKVA LQEAKLKAKG LNLDGTPALS TLGGFSPASK PSSPREVKAE EKSPVSINVK
TVKKEPEDRQ QASKSPYNGV RKDSKRSRNS RSASRSRSRT RSRSRSHTPR RHYNNRRSRS
GTYSSRSRSR SRSHSESPRR HHNHGSPHLK AKHTREDLKS SNRHGHKRKK SRSRSQSKTR
DHSDVTKKHR HERGHHRDRR ERSRSFERSH KGKHHGGSRS GHGRHRR
