ID   CCNL1_CHICK             Reviewed;         534 AA.
AC   Q5ZJP9;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cyclin-L1;
GN   Name=CCNL1; ORFNames=RCJMB04_16i10;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720385; CAG32044.1; -; mRNA.
DR   RefSeq; NP_989801.2; NM_204470.2.
DR   AlphaFoldDB; Q5ZJP9; -.
DR   SMR; Q5ZJP9; -.
DR   STRING; 9031.ENSGALP00000002355; -.
DR   PaxDb; Q5ZJP9; -.
DR   PRIDE; Q5ZJP9; -.
DR   GeneID; 395124; -.
DR   KEGG; gga:395124; -.
DR   CTD; 81669; -.
DR   VEuPathDB; HostDB:geneid_395124; -.
DR   eggNOG; KOG0835; Eukaryota.
DR   InParanoid; Q5ZJP9; -.
DR   OrthoDB; 1519153at2759; -.
DR   PhylomeDB; Q5ZJP9; -.
DR   PRO; PR:Q5ZJP9; -.
DR   Proteomes; UP000000539; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; PTHR10026; 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   2: Evidence at transcript level;
KW   Cyclin; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..534
FT                   /note="Cyclin-L1"
FT                   /id="PRO_0000080484"
FT   REGION          94..196
FT                   /note="Cyclin-like 1"
FT   REGION          209..293
FT                   /note="Cyclin-like 2"
FT   REGION          327..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..436
FT                   /note="RS"
FT   COMPBIAS        378..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  59830 MW;  284964C4B4143E8E CRC64;
     MAAGSGSAAA VAAVAGGGPA GPHAAGVTAG AVTTGSGAPV PGPGAVLIGD RLYSGVLITL
     ENCLLPEHTL RFTPSMSSGL DPDTETELRV TGCELIQAAG ILLRLPQVAM ATGQVLFQRF
     FYTKSFVKHS MEHVSMACVH LASKIEEAPR RIRDVINVFH RLRHLREKKK PVPLILDQEY
     VNLKNQIIKA ERRVLKELGF CVHVKHPHKI IVMYLQVLEC ERNQHLVQTS WNYMNDSLRT
     DVFVRFQPES IACACIYLAA RTLEIPLPNR PHWFLLFGTT EEEIQEICLK ILQLYTRKKV
     DLSDLESKIE KKKLAIEEAK AQAKGLLPEG APVLDNTSGF SPLPKNESPK EVKGNKPSPL
     PVQAMKNAKR KAEGAKRTGS NSPVNGVQKG RESRSRSGSR DQSYSRSPSR SASPKHRKSE
     SYSTSSGSKS HSRSRSRSGS PPRQFNHSST YKSSKMRSYK KSKDYKYSAH KARKSRSRSS
     SRSRSRSRER SDHSGKYKKK SHYYRNHRHE RSRSYERASH RYDRDHPGHS RHRR