CYL1_CAEEL
ID CYL1_CAEEL Reviewed; 480 AA.
AC G5EBX3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cyclin L homolog cyl-1 {ECO:0000305};
GN Name=cyl-1 {ECO:0000312|WormBase:C52E4.6a};
GN ORFNames=C52E4.6 {ECO:0000312|WormBase:C52E4.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAS64750.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LEU-158.
RX PubMed=15611166; DOI=10.1534/genetics.104.028423;
RA Hajdu-Cronin Y.M., Chen W.J., Sternberg P.W.;
RT "The L-type cyclin CYL-1 and the heat-shock-factor HSF-1 are required for
RT heat-shock-induced protein expression in Caenorhabditis elegans.";
RL Genetics 168:1937-1949(2004).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27923661; DOI=10.1016/j.bbrc.2016.12.014;
RA Oh S., Yoon S., Youn E., Kawasaki I., Shim Y.H.;
RT "cdc-25.2, a Caenorhabditis elegans ortholog of cdc25, is required for male
RT tail morphogenesis.";
RL Biochem. Biophys. Res. Commun. 482:1213-1218(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing (By similarity). Functions in
CC association with cyclin-dependent kinases (CDKs) (By similarity).
CC Involved in induction of expression of heat shock protein hsp-16.2 in
CC response to heat shock (PubMed:15611166). Plays a role in male tail
CC development, perhaps acting together with cell cycle regulators cdc-
CC 25.2, cdk-1, cyb-3, and cyd-1 (PubMed:27923661).
CC {ECO:0000250|UniProtKB:Q9UK58, ECO:0000269|PubMed:15611166,
CC ECO:0000269|PubMed:27923661}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes abnormal male tail
CC morphology. {ECO:0000269|PubMed:27923661}.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000255|RuleBase:RU000383}.
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DR EMBL; AY557405; AAS64750.1; -; mRNA.
DR EMBL; BX284605; CAB01416.1; -; Genomic_DNA.
DR PIR; T20154; T20154.
DR PIR; T20155; T20155.
DR RefSeq; NP_506007.1; NM_073606.3.
DR AlphaFoldDB; G5EBX3; -.
DR SMR; G5EBX3; -.
DR IntAct; G5EBX3; 1.
DR STRING; 6239.C52E4.6a.1; -.
DR EPD; G5EBX3; -.
DR PaxDb; G5EBX3; -.
DR PeptideAtlas; G5EBX3; -.
DR EnsemblMetazoa; C52E4.6a.1; C52E4.6a.1; WBGene00000876.
DR GeneID; 179643; -.
DR KEGG; cel:CELE_C52E4.6; -.
DR CTD; 179643; -.
DR WormBase; C52E4.6a; CE17597; WBGene00000876; cyl-1.
DR eggNOG; KOG0835; Eukaryota.
DR GeneTree; ENSGT00940000165223; -.
DR HOGENOM; CLU_022000_6_0_1; -.
DR InParanoid; G5EBX3; -.
DR OMA; RCHMVQE; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; G5EBX3; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000876; Expressed in embryo and 4 other tissues.
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:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
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; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Cyclin; Reference proteome.
FT CHAIN 1..480
FT /note="Cyclin L homolog cyl-1"
FT /id="PRO_0000453733"
FT DOMAIN 91..230
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 158
FT /note="L->F: In sy433; Reduces induction of expression of
FT heat shock protein hsp-16.2 in response to heat-shock."
FT /evidence="ECO:0000269|PubMed:15611166"
SQ SEQUENCE 480 AA; 55993 MW; 190A6FDE9B96C7B4 CRC64;
MASFVEMRKL AEAKVQNMIR TIVKPKEQNG NVEPKKEEDE KFESTYKQNE NTQITPSSFG
KRPLYSKVDI NCDKWLMTLD EESRLKIDNP PSLVDGLSKE TESELRYLGC ELIQQGAILL
KLPQTAAATG QILFQRYYYQ KSFVRYHFEH AVQACLLLAS KIEEEPRRPR EVYNVFHRLE
RLHRLQQSGH DINKETTRGM KPPAVDMNYI NTKQHMINSE RRILATLGFV VHVKHPHRLI
VAYGHTLGIT QSRPDILQRS WNYMNDGLRT DIFMRYKPET IACACIFLAA RTVENPIALP
STPFHWFEAF DTSDRDVEAI ALQLVGLYAR RTFPNWPRIK AELDALRSVK DAEMKAVKAK
EIAENLAKMA PDGEKSTSTV TIGKDSRKVS PDRKNGTKDR GEADRGKKEK DRHRRRSNDR
DGRGDRRDRD KDRGDRRKDE KKDRRKRTRS RSRDRKDKNR NRDVGKRYRK ESSTPPRSRR
