CCNL2_XENTR
ID CCNL2_XENTR Reviewed; 497 AA.
AC Q5BKF8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cyclin-L2;
GN Name=ccnl2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in pre-mRNA splicing.
CC {ECO:0000250|UniProtKB:Q96S94}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96S94}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96S94}.
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; BC091090; AAH91090.1; -; mRNA.
DR RefSeq; NP_001025623.1; NM_001030452.1.
DR AlphaFoldDB; Q5BKF8; -.
DR SMR; Q5BKF8; -.
DR STRING; 8364.ENSXETP00000024290; -.
DR PaxDb; Q5BKF8; -.
DR PRIDE; Q5BKF8; -.
DR GeneID; 595011; -.
DR KEGG; xtr:595011; -.
DR CTD; 81669; -.
DR Xenbase; XB-GENE-956522; ccnl2.
DR eggNOG; KOG0835; Eukaryota.
DR InParanoid; Q5BKF8; -.
DR OrthoDB; 1519153at2759; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; 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..497
FT /note="Cyclin-L2"
FT /id="PRO_0000080490"
FT REGION 61..163
FT /note="Cyclin-like 1"
FT REGION 176..260
FT /note="Cyclin-like 2"
FT REGION 293..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..404
FT /note="RS"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 56848 MW; FA6177D97C867AD1 CRC64;
MAANSSAVSS DGILIGDKLY SGVMISLENC LMAEERCALT PSVVDGIDVN TEIDLRCVGC
ELVQAAGILL RLPQVAMATG QVLFQRFFYT KSFVKHSMEH VAMACVHLAS KIEEAPRRIR
DVINVFHRLR QLREKQKSTP LILDQEYVNL KNQIIKAERR VLKELGFCVH VKHPHKIIVM
YLQVLECERN KHLVQTSWNY MNDSLRTDVF VRFNPETIAC ACIFLAARTL EIPLPNRPHW
FYLFGASEED IKEICLQILR LYTRKKADVA LLENKVEKRK LFIEEAKAKA KGLLPDGTPR
LENAPEFSPS LKNDSPKELK ANKPSPLAVH ALKNCKRKVD GTKRPTSSSP VNGRVSKGRD
SRSGSRSRDQ SYSRSQSRSQ SPKRRKSQSY SPSSDSKSRS PSRSRSDSPP HKPNHGSYKS
TKGHVYGNNS DYKYQGHKRR SRSRSSSPSH SRSRESSDSG KYKKKDHYYR RERSRSYDRV
SHRGYDREYH GHSHHRR