ID A0A2U3XMB0_LEPWE Unreviewed; 523 AA.
AC A0A2U3XMB0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cyclin-L2 isoform X1 {ECO:0000313|RefSeq:XP_006732473.1};
GN Name=CCNL2 {ECO:0000313|RefSeq:XP_006732473.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006732473.1};
RN [1] {ECO:0000313|RefSeq:XP_006732473.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006732473.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC {ECO:0000256|ARBA:ARBA00010589}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006732473.1; XM_006732410.2.
DR AlphaFoldDB; A0A2U3XMB0; -.
DR STRING; 9713.A0A2U3XMB0; -.
DR GeneID; 102750145; -.
DR KEGG; lww:102750145; -.
DR CTD; 81669; -.
DR OrthoDB; 4848076at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd20590; CYCLIN_CCNL2_rpt1; 1.
DR CDD; cd20593; CYCLIN_CCNL2_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
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; CYCLIN; 1.
DR PANTHER; PTHR10026:SF45; CYCLIN-L2; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF036580; Cyclin_L; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 85..187
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 196..320
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 200..284
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 323..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58695 MW; 06C9C420838314E3 CRC64;
MAAAAATVAA GAPGPAAPAA AACAPGSGSA APGSQGMLIG DRLYSGVLIT LENCLLPDDK
LRFTPSMSSG LDTDTETDLR VVGCELIQAA GILLRLPQVA MATGQVLFQR FFYTKSFVKH
SMEHVSMACV HLASKIEEAP RRIRDVINVF HRLRHLREKK KPVPLLLDQD YVNLKNQIIK
AERRVLKELG FCVHVKHPHK IIVMYLQVLE CERNQHLVQT SWNYMNDSLR TDVFVRFQPE
SIACACIYLA ARTLEIPLPN RPHWFLLFGA TEDEIQEICL KILQLYTRKK VDLTHLESEV
EKRRHAIEEA KAQAKGLLPA GTQVLDSTSG FSPAPKLAES PKEGKGNKPS PLSVKNAKRK
MEGVKKVKAD SPVNGLPKGR GSRSRSGSRE QSYSRSPSRS ASPKRRKSDS GSTSGGSKSQ
SRSRSRSDSP PRQVHRGVPY KSSKVRSYRK SKDCKYPTQK PHKSRSRSSS RSRSRSRERA
DSSGKYKKKS HYYRDQRRER SRSYERTSHR YERDHPGHSR HRR
//