ID A0A2Y9JQS5_ENHLU Unreviewed; 520 AA.
AC A0A2Y9JQS5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cyclin-L1 {ECO:0000256|ARBA:ARBA00019921};
GN Name=LOC111149218 {ECO:0000313|RefSeq:XP_022361884.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022361884.1};
RN [1] {ECO:0000313|RefSeq:XP_022361884.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022361884.1};
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}.
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DR RefSeq; XP_022361884.1; XM_022506176.1.
DR AlphaFoldDB; A0A2Y9JQS5; -.
DR Proteomes; UP000248482; 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; cd20592; CYCLIN_CCNL1_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:SF64; CYCLIN-L1; 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:UP000248482}.
FT DOMAIN 88..190
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 199..314
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 203..287
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..409
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..442
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..520
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 58788 MW; 2DE4CD050CC1210E CRC64;
MASGPHPTAT AAAAASSAAP SAGGSSSGTT TTTTTTTGGI LIGDRLYSEV SLTIDHSLIP
EERLSPTPSM QDGLDLPSET DLRILGCELI QAAGILLRLP QVAMATGQVL FHRFFYSKSF
VKHSFEIVAM ACINLASKIE EAPRRIRDVI NVFHHLRQLR GKRTPSPLIL DQNYINTKNQ
VIKAERRVLK ELGFCVHVKH PHKIIVMYLQ VLECERNQTL VQTAWNYMND SLRTNVFVRF
QPETIACACI YLAARALQIP LPTRPHWFLL FGTTEEEIQE ICIETLRLYT RKKPNYELLE
KEVEKRKVAL QEAKLKAKGL NPDGTPALST LGGFSPASKP SSPREVKAEE KSPISVNVKT
VKKEPEDRQQ ASKSPYNGKD SKRSRNSRSA SRSRSRTRSR SRSHTPRRQR SRSGTYSSRS
RSRSRSHSES PRRHHNHGSP HLKAKHTRDD LKSSNRHGHK RKKSRSRSQS KSRDHSDAAK
KHRHERGHHR DRRERSRSFE RSHKGKHHGG SRSGHGRHRR
//
