ID A0A2U3Y2E6_LEPWE Unreviewed; 730 AA.
AC A0A2U3Y2E6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cyclin-T2 isoform X1 {ECO:0000313|RefSeq:XP_006737808.1};
GN Name=CCNT2 {ECO:0000313|RefSeq:XP_006737808.1};
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_006737808.1};
RN [1] {ECO:0000313|RefSeq:XP_006737808.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006737808.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR RefSeq; XP_006737808.1; XM_006737745.2.
DR AlphaFoldDB; A0A2U3Y2E6; -.
DR STRING; 9713.A0A2U3Y2E6; -.
DR GeneID; 102726907; -.
DR KEGG; lww:102726907; -.
DR CTD; 905; -.
DR OrthoDB; 4848076at2759; -.
DR Proteomes; UP000245341; Unplaced.
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; cd20596; CYCLIN_CCNT2_rpt1; 1.
DR CDD; cd20598; CYCLIN_CCNT2_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; IPR047321; CYCLIN_CCNT2_rpt1.
DR InterPro; IPR047322; CYCLIN_CCNT2_rpt2.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF43; CYCLIN-T2; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF21797; CycT2-like_C; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341}.
FT DOMAIN 42..141
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 154..242
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 404..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..584
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 81207 MW; 45B76FE86F383438 CRC64;
MASGRGASSR WFFTREQLEN TPSRRCGVEA DKELSYRQQA ANLIQDMGQR LNVSQLTINT
AIVYMHRFYM HHSFTKFNRN IISPTALFLA AKVEEQARKL EHVIKVAHAC LHPLEPLLDT
KCDAYLQQTQ ELVLLETIML QTLGFEITIE HPHTDVVKCT QLVRASKDLA QTSYFMATNS
LHLTTFCLQY KPTVIACVCI HLACKWSNWE IPVSTDGKHW WEYVDPTVTL ELLDELTHEF
LQILEKTPSR LKRIRNWRAN QAAKKPKVDG QVSETPLLGS SLVQNSILVD SVTGVPTNPS
FQKPSTSAFP APVPLNSGNI SVQDSHTSDN LSMLATGMPS TSYGLSSHQE WPQHQESART
EQMYSQKQET SLSGTQYNIN FQQGPSISLH SGLHHRPDRI SDHSSIKQEY AHKAGSSKHH
GPISATPGVI PQKMSLDKYR EKRKLETLDL DVRDHYVAAQ VEQQHKHVQS QPASSSSVTS
PIKMKIPITN TEKPEKCMAE KKEKSGSLKL RIPIPPTDKS ASKEELKMKI KVASSERHSS
SDEGSGKSKH SSPHISRDHK EKHKDHPSNR HHPSSHKHSH SHSGGSSKHS ADGIPPTVLR
SPVGLSSDGI SSSSGSSRKK LHVSDASHNH HSKMSKSSKS SGSSSSSSSS VKQYIPSHSS
VFNHPLPPPP PVTYQVGYGQ LSTLVKLDKK PVETNGPDVN HEYSTNSQHM DYKDTFDMLD
SLLSAQGMNM
//
