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Database: UniProt
Entry: A0A2Y9KI14_ENHLU
LinkDB: A0A2Y9KI14_ENHLU
Original site: A0A2Y9KI14_ENHLU 
ID   A0A2Y9KI14_ENHLU        Unreviewed;       386 AA.
AC   A0A2Y9KI14;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=G2/mitotic-specific cyclin-B1 {ECO:0000256|ARBA:ARBA00035702};
GN   Name=LOC111155277 {ECO:0000313|RefSeq:XP_022371114.1};
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_022371114.1};
RN   [1] {ECO:0000313|RefSeq:XP_022371114.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022371114.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. {ECO:0000256|ARBA:ARBA00003222}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006955}.
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DR   RefSeq; XP_022371114.1; XM_022515406.1.
DR   AlphaFoldDB; A0A2Y9KI14; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR   CDD; cd20565; CYCLIN_CCNB1_rpt1; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR048026; CCNB1_first_cyclin-box.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF193; G2_MITOTIC-SPECIFIC CYCLIN-B1; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 2.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT   DOMAIN          197..281
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          290..386
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          294..377
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          29..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  43048 MW;  4B4549CB40067907 CRC64;
     MALRVTRNAK VNVENKAKIS MAGAKRVPLA TTAASKPGLR PRTALGDIGN KVSEQPQAKL
     PLKKEAKTLV PGKVIAKKLP KPLEKAPEPV PEPEPEPEPV KEEKLSPEPI LVDTPSPSPM
     ETSGCAPAEE YLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ LEEEQAIRPK
     YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP KKMLQLVGVT
     AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RSLNFGLGRP LPLHFLRRAS
     KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGD WTIKNKYATS
     KHAKISTLAQ LNSALVQDLA KAVAKV
//
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