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Database: UniProt
Entry: A0A3B4T476_SERDU
LinkDB: A0A3B4T476_SERDU
Original site: A0A3B4T476_SERDU 
ID   A0A3B4T476_SERDU        Unreviewed;      1077 AA.
AC   A0A3B4T476;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Retinoblastoma-like protein 2 {ECO:0000313|Ensembl:ENSSDUP00000000948.1};
GN   Name=RBL2 {ECO:0000313|Ensembl:ENSSDUP00000000948.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000000948.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000000948.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC       {ECO:0000256|ARBA:ARBA00009475}.
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DR   AlphaFoldDB; A0A3B4T476; -.
DR   STRING; 41447.ENSSDUP00000000948; -.
DR   Ensembl; ENSSDUT00000000992.1; ENSSDUP00000000948.1; ENSSDUG00000000771.1.
DR   GeneTree; ENSGT00950000183202; -.
DR   OrthoDB; 519973at2759; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd20606; CYCLIN_RBL2; 1.
DR   CDD; cd00043; CYCLIN_SF; 1.
DR   Gene3D; 1.10.472.140; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 3.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR002720; RB_A.
DR   InterPro; IPR002719; RB_B.
DR   InterPro; IPR015030; RB_C.
DR   InterPro; IPR028309; RB_fam.
DR   InterPro; IPR024599; RB_N.
DR   PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 1.
DR   PANTHER; PTHR13742:SF8; RETINOBLASTOMA-LIKE PROTEIN 2; 1.
DR   Pfam; PF11934; DUF3452; 1.
DR   Pfam; PF01858; RB_A; 1.
DR   Pfam; PF01857; RB_B; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SMART; SM01367; DUF3452; 1.
DR   SMART; SM01368; RB_A; 1.
DR   SMART; SM01369; Rb_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          63..205
FT                   /note="Retinoblastoma-associated protein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01367"
FT   DOMAIN          377..570
FT                   /note="Retinoblastoma-associated protein A-box"
FT                   /evidence="ECO:0000259|SMART:SM01368"
FT   DOMAIN          783..946
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          959..1077
FT                   /note="Retinoblastoma-associated protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01369"
FT   REGION          589..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..892
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1077 AA;  119867 MW;  FA74F2723DA888B0 CRC64;
     MSDEDEFLQK ARAGFEDLCR ALNMDEEAST EAWKTYENIS RNFTLEGSEL HWLACALYVA
     CRSSVPTVGK GTVEGNYVSL TRILRCSEMS LIEFFNKMKK WQDMADLPQD FRQSTEKLER
     NFTVSAVIFK KYVPIFKAIF KAPSEEPPRV HRSRKQRRHP CTVTEVFNFC WVLFVHAKGN
     FPMISDDLVN SYHLLLCALD LVFTNALLCH ARKDLLNPDF TGLPEDFSSK DYRPSSGPYC
     FIEQLCELHE GLVLEAKGVK EHFWKPFIKK LFHKRILRGK EDSLTGFLDP MNFGDSFLSL
     SRVYEEHVLA TGSLDERIFT GEGASEDIGT PGPCLCEGVE NQDSATYRLH TNLTASALKV
     STPLTGRKYV QENSLASPVS SAMKSVGRLH TLLSGTKQGP SPKLTETLRT CARDPSDVIS
     KRLKDMFDLF SQHYEKSGAE KRGMGKDMAV KYFHLAEALY YRILESIIER EKMILGDADL
     SCILEQDIFH RSLLACCLEI VTFSYRPPGD FPNVITIFQL PAYHFYKVIE VLVRSEQGLF
     REVVKHLNQV EEQVLESLAW TRDSPLWESL RGAKDLVPAC QEVMPPQYLE QNDDSSTGSV
     PNTPVNHGPE LNTNSTVKGV SPSPTTLLDR YSSSPTGTAR RRLFVDPVDG ETGVTSTSST
     STTSTTPTSV TKTRQASLVT AIPAGQTVVT MATATVTANN GQTVTIPVQG IANESGGITF
     IPVQVSVTGQ GGATLQPLSA QTLTGTLTVQ SAVTKPAAKP ASSPLRKGSL SLFFRKVYHL
     ASVRLRDLCA KLDISSELRR KIWTCFEYSL VHCTDLMMDR HLDQLLMCAV YVMAKVTKED
     KSFQNIMKCY RTQPQASSNV YRSVLISGRR RRHSGTNDTN KQNSSPDTSL DPAGGDNSPV
     PIRSSSTLPA PQPGSAPSTP NKNPSSSSSA EEERGDLIHF YNNVYIKQMR LFALRYSPSS
     PSAGVESPSL CPYPTLRIGS PRRMLLSSKH SIYISPHKTG SAPSPTTPRD KIYYYICSSP
     PNRLQEINSM IRTGETPTRK RSMPLEDETS PKRVCPDNHS ALLRRLQDVA NDRSSSH
//
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