ID   A0A3Q1IFA7_ANATE        Unreviewed;       846 AA.
AC   A0A3Q1IFA7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Retinoblastoma 1 {ECO:0000313|Ensembl:ENSATEP00000020332.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000020332.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000020332.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q1IFA7; -.
DR   Ensembl; ENSATET00000020682.2; ENSATEP00000020332.1; ENSATEG00000013597.2.
DR   GeneTree; ENSGT00950000183202; -.
DR   Proteomes; UP000265040; 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:0051172; P:negative regulation of nitrogen compound metabolic process; IEA:UniProt.
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; cd20599; CYCLIN_RB; 1.
DR   Gene3D; 1.10.472.140; -; 1.
DR   Gene3D; 6.10.250.530; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
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:SF17; RETINOBLASTOMA-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 1.
DR   Pfam; PF11934; DUF3452; 1.
DR   Pfam; PF01858; RB_A; 1.
DR   Pfam; PF01857; RB_B; 1.
DR   Pfam; PF08934; Rb_C; 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   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          84..195
FT                   /note="Retinoblastoma-associated protein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01367"
FT   DOMAIN          338..533
FT                   /note="Retinoblastoma-associated protein A-box"
FT                   /evidence="ECO:0000259|SMART:SM01368"
FT   DOMAIN          606..715
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          714..846
FT                   /note="Retinoblastoma-associated protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01369"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..846
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   846 AA;  95961 MW;  3918466A3FF2C4B3 CRC64;
     MPPKKRSSGA TQSKELKPSA EGASPDKKES PEHRDKDAEF VTLCKSLHVT DLVCDRAWVL
     WKTVQDSTDE VTEVQKKLWG ACLFVTATDM DASCFTFTQV LKAVNLSVKQ FVALVKKLDV
     NLDTISTKVN SALARLEKKY DVMLALYQRF EKERDTMRSC WTMFLLAKGR ALQMDDDLVI
     SFQLLLCTLE LFIKRCPSEL LQAPYTVSKV QSPPTRTSRR NQSRAKPRPP EPEVDVQLLE
     TLCKENDCNT EEVKNVYQTS FSAFLDSLDL SRSPDFPQVN DLDQQYEEHY LKSRDIDGRL
     FFDGDETVLA PKLEITQVER TPKKNLPDED AVLIPPQTPI RAAMTSIQQL RGGLISSGDQ
     PSTILTTYFK NCTVDPTQDI QKRLETLEQV FSQRFAQAVG PRCAVLGKQR FTLGVRLYYR
     VMEELLKSVH KLLNDSTFHT SLLACALEVV MATYGGTGGY NSAGGDPAET DVCFPWILDT
     FSLAAFDFYK VIESFIKAFP TVTKDIIKHL ETCENLIMER IAWRTGSLLF ELLKQECESG
     AAVEQVETTA SFAQPLQHNH TAADLYLSPV RPGLRILPPD SPSSPRHPKS NSLSLFYKKL
     YRLAYMRLKT LCSYLLSSHP ELEPIIWTLF QYTLQHEYEL MKDRHLDQLM MSAMYAICKV
     KSVDLRFKTI VTAYKNLPNT NQETFKNVLI SEGHYDSIIV FYNQVFMQKL KTNILQYASN
     RPPTLSPIPQ IPRSPYKFPN SPLRVPGSNN VYVSPLKSPR MSPSIMTPRS RMLVSIGESF
     GLSNRFQKIN QMVNNSDRSF KRTHDLGSTP KPLKRLRFDV DGQDEADGSK SSGDSTLIQK
     LAEMSK
//