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Database: UniProt
Entry: A3DUJ4_XIPMA
LinkDB: A3DUJ4_XIPMA
Original site: A3DUJ4_XIPMA 
ID   A3DUJ4_XIPMA            Unreviewed;       912 AA.
AC   A3DUJ4;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=RB transcriptional corepressor 1 {ECO:0000313|Ensembl:ENSXMAP00000030748.1};
DE   SubName: Full=Retinoblastoma susceptibility protein {ECO:0000313|EMBL:ABD78137.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|EMBL:ABD78137.1};
RN   [1] {ECO:0000313|EMBL:ABD78137.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17011832; DOI=10.1016/j.cbpc.2006.07.013;
RA   Butler A.P., Trono D., Coletta L.D., Beard R., Fraijo R., Kazianis S.,
RA   Nairn R.S.;
RT   "Regulation of CDKN2A/B and Retinoblastoma genes in Xiphophorus melanoma.";
RL   Comp. Biochem. Physiol. C Toxicol. Pharmacol. 145:145-155(2007).
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [4] {ECO:0000313|Ensembl:ENSXMAP00000030748.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000030748.1};
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   EMBL; DQ418730; ABD78137.1; -; mRNA.
DR   RefSeq; NP_001273236.1; NM_001286307.2.
DR   STRING; 8083.ENSXMAP00000030748; -.
DR   Ensembl; ENSXMAT00000036253.1; ENSXMAP00000030748.1; ENSXMAG00000015729.2.
DR   GeneID; 102230233; -.
DR   KEGG; xma:102230233; -.
DR   CTD; 5925; -.
DR   GeneTree; ENSGT00950000183202; -.
DR   HOGENOM; CLU_008943_2_0_1; -.
DR   OMA; VKDIGCI; -.
DR   OrthoDB; 519973at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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; 6.10.140.1380; -; 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   2: Evidence at transcript level;
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:UP000002852};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          91..214
FT                   /note="Retinoblastoma-associated protein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01367"
FT   DOMAIN          359..562
FT                   /note="Retinoblastoma-associated protein A-box"
FT                   /evidence="ECO:0000259|SMART:SM01368"
FT   DOMAIN          652..739
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          760..912
FT                   /note="Retinoblastoma-associated protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01369"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..894
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  103867 MW;  121BFF32BEB0130B CRC64;
     MPPKKRHSGT TQNKEPKPSA DSASPPDKQD SPELSEKKHR EKHAEFVSLC KSLHVSDLVC
     DRAWTLWESV RESMDKVPGS QQRLWGACLF VIITDMDTGS FTVTQVLKAV SLNLKQFLAL
     VRQLDVNLDT ISMKVNSALT RLEKKYDVML ALYQRFEKTC KNIFVLTSDG RERETMRTCW
     TMFLLAKGRA LQMEDDLVIS FQLLLCTLEL FIKRCSSDQL QSLYQSAISK VLSPPTRTSR
     RNQSKAKSRP SEPEVDAQLL ETLCKDNECN FEEVKNVYQT SFLAFLDSTD LSRSIDFPQV
     NDVNQQYEEL YLKSRDIDGR LFFDGDETVL PPKFEISKVE RTPKKNQPEE DGPMIPPQTP
     IRAAMTSIRM LRGDLPSNGD QPSTTLTTYF KNCTVDPTQD VQKRLETLGQ VFSQKFGEAV
     GPHCVVYGRQ RFALGVRLYY KVMEAMLKSE EKRLSVQNFS KLLNDFTFHT SLLACSLEVV
     MATYEESSFK NGGSDQTGTN LCFPWILNVL NLSAFDFYKV IESFIKAEPT LSKDIIKHLE
     TCENLIMERI AWRTGSPLFE LLKQEHASAA AEPVETPASF SQPLQHSHTA ADLYLTPTRP
     ASRVLPPDSP ATPPQQPTAS QSTSQAPCQA PRQPKSNSLS LFYKKLYRLA YTRLKTLCSY
     LLSSHPELEP IIWTLFQYTL QHEYELMRDR HLDQLMMSAM YAICKVKSVD LRFKSIVSAY
     KNMTNTNQET FKNVLIIEGH YDSIIVFYNQ VFMQKLKTNI LQHASIRPPP LSPIPQIPRS
     PYKLPNSPLR VPGSNNIYIS PLRSSRMSPG IMTPRSRMLV SIGESFGLGN RFQKINQMVN
     SERSHKRTMD QSAAIKPLKK LRFDVDGQDE ADGSKPGGDS TLIQKLTEMS STWSRMHEQK
     MKEEPETRDE PQ
//
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