GenomeNet

Database: UniProt
Entry: H0VCW3_CAVPO
LinkDB: H0VCW3_CAVPO
Original site: H0VCW3_CAVPO 
ID   H0VCW3_CAVPO            Unreviewed;       840 AA.
AC   H0VCW3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=RB transcriptional corepressor 1 {ECO:0000313|Ensembl:ENSCPOP00000007795.3};
GN   Name=RB1 {ECO:0000313|Ensembl:ENSCPOP00000007795.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000007795.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000007795.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000007795.3};
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; AAKN02011171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02011172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02011173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02011174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02011175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0VCW3; -.
DR   STRING; 10141.ENSCPOP00000007795; -.
DR   Ensembl; ENSCPOT00000008761.3; ENSCPOP00000007795.3; ENSCPOG00000008683.4.
DR   VEuPathDB; HostDB:ENSCPOG00000008683; -.
DR   eggNOG; KOG1010; Eukaryota.
DR   GeneTree; ENSGT00950000183202; -.
DR   HOGENOM; CLU_015754_0_0_1; -.
DR   InParanoid; H0VCW3; -.
DR   OMA; VKDIGCI; -.
DR   TreeFam; TF105568; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000008683; Expressed in cerebellum and 12 other cell types or tissues.
DR   GO; GO:0061793; C:chromatin lock complex; IEA:Ensembl.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IEA:Ensembl.
DR   GO; GO:0016605; C:PML body; IEA:Ensembl.
DR   GO; GO:0035189; C:Rb-E2F complex; IEA:Ensembl.
DR   GO; GO:0005819; C:spindle; IEA:Ensembl.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0061676; F:importin-alpha family protein binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR   GO; GO:0051301; P:cell division; IEA:Ensembl.
DR   GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:Ensembl.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR   GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0031507; P:heterochromatin formation; IEA:Ensembl.
DR   GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IEA:Ensembl.
DR   GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:1904761; P:negative regulation of myofibroblast differentiation; IEA:Ensembl.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:1904028; P:positive regulation of collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0071459; P:protein localization to chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR   GO; GO:0031134; P:sister chromatid biorientation; IEA:Ensembl.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          15..141
FT                   /note="Retinoblastoma-associated protein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01367"
FT   DOMAIN          285..485
FT                   /note="Retinoblastoma-associated protein A-box"
FT                   /evidence="ECO:0000259|SMART:SM01368"
FT   DOMAIN          572..673
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          680..839
FT                   /note="Retinoblastoma-associated protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01369"
FT   REGION          521..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..805
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   840 AA;  96361 MW;  E74CD65B7BB81790 CRC64;
     KDYIQKKKEL WGICIFIAAV DLDEMPFTFT ELQKNIETSV YKFFDLVKEI DTSTKVDNAM
     SRLLKKYNVL CALYSKLERT CELIYLTQPS SSLSTEINSA LVLKVSWITF LLAKGDVLQM
     EDDLVISFQL MLCVLDYFIK LSPPVLLREP YKTAVIPISG SPRTPRRGQN RSARIAKQLE
     NDTRIIEVLC KEHECNIDEV KNVYFKNFIP FMNTLGIVTS NGLPEVESLS KRYEEIYLKN
     KDIDARLFLD HDKTLQADPI DSFEMQRTPQ KSNPDEEVNV IPPHTPVRTV MNTIQQLMMI
     LNSASDQPSE ILISYFNNCT VNPKENILKR VKDIGHIFKE KFAKAVGQGC IEIGSQRYKL
     GVRLYYRVME SMLKSEEERL SIQNFSKLLN DNIFHMSLLA CALEVVMATY SRSTSQNLDS
     GTDLSFPWIL NVLNLKAFDF YKVIESFIKA EANLTREMIK HLERCEHRIM ESLAWLSDSP
     LFDLIKQSKD REGPADHLES ACPLNLPLQN NHTAADMYLS PIRSPKKKGS TTRGNSTANA
     ETQATSAFQT QRPLKSTSLS LFYKKVYRLA YLRLNTLCAR LLSDHPELEH IIWTLFQHTL
     QNEYELMRDR HLDQIMMCSM YGICKVKNID LKFKIIVTAY KDLPHAVQET FKRVLIREDE
     YDSIIVFYNS VFMQRLKTNI LQYASTRPPT LSPIPHIPRS PYKFSSSPLR IPGGNIYISP
     LKSPYKISEG LPTPTKMTPT SRILVSIGES FGTSEKFQKI NQMVGNSDRV LKRSAEGSNP
     PKPLKKLRFD IEGSDEADGS KHLPGESKFQ QKLAEMTSTR TRMQKQKMND SMDASNKEEQ
//
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