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Retinoblastoma-like protein homolog lin-35 (Abnormal cell lineage protein 35) (Synthetic multivulva protein lin-35)

 LIN35_CAEEL             Reviewed;         961 AA.
G5EDT1;
05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
22-NOV-2017, entry version 63.
RecName: Full=Retinoblastoma-like protein homolog lin-35 {ECO:0000305};
AltName: Full=Abnormal cell lineage protein 35 {ECO:0000312|WormBase:C32F10.2};
AltName: Full=Synthetic multivulva protein lin-35 {ECO:0000305};
Name=lin-35 {ECO:0000312|WormBase:C32F10.2};
ORFNames=C32F10.2 {ECO:0000312|WormBase:C32F10.2};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:AAD05570.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH LIN-53,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=9875852; DOI=10.1016/S0092-8674(00)81722-5;
Lu X., Horvitz H.R.;
"lin-35 and lin-53, two genes that antagonize a C. elegans Ras
pathway, encode proteins similar to Rb and its binding protein
RbAp48.";
Cell 95:981-991(1998).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11684669;
Boxem M., van den Heuvel S.;
"lin-35 Rb and cki-1 Cip/Kip cooperate in developmental regulation of
G1 progression in C. elegans.";
Development 128:4349-4359(2001).
[4] {ECO:0000305}
INTERACTION WITH DPL-1 AND EFL-1.
PubMed=11463372; DOI=10.1016/S1097-2765(01)00194-0;
Ceol C.J., Horvitz H.R.;
"dpl-1 DP and efl-1 E2F act with lin-35 Rb to antagonize Ras signaling
in C.elegans vulval development.";
Mol. Cell 7:461-473(2001).
[5] {ECO:0000305}
FUNCTION.
PubMed=12062054;
Boxem M., van den Heuvel S.;
"C. elegans class B synthetic multivulva genes act in G(1)
regulation.";
Curr. Biol. 12:906-911(2002).
[6] {ECO:0000305}
FUNCTION.
PubMed=11850412; DOI=10.1101/gad.952302;
Fay D.S., Keenan S., Han M.;
"fzr-1 and lin-35/Rb function redundantly to control cell
proliferation in C. elegans as revealed by a nonbiased synthetic
screen.";
Genes Dev. 16:503-517(2002).
[7] {ECO:0000305}
FUNCTION.
PubMed=12783801;
Fay D.S., Large E., Han M., Darland M.;
"lin-35/Rb and ubc-18, an E2 ubiquitin-conjugating enzyme, function
redundantly to control pharyngeal morphogenesis in C. elegans.";
Development 130:3319-3330(2003).
[8] {ECO:0000305}
FUNCTION.
PubMed=15315757; DOI=10.1016/j.cell.2004.07.026;
Reddy K.C., Villeneuve A.M.;
"C. elegans HIM-17 links chromatin modification and competence for
initiation of meiotic recombination.";
Cell 118:439-452(2004).
[9] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15196946; DOI=10.1016/j.ydbio.2004.03.022;
Fay D.S., Qiu X., Large E., Smith C.P., Mango S., Johanson B.L.;
"The coordinate regulation of pharyngeal development in C. elegans by
lin-35/Rb, pha-1, and ubc-18.";
Dev. Biol. 271:11-25(2004).
[10] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15328017; DOI=10.1016/j.ydbio.2004.06.009;
Bender A.M., Wells O., Fay D.S.;
"lin-35/Rb and xnp-1/ATR-X function redundantly to control somatic
gonad development in C. elegans.";
Dev. Biol. 273:335-349(2004).
[11] {ECO:0000305}
FUNCTION.
PubMed=15238519; DOI=10.1534/genetics.103.026021;
Garbe D., Doto J.B., Sundaram M.V.;
"Caenorhabditis elegans lin-35/Rb, efl-1/E2F and other synthetic
multivulva genes negatively regulate the anaphase-promoting complex
gene mat-3/APC8.";
Genetics 167:663-672(2004).
[12] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15280233; DOI=10.1534/genetics.103.024554;
Cui M., Fay D.S., Han M.;
"lin-35/Rb cooperates with the SWI/SNF complex to control
Caenorhabditis elegans larval development.";
Genetics 167:1177-1185(2004).
[13] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15649460; DOI=10.1016/j.ydbio.2004.10.014;
Cardoso C., Couillault C., Mignon-Ravix C., Millet A., Ewbank J.J.,
Fontes M., Pujol N.;
"XNP-1/ATR-X acts with RB, HP1 and the NuRD complex during larval
development in C. elegans.";
Dev. Biol. 278:49-59(2005).
[14] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=15621535; DOI=10.1016/j.devcel.2004.11.015;
Myers T.R., Greenwald I.;
"lin-35 Rb acts in the major hypodermis to oppose ras-mediated vulval
induction in C. elegans.";
Dev. Cell 8:117-123(2005).
[15] {ECO:0000305}
INTERACTION WITH LIN-8.
PubMed=16020796; DOI=10.1534/genetics.104.034173;
Davison E.M., Harrison M.M., Walhout A.J., Vidal M., Horvitz H.R.;
"lin-8, which antagonizes Caenorhabditis elegans Ras-mediated vulval
induction, encodes a novel nuclear protein that interacts with the
LIN-35 Rb protein.";
Genetics 171:1017-1031(2005).
[16] {ECO:0000305}
FUNCTION.
PubMed=16287966; DOI=10.1073/pnas.0508989102;
Grishok A., Sharp P.A.;
"Negative regulation of nuclear divisions in Caenorhabditis elegans by
retinoblastoma and RNA interference-related genes.";
Proc. Natl. Acad. Sci. U.S.A. 102:17360-17365(2005).
[17] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16624904; DOI=10.1534/genetics.106.056465;
Ceol C.J., Stegmeier F., Harrison M.M., Horvitz H.R.;
"Identification and classification of genes that act antagonistically
to let-60 Ras signaling in Caenorhabditis elegans vulval
development.";
Genetics 173:709-726(2006).
[18] {ECO:0000305}
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=16507136; DOI=10.1186/gb-2006-7-1-r4;
Lehner B., Calixto A., Crombie C., Tischler J., Fortunato A.,
Chalfie M., Fraser A.G.;
"Loss of LIN-35, the Caenorhabditis elegans ortholog of the tumor
suppressor p105Rb, results in enhanced RNA interference.";
Genome Biol. 7:R4.1-R4.10(2006).
[19] {ECO:0000305}
FUNCTION, AND IDENTIFICATION IN THE DRM COMPLEX.
PubMed=17075059; DOI=10.1073/pnas.0608461103;
Harrison M.M., Ceol C.J., Lu X., Horvitz H.R.;
"Some C. elegans class B synthetic multivulva proteins encode a
conserved LIN-35 Rb-containing complex distinct from a NuRD-like
complex.";
Proc. Natl. Acad. Sci. U.S.A. 103:16782-16787(2006).
[20] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17417969; DOI=10.1186/1471-213X-7-30;
Ceron J., Rual J.F., Chandra A., Dupuy D., Vidal M.,
van den Heuvel S.;
"Large-scale RNAi screens identify novel genes that interact with the
C. elegans retinoblastoma pathway as well as splicing-related
components with synMuv B activity.";
BMC Dev. Biol. 7:30-30(2007).
[21] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17466069; DOI=10.1186/1471-213X-7-38;
Ouellet J., Roy R.;
"The lin-35/Rb and RNAi pathways cooperate to regulate a key cell
cycle transition in C. elegans.";
BMC Dev. Biol. 7:38-38(2007).
[22] {ECO:0000305}
FUNCTION.
PubMed=17881492; DOI=10.1242/dev.004606;
Schertel C., Conradt B.;
"C. elegans orthologs of components of the RB tumor suppressor complex
have distinct pro-apoptotic functions.";
Development 134:3691-3701(2007).
[23] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17070797; DOI=10.1016/j.ydbio.2006.09.051;
Bender A.M., Kirienko N.V., Olson S.K., Esko J.D., Fay D.S.;
"lin-35/Rb and the CoREST ortholog spr-1 coordinately regulate vulval
morphogenesis and gonad development in C. elegans.";
Dev. Biol. 302:448-462(2007).
[24] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17237514; DOI=10.1534/genetics.106.068148;
Reddien P.W., Andersen E.C., Huang M.C., Horvitz H.R.;
"DPL-1 DP, LIN-35 Rb and EFL-1 E2F act with the MCD-1 zinc-finger
protein to promote programmed cell death in Caenorhabditis elegans.";
Genetics 175:1719-1733(2007).
[25] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18437219; DOI=10.1371/journal.pgen.1000059;
Kirienko N.V., McEnerney J.D., Fay D.S.;
"Coordinated regulation of intestinal functions in C. elegans by LIN-
35/Rb and SLR-2.";
PLoS Genet. 4:E1000059-E1000059(2008).
[26] {ECO:0000305}
FUNCTION.
PubMed=19521497; DOI=10.1371/journal.pgen.1000510;
Mani K., Fay D.S.;
"A mechanistic basis for the coordinated regulation of pharyngeal
morphogenesis in Caenorhabditis elegans by LIN-35/Rb and UBC-18-ARI-
1.";
PLoS Genet. 5:E1000510-E1000510(2009).
[27] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22542970; DOI=10.1534/genetics.112.140152;
Polley S.R., Fay D.S.;
"A network of genes antagonistic to the LIN-35 retinoblastoma protein
of Caenorhabditis elegans.";
Genetics 191:1367-1380(2012).
[28] {ECO:0000305}
FUNCTION.
PubMed=23664972; DOI=10.1016/j.cub.2013.04.046;
Cui M., Cohen M.L., Teng C., Han M.;
"The tumor suppressor Rb critically regulates starvation-induced
stress response in C. elegans.";
Curr. Biol. 23:975-980(2013).
[29] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23347407; DOI=10.1186/gb-2013-14-1-r5;
Kudron M., Niu W., Lu Z., Wang G., Gerstein M., Snyder M., Reinke V.;
"Tissue-specific direct targets of Caenorhabditis elegans Rb/E2F
dictate distinct somatic and germline programs.";
Genome Biol. 14:R5.1-R5.17(2013).
[30] {ECO:0000305}
FUNCTION.
PubMed=24214340; DOI=10.1534/genetics.113.158485;
Polley S.R., Kuzmanov A., Kuang J., Karpel J., Lazetic V.,
Karina E.I., Veo B.L., Fay D.S.;
"Implicating SCF complexes in organogenesis in Caenorhabditis
elegans.";
Genetics 196:211-223(2014).
[31] {ECO:0000305}
FUNCTION.
PubMed=24752899; DOI=10.1128/MCB.01532-13;
Lascarez-Lagunas L.I., Silva-Garcia C.G., Dinkova T.D., Navarro R.E.;
"LIN-35/Rb causes starvation-induced germ cell apoptosis via CED-
9/Bcl2 downregulation in Caenorhabditis elegans.";
Mol. Cell. Biol. 34:2499-2516(2014).
[32] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24715729; DOI=10.1073/pnas.1321698111;
Kozlowski L., Garvis S., Bedet C., Palladino F.;
"The Caenorhabditis elegans HP1 family protein HPL-2 maintains ER
homeostasis through the UPR and hormesis.";
Proc. Natl. Acad. Sci. U.S.A. 111:5956-5961(2014).
[33] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26100681; DOI=10.1534/g3.115.019257;
Kelly A.L., Senter-Zapata M.J., Campbell A.C., Lust H.E.,
Theriault M.E., Andralojc K.M., Updike D.L.;
"A forward genetic screen for suppressors of somatic P granules in
Caenorhabditis elegans.";
G3 (Bethesda) 5:2209-2215(2015).
[34] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-714 AND
THR-719, AND DISRUPTION PHENOTYPE.
PubMed=25562820; DOI=10.1038/ncomms6906;
The I., Ruijtenberg S., Bouchet B.P., Cristobal A., Prinsen M.B.,
van Mourik T., Koreth J., Xu H., Heck A.J., Akhmanova A., Cuppen E.,
Boxem M., Munoz J., van den Heuvel S.;
"Rb and FZR1/Cdh1 determine CDK4/6-cyclin D requirement in C. elegans
and human cancer cells.";
Nat. Commun. 6:5906-5906(2015).
[35] {ECO:0000305}
FUNCTION.
PubMed=27104746; DOI=10.1080/15384101.2016.1146839;
Lee Y.U., Son M., Kim J., Shim Y.H., Kawasaki I.;
"CDC-25.2, a C. elegans ortholog of cdc25, is essential for the
progression of intestinal divisions.";
Cell Cycle 15:654-666(2016).
-!- FUNCTION: Key regulator of cell division which acts as a
transcriptional repressor and negatively regulates cell cycle
progression in its active unphosphorylated form, but allows cell
cycle progression when phosphorylated (PubMed:11684669,
PubMed:12062054, PubMed:16287966, PubMed:17466069,
PubMed:25562820). When unphosphorylated and in its active form,
interacts with E2F transcription factors such as efl-1 to repress
their transcriptional activity and negatively regulate the
progression through the G1 phase of the cell cycle during
postembryonic development (PubMed:11684669, PubMed:12062054,
PubMed:15238519, PubMed:17466069, PubMed:25562820). May
furthermore act with cell cycle regulator cki-1 to negatively
regulate cell cycle progression (PubMed:11684669). Acts
redundantly with lin-53, fzr-1 and lin-23 to control cell cycle
progression by regulating the expression of G1 phase cyclins
(PubMed:11850412, PubMed:25562820). In particular, negatively
regulates the expression of the cyclin E homolog cye-1, which is
essential for the G1/S phase transition (PubMed:16287966,
PubMed:17466069). Regulates cell division in the intestinal
lineage, repressing the expression of genes such as cdc-25.2,
which are required for intestinal cells to transition from the
karyokinesis cell cycle (also known as nuclear division) to
endoreplication, a specific growth pathway in the intestinal
epithelium required for feeding and gut development in growing
larvae during the L1 stage molt (PubMed:17466069,
PubMed:27104746). Its role as a transcriptional repressor in the
regulation of intestinal cell division during postembryonic
development is most likely in complex with an E2F cell cycle
regulatory transcription factor efl-1 and its binding partner the
synthetic multivulva class B protein dpl-1 (PubMed:17466069).
Synthetic multivulva (synMuv) class B protein (PubMed:9875852,
PubMed:11850412). SynMuv proteins are required to repress the
induction of vulval development by Ras signaling and probably act
by forming the multiprotein DRM complex that represses
transcription (PubMed:9875852, PubMed:17075059). Together with
synMuv class B protein lin-53, and redundantly with synMuv class A
protein lin-15A, represses transcription to control vulval
development, most likely through antagonization of the Ras-
signaling pathway in the major hypodermal syncytium hyp7
(PubMed:9875852, PubMed:15621535, PubMed:16624904,
PubMed:26100681). Acts redundantly with the transcriptional
corepressor spr-1 and the zinc finger protein zfp-2 to play a role
in vulval morphogenesis, promote germline proliferation and
somatic gonad development (PubMed:17417969, PubMed:17070797). Acts
redundantly with ubc-18 in the regulation of pharyngeal
morphogenesis during embryonic develpment by negatively regulating
the expression of proteins such as sup-35 (PubMed:12783801,
PubMed:19521497, PubMed:24214340). Functions with the SWI/SNF
complex and proteins such as pha-1 to regulate larval development
(PubMed:15196946, PubMed:15280233). Functions redundantly with
xnp-1 to regulate somatic gonad development (PubMed:15328017,
PubMed:15649460). Acts redundantly with slr-2 to regulate the
expression of intestinal genes required for nutrient utilization
(PubMed:18437219, PubMed:22542970). Regulates transcription in
response to starvation (PubMed:23664972). Furthermore, in response
to starvation, promotes germ cell programmed cell death by
negatively regulating the expression of the anti-apoptotic protein
ced-9 (PubMed:17881492, PubMed:24752899). Conversely, in
conjuction with mcd-1, efl-1 and the synthetic multivulva class B
proteins dpl-1, lin-37 and lin-52, may also regulate transcription
to promote programmed cell death independently of ced-1, ced-8 and
ced-9 cell death pathways (PubMed:17237514). Directly involved in
heterochromatin formation by maintaining overall chromatin
structure and, in particular, that of constitutive heterochromatin
by stabilizing histone methylation (PubMed:23347407). In
particular, negatively regulates the expression of mes-4, a
histone methyltransferase that controls the expression of germline
specific genes (PubMed:23347407). May play a role in double strand
break formation during meiosis (PubMed:15315757). May suppress
sensitivity to RNAi (PubMed:16507136, PubMed:17417969). May play a
role in the response to endoplasmic reticulum (ER) stress
(PubMed:24715729). {ECO:0000269|PubMed:11684669,
ECO:0000269|PubMed:11850412, ECO:0000269|PubMed:12062054,
ECO:0000269|PubMed:12783801, ECO:0000269|PubMed:15196946,
ECO:0000269|PubMed:15280233, ECO:0000269|PubMed:15328017,
ECO:0000269|PubMed:15621535, ECO:0000269|PubMed:15649460,
ECO:0000269|PubMed:16287966, ECO:0000269|PubMed:16624904,
ECO:0000269|PubMed:17070797, ECO:0000269|PubMed:17075059,
ECO:0000269|PubMed:17237514, ECO:0000269|PubMed:17417969,
ECO:0000269|PubMed:17466069, ECO:0000269|PubMed:17881492,
ECO:0000269|PubMed:18437219, ECO:0000269|PubMed:19521497,
ECO:0000269|PubMed:22542970, ECO:0000269|PubMed:23347407,
ECO:0000269|PubMed:23664972, ECO:0000269|PubMed:24214340,
ECO:0000269|PubMed:24752899, ECO:0000269|PubMed:25562820,
ECO:0000269|PubMed:26100681, ECO:0000269|PubMed:27104746,
ECO:0000269|PubMed:9875852, ECO:0000305|PubMed:15315757,
ECO:0000305|PubMed:16507136, ECO:0000305|PubMed:24715729}.
-!- SUBUNIT: Component of the DRM complex, at least composed of lin-9,
lin-35, lin-37, lin-52, lin-53, lin-54, dpl-1 and efl-1
(PubMed:17075059). Interacts with lin-53 (PubMed:9875852).
Interacts (via C-terminus) with dpl-1 (via C-terminus) and efl-1
(via C-terminus) (PubMed:11463372). Interacts (via C-terminus)
with lin-8 (PubMed:16020796). {ECO:0000269|PubMed:11463372,
ECO:0000269|PubMed:16020796, ECO:0000269|PubMed:17075059,
ECO:0000269|PubMed:9875852}.
-!- INTERACTION:
Q22703:dpl-1; NbExp=2; IntAct=EBI-321470, EBI-324825;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15621535,
ECO:0000269|PubMed:23347407, ECO:0000269|PubMed:25562820,
ECO:0000269|PubMed:9875852}. Note=Expressed in dividing cells, but
decreased expression after cell cycle exit.
{ECO:0000269|PubMed:25562820}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos and newly hatched L1
larvae (PubMed:9875852). In older larvae and adults expressed in
P(3-8).p vulval precursor cells and its descendents
(PubMed:9875852). Expressed in the major hypodermal syncytium hyp7
during the L3 stage of larval development (PubMed:15621535).
{ECO:0000269|PubMed:15621535, ECO:0000269|PubMed:9875852}.
-!- PTM: Phosphorylated by the cyclin dependent kinase cdk-4.
Phosphorylation inhibits the transcriptional repressor activity of
lin-35 and allows for progression through the G1 phase of the cell
cycle during postembryonic development.
{ECO:0000269|PubMed:25562820}.
-!- DISRUPTION PHENOTYPE: Viable, but with a reduced fertility and
brood size (PubMed:11684669, PubMed:15328017, PubMed:15280233,
PubMed:17417969). Low penetrance defects including reduced
integrity of the proximal gonad, a low percentage of endomitotic
oocytes, distal tip cell migration defects and abnormalities in
vulval morphology (PubMed:17417969). Some studies demonstrate
aberrant intestinal nuclear divisions, with increased intestinal
nuclei in growing larvae (PubMed:17466069). In addition there is
increased sensitivity to RNA-induced gene silencing by RNAi
(PubMed:16507136, PubMed:17417969). RNAi-mediated knockdown
results in increased survival in response to ER stress inducer
tunicamycin as compared to wild-type animals (PubMed:24715729).
RNAi-mediated knockdown results in larval arrest at 25 degrees
Celsius in an xpn-1 mutant background (PubMed:15649460). Double
knockout with the synthetic multivulva class B protein lin-15A
results in a multiple vulva (Muv) phenotype (PubMed:16624904,
PubMed:26100681). Double knockout with either cdk-4 or cyd-1
rescues the cell cycle progression defect in the single cdk-4 and
cyd-1 mutants (PubMed:11684669, PubMed:25562820). Double knockout
with xnp-1 results in 43% embryonic lethality (PubMed:15328017).
Surviving animals develop slowly, are small, sterile and display
male and female gonad developmental defects characterized by
shorter gonadal arms, fewer germ cells, an everted vulva
phenotype, and failed formation of sheath and spermathecal cells
(PubMed:15328017). Double knockout with spr-1 or zfp-2 results in
defects in growth, vulval morphogenesis, somatic gonad development
and fertility (PubMed:17417969, PubMed:17070797). Double knockout
with the programmed cell death regulator mcd-1 results in 100%
lethality during the L1 stage of larval development
(PubMed:17237514). Programmed cell death defect in a ced-3 n2427
mutant background (PubMed:17237514). Knockout with RNAi-mediated
knockdown of psa-1, ham-3, swsn-2.2, swsn-3 or swsn-6 (components
of the SWI/SNF complex) results in larval arrest during larval
development (PubMed:15280233). Knockout with RNAi-mediated
knockdown of pha-1 (developmental protein), snfc-5 or swsn-8
(additional SWI/SNF complex components) results in sterility
and/or a protruding vulva phenotype (PubMed:15196946,
PubMed:15280233). Double knockout with slr-2 results in early
larval arrest due to mis-regulation of intestinal specific gene
expression, which results in starvation-induced growth arrest
(PubMed:18437219, PubMed:22542970). {ECO:0000269|PubMed:11684669,
ECO:0000269|PubMed:15196946, ECO:0000269|PubMed:15280233,
ECO:0000269|PubMed:15328017, ECO:0000269|PubMed:15649460,
ECO:0000269|PubMed:16507136, ECO:0000269|PubMed:16624904,
ECO:0000269|PubMed:17070797, ECO:0000269|PubMed:17237514,
ECO:0000269|PubMed:17417969, ECO:0000269|PubMed:17466069,
ECO:0000269|PubMed:18437219, ECO:0000269|PubMed:22542970,
ECO:0000269|PubMed:24715729, ECO:0000269|PubMed:25562820,
ECO:0000269|PubMed:26100681}.
-!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
{ECO:0000305}.
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EMBL; AF116529; AAD05570.1; -; mRNA.
EMBL; BX284601; CCD61908.1; -; Genomic_DNA.
PIR; T34024; T34024.
RefSeq; NP_491686.1; NM_059285.3.
UniGene; Cel.5952; -.
IntAct; G5EDT1; 9.
STRING; 6239.C32F10.2; -.
iPTMnet; G5EDT1; -.
EPD; G5EDT1; -.
EnsemblMetazoa; C32F10.2; C32F10.2; WBGene00003020.
GeneID; 172249; -.
KEGG; cel:CELE_C32F10.2; -.
CTD; 172249; -.
WormBase; C32F10.2; CE24823; WBGene00003020; lin-35.
eggNOG; KOG1010; Eukaryota.
eggNOG; ENOG410XQF7; LUCA.
GeneTree; ENSGT00530000063235; -.
KO; K04681; -.
OMA; FCFCVEL; -.
OrthoDB; EOG091G0398; -.
Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
Reactome; R-CEL-69231; Cyclin D associated events in G1.
PRO; PR:G5EDT1; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00003020; -.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:WormBase.
GO; GO:0008406; P:gonad development; IGI:UniProtKB.
GO; GO:0071850; P:mitotic cell cycle arrest; IGI:WormBase.
GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IGI:UniProtKB.
GO; GO:0032876; P:negative regulation of DNA endoreduplication; IGI:UniProtKB.
GO; GO:0016479; P:negative regulation of transcription from RNA polymerase I promoter; ISS:WormBase.
GO; GO:0040027; P:negative regulation of vulval development; IGI:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:WormBase.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IGI:UniProtKB.
GO; GO:0051302; P:regulation of cell division; IGI:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.472.10; -; 3.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR002720; RB_A.
InterPro; IPR002719; RB_B.
InterPro; IPR028309; RB_fam.
InterPro; IPR024599; RB_N.
PANTHER; PTHR13742; PTHR13742; 1.
Pfam; PF11934; DUF3452; 1.
Pfam; PF01858; RB_A; 1.
Pfam; PF01857; RB_B; 1.
SMART; SM01367; DUF3452; 1.
SMART; SM01368; RB_A; 1.
SUPFAM; SSF47954; SSF47954; 3.
1: Evidence at protein level;
Cell cycle; Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 961 Retinoblastoma-like protein homolog lin-
35. {ECO:0000305}.
/FTId=PRO_0000441023.
MOD_RES 714 714 Phosphoserine; by CDK4.
{ECO:0000269|PubMed:25562820}.
MOD_RES 719 719 Phosphothreonine; by CDK4.
{ECO:0000269|PubMed:25562820}.
SEQUENCE 961 AA; 110903 MW; 712475505E527DF1 CRC64;
MPKRAADEPG TSTTDPFHEQ SPFDAVLAGT ETTDTICEEP PAKRIDLDIK QEFNGGVQSG
GLIKNESELT QMTIKQETEG NINEARREEE DEEQDEDSRT SMPPALGEDD DYEEDDADSF
IDKTNTPPPS QSFLEGCRAA NLPNDIVTGA WETYNHAVQR VSLEGSESAW QLSAIYYYLL
SKGIKRRGKT IRILIQPFPV SILTIANSFD ISVAEMLDKT ARFVEIIHSR KIRRYQEYIR
RIQEGLAVSC VIFKKFCRIF CKIFEEIKVG SENCPSSHEL FTVLWTSFLV MKSRMTVDDL
ISNYQLLFSI LDQVYTEMCS MKEGIVHHLN QKFVEDLLEN DCTIIRALCT QFGGSVLDAR
HFSDHTFKKM EKTGIPSTWN FQEFRDLIMN VPKTAYENYL LQRGSIDERI FIPSVEDFSK
IFQSPDTYSV ADILKVSYSG RRFRDAEFLT KISNNHCLEK LALGGKVASE KLVTQSKEQP
RVPCVEYNLE LGNYPDDLES NNQSLYNRLT KIIGSWKLEN SKLEEVCGTM SDSPMATILL
KSDEMTNKFE RTLSAELGET INENIPKYHY NVRKELELVF LIFMEKIIVA ELKKKVREED
LLNVIRREEF LDSVFCFCVE LILVSNGYDR PFPWSAELCG VHPFMFHKVI DLMITHEKQL
SRQMVQHFSR IEETVIEYFS WKSDSPLWPM VVRCPFAHFQ EFGEDWADKL NSYSPIKFTP
IKKPDDLRDE LGRPIVPQNQ TSRTLRIFLK RTYFTAARRL QDLTDRVSMG ARAKSQCWSL
FDYLLRNDTL IFMDRHLDQI LLCCVFVIMK INESSMLFTE IMAQYRRQSA NSLLVYRSVT
VFQEQLNPEN PQAVNTKETI LERLEGPQKE KTTVDIIKYY NIEFRDRIKY IIGQIDSASD
EDLMEMPVAT ESGLMPVRVY LTHKLSIQTL PKTKHGESKQ ERAIANLEKS GITIAMERSG
D


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