RBCC1_MOUSE
ID RBCC1_MOUSE Reviewed; 1588 AA.
AC Q9ESK9; E9QLQ2; Q3TXX2; Q61384; Q8BRY9; Q9JK14;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=RB1-inducible coiled-coil protein 1 {ECO:0000305};
DE AltName: Full=Coiled-coil-forming protein 1;
DE AltName: Full=FAK family kinase-interacting protein of 200 kDa;
DE Short=FIP200;
DE AltName: Full=LaXp180;
GN Name=Rb1cc1 {ECO:0000312|MGI:MGI:1341850}; Synonyms=Cc1, Kiaa0203;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP COLOCALIZATION WITH RB1, AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX PubMed=12095676; DOI=10.1016/s0378-1119(02)00585-1;
RA Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A., Saeki Y.,
RA Okabe H.;
RT "Isolation, characterization and mapping of the mouse and human RB1CC1
RT genes.";
RL Gene 291:29-34(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-1304 AND 1374-1588.
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1081-1222.
RX PubMed=7724523; DOI=10.1073/pnas.92.8.3100;
RA Maucuer A., Camonis J.H., Sobel A.;
RT "Stathmin interaction with a putative kinase and coiled-coil-forming
RT protein domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1359-1588.
RC STRAIN=CD-1;
RX PubMed=11207567; DOI=10.1046/j.1462-5822.2000.00034.x;
RA Pfeuffer T., Goebel W., Laubinger J., Bachmann M., Kuhn M.;
RT "LaXp180, a mammalian ActA-binding protein, identified with the yeast two-
RT hybrid system co-localizes with intracellular Listeria monocytogenes.";
RL Cell. Microbiol. 2:101-114(2000).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15375585;
RA Bamba N., Chano T., Taga T., Ohta S., Takeuchi Y., Okabe H.;
RT "Expression and regulation of RB1CC1 in developing murine and human
RT tissues.";
RL Int. J. Mol. Med. 14:583-587(2004).
RN [7]
RP FUNCTION.
RX PubMed=15968549; DOI=10.1007/s00428-004-1183-1;
RA Watanabe R., Chano T., Inoue H., Isono T., Koiwai O., Okabe H.;
RT "Rb1cc1 is critical for myoblast differentiation through Rb1 regulation.";
RL Virchows Arch. 447:643-648(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP FUNCTION, INTERACTION WITH ULK1 AND ATG13, AND SUBCELLULAR LOCATION.
RX PubMed=19258318; DOI=10.1074/jbc.m900573200;
RA Ganley I.G., Lam du H., Wang J., Ding X., Chen S., Jiang X.;
RT "ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for
RT autophagy.";
RL J. Biol. Chem. 284:12297-12305(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; THR-238; SER-243;
RP SER-261; SER-623; SER-646; SER-649; SER-652 AND SER-1087, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION.
RX PubMed=19940130; DOI=10.1074/jbc.m109.072389;
RA Liang C.C., Wang C., Peng X., Gan B., Guan J.L.;
RT "Neural-specific deletion of FIP200 leads to cerebellar degeneration caused
RT by increased neuronal death and axon degeneration.";
RL J. Biol. Chem. 285:3499-3509(2010).
RN [13]
RP FUNCTION.
RX PubMed=21088496; DOI=10.4161/auto.7.2.14125;
RA Liu F., Guan J.L.;
RT "FIP200, an essential component of mammalian autophagy is indispensible for
RT fetal hematopoiesis.";
RL Autophagy 7:229-230(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH RNF111; SKI AND SMAD7.
RX PubMed=21795712; DOI=10.1074/jbc.m111.227561;
RA Koinuma D., Shinozaki M., Nagano Y., Ikushima H., Horiguchi K., Goto K.,
RA Chano T., Saitoh M., Imamura T., Miyazono K., Miyazawa K.;
RT "RB1CC1 protein positively regulates transforming growth factor-beta
RT signaling through the modulation of Arkadia E3 ubiquitin ligase activity.";
RL J. Biol. Chem. 286:32502-32512(2011).
RN [15]
RP FUNCTION.
RX PubMed=21525242; DOI=10.1091/mbc.e10-11-0893;
RA Kageyama S., Omori H., Saitoh T., Sone T., Guan J.L., Akira S., Imamoto F.,
RA Noda T., Yoshimori T.;
RT "The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane
RT formation in the autophagic response against Salmonella.";
RL Mol. Biol. Cell 22:2290-2300(2011).
RN [16]
RP FUNCTION.
RX PubMed=21807966; DOI=10.1158/1541-7786.mcr-11-0098;
RA Bae H., Guan J.L.;
RT "Suppression of autophagy by FIP200 deletion impairs DNA damage repair and
RT increases cell death upon treatments with anticancer agents.";
RL Mol. Cancer Res. 9:1232-1241(2011).
RN [17]
RP FUNCTION.
RX PubMed=23285000; DOI=10.1371/journal.pone.0052347;
RA Chen X., Li M., Chen D., Gao W., Guan J.L., Komatsu M., Yin X.M.;
RT "Autophagy induced by calcium phosphate precipitates involves endoplasmic
RT reticulum membranes in autophagosome biogenesis.";
RL PLoS ONE 7:E52347-E52347(2012).
RN [18]
RP FUNCTION, AND INTERACTION WITH ATG16L1.
RX PubMed=23392225; DOI=10.1038/embor.2013.6;
RA Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T., Akira S.,
RA Virgin H.W., Mizushima N.;
RT "FIP200 regulates targeting of Atg16L1 to the isolation membrane.";
RL EMBO Rep. 14:284-291(2013).
RN [19]
RP FUNCTION, AND INTERACTION WITH ATG16L1.
RX PubMed=23262492; DOI=10.1038/nsmb.2475;
RA Gammoh N., Florey O., Overholtzer M., Jiang X.;
RT "Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-
RT dependent and -independent autophagy.";
RL Nat. Struct. Mol. Biol. 20:144-149(2013).
RN [20]
RP INTERACTION WITH WDR45B.
RX PubMed=28561066; DOI=10.1038/ncomms15637;
RA Bakula D., Mueller A.J., Zuleger T., Takacs Z., Franz-Wachtel M.,
RA Thost A.K., Brigger D., Tschan M.P., Frickey T., Robenek H., Macek B.,
RA Proikas-Cezanne T.;
RT "WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling
RT circuits in the control of autophagy.";
RL Nat. Commun. 8:15637-15637(2017).
CC -!- FUNCTION: Involved in autophagy (PubMed:23262492, PubMed:19258318).
CC Regulates early events but also late events of autophagosome formation
CC through direct interaction with Atg16L1 (PubMed:23392225,
CC PubMed:23285000, PubMed:19258318). Required for the formation of the
CC autophagosome-like double-membrane structure that surrounds the
CC Salmonella-containing vacuole (SCV) during S.typhimurium infection and
CC subsequent xenophagy (PubMed:21525242). Involved in repair of DNA
CC damage caused by ionizing radiation, which subsequently improves cell
CC survival by decreasing apoptosis (PubMed:21807966). Inhibits PTK2/FAK1
CC and PTK2B/PYK2 kinase activity, affecting their downstream signaling
CC pathways (By similarity). Plays a role as a modulator of TGF-beta-
CC signaling by restricting substrate specificity of RNF111
CC (PubMed:21795712). Functions as a DNA-binding transcription factor
CC (PubMed:12095676). Is a potent regulator of the RB1 pathway through
CC induction of RB1 expression (PubMed:15968549). Plays a crucial role in
CC muscular differentiation (PubMed:15968549). Plays an indispensable role
CC in fetal hematopoiesis and in the regulation of neuronal homeostasis
CC (PubMed:19940130, PubMed:21088496). {ECO:0000250|UniProtKB:Q8TDY2,
CC ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:15968549,
CC ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:19940130,
CC ECO:0000269|PubMed:21088496, ECO:0000269|PubMed:21525242,
CC ECO:0000269|PubMed:21795712, ECO:0000269|PubMed:21807966,
CC ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23285000,
CC ECO:0000269|PubMed:23392225}.
CC -!- SUBUNIT: Part of a complex containing ATG13/KIAA0652, ULK1 and RB1CC1
CC (PubMed:19258318). This complex associates with ATG101 (By similarity).
CC Interacts with PTK2/FAK1 and PTK2B/PYK2 (By similarity). Interacts with
CC GABARAP and GABARAPL1 (By similarity). Interacts with ATG16L1; the
CC interaction is required for ULK1 complex-dependent autophagy
CC (PubMed:23392225, PubMed:23262492). Interacts with RNF111, SKI and
CC SMAD7 (PubMed:21795712). Interacts with COP1 in the cytoplasm of
CC proliferating cells in response to UV stimulation (By similarity).
CC Interacts with TP53 (By similarity). Interacts with C9orf72 (By
CC similarity). Interacts with WDR45B (PubMed:28561066). Interacts with
CC ATG13; this interaction is increased in the absence of TMEM39A (By
CC similarity). Interacts with WIPI2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TDY2, ECO:0000269|PubMed:19258318,
CC ECO:0000269|PubMed:21795712, ECO:0000269|PubMed:23262492,
CC ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:28561066}.
CC -!- INTERACTION:
CC Q9ESK9; Q8C0J2: Atg16l1; NbExp=4; IntAct=EBI-647302, EBI-769195;
CC Q9ESK9; Q8C0J2-3: Atg16l1; NbExp=3; IntAct=EBI-647302, EBI-16029274;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12095676}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:19258318}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TDY2}. Preautophagosomal structure
CC {ECO:0000269|PubMed:19258318}. Lysosome {ECO:0000250|UniProtKB:Q8TDY2}.
CC Note=Under starvation conditions, is localized to puncate structures
CC primarily representing the isolation membrane that sequesters a portion
CC of the cytoplasm resulting in the formation of an autophagosome.
CC {ECO:0000269|PubMed:19258318}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in heart and testis, and
CC moderately in kidney, liver and skeletal muscles. Very low expression
CC levels in lung and spleen. Colocalizes with RB1 in various tissues.
CC {ECO:0000269|PubMed:12095676}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed from an early stage of the
CC embryo throughout development. Ubiquitously expressed, especially in
CC the musculoskeletal system, heart and neural tissues.
CC {ECO:0000269|PubMed:15375585}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30793.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB050017; BAB16846.2; -; mRNA.
DR EMBL; AB070619; BAB85610.1; -; mRNA.
DR EMBL; AC102781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK041038; BAC30793.1; ALT_INIT; mRNA.
DR EMBL; AK159066; BAE34792.1; -; mRNA.
DR EMBL; X82318; CAA57761.1; -; mRNA.
DR EMBL; AJ242720; CAB92238.1; -; mRNA.
DR CCDS; CCDS35507.1; -.
DR PIR; I48282; I48282.
DR RefSeq; NP_033956.2; NM_009826.4.
DR AlphaFoldDB; Q9ESK9; -.
DR SMR; Q9ESK9; -.
DR BioGRID; 198540; 14.
DR ComplexPortal; CPX-380; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex.
DR DIP; DIP-49679N; -.
DR IntAct; Q9ESK9; 7.
DR MINT; Q9ESK9; -.
DR STRING; 10090.ENSMUSP00000027040; -.
DR iPTMnet; Q9ESK9; -.
DR PhosphoSitePlus; Q9ESK9; -.
DR EPD; Q9ESK9; -.
DR jPOST; Q9ESK9; -.
DR MaxQB; Q9ESK9; -.
DR PaxDb; Q9ESK9; -.
DR PeptideAtlas; Q9ESK9; -.
DR PRIDE; Q9ESK9; -.
DR ProteomicsDB; 253180; -.
DR Antibodypedia; 24432; 331 antibodies from 30 providers.
DR DNASU; 12421; -.
DR Ensembl; ENSMUST00000027040; ENSMUSP00000027040; ENSMUSG00000025907.
DR GeneID; 12421; -.
DR KEGG; mmu:12421; -.
DR UCSC; uc007afr.2; mouse.
DR CTD; 9821; -.
DR MGI; MGI:1341850; Rb1cc1.
DR VEuPathDB; HostDB:ENSMUSG00000025907; -.
DR eggNOG; KOG4572; Eukaryota.
DR GeneTree; ENSGT00390000015871; -.
DR HOGENOM; CLU_003711_0_0_1; -.
DR InParanoid; Q9ESK9; -.
DR OMA; AQDSKVH; -.
DR OrthoDB; 91906at2759; -.
DR PhylomeDB; Q9ESK9; -.
DR TreeFam; TF323750; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 12421; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Rb1cc1; mouse.
DR PRO; PR:Q9ESK9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ESK9; protein.
DR Bgee; ENSMUSG00000025907; Expressed in spermatocyte and 254 other tissues.
DR ExpressionAtlas; Q9ESK9; baseline and differential.
DR Genevisible; Q9ESK9; MM.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IDA:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0061723; P:glycophagy; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ComplexPortal.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:ComplexPortal.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal.
DR GO; GO:0061709; P:reticulophagy; IMP:MGI.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR13222; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cell cycle; Coiled coil; Cytoplasm; Lysosome; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..1588
FT /note="RB1-inducible coiled-coil protein 1"
FT /id="PRO_0000097184"
FT REGION 638..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 858..1393
FT /evidence="ECO:0000255"
FT COILED 1440..1479
FT /evidence="ECO:0000255"
FT MOTIF 565..568
FT /note="Nuclear localization signal"
FT COMPBIAS 638..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDY2"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDY2"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDY2"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDY2"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDY2"
FT MOD_RES 1478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDY2"
FT CONFLICT 809
FT /note="S -> T (in Ref. 1; BAB16846/BAB85610)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="Q -> E (in Ref. 1; BAB16846/BAB85610)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="D -> A (in Ref. 4; CAA57761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1450..1451
FT /note="KQ -> NE (in Ref. 5; CAB92238)"
FT /evidence="ECO:0000305"
FT CONFLICT 1537..1539
FT /note="Missing (in Ref. 5; CAB92238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1588 AA; 182350 MW; 2D14F1434604C0AF CRC64;
MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG ECMAADRRVC
TYSAGTDTNP IFLFNKEMIL CDRAPAIPKA TFSTENDMEI KVEESLMMPA VFHTVASRTQ
LAVEMYDVAK KLCSFCEGLV HDEHLQHQGW AAIMANLEDC SNSYQKLLFK FESIYSDYLQ
SIEDIKLKLT HLGTAVSVMA KIPLLECLTR HSYRECLGRP DSLNEHEGSE KAEMKRSTEL
VLSPDMPRTT NTSLVTSFHK SMEHVAPDPT GTERGKELRE SCQSTVQQEE ASVDAKDSDL
PFFNVSLLDW INVQDRPNDV ESLVRKCFDS MSRLDPKIIQ PFMLECHQTI AKLDNQNMKA
IKGLEDRLYA LDQMIASCSR LVNEQKELAQ GFLANQMRAE NLKDASVLPD LCLSHANQLM
IMLQNHRKLL DIKQKCTTAK QELANNLHVR LKWCCFVMLH ADQDGEKLQA LLRLVIELLE
RVRIVEALST VPQMYCLAVV EVVRRKMFIK HYREWAGALV KDGKQLYEAE KSKRESFGKL
FRKSFLRNRL FKGLDSWPSS FCTQKPRKFD CELPDISLKD LQFLQSFCPS EVQPFLRVPL
LCDFEPLHQH VLALHNLVKA AQSLDEMSQT ITDLLNEQKV STSQASPQSA ASPRIESTTG
ITTTTSPKTP PPLTVQDTLC PAVCPLEELS PDSIDAHTFD FETISHPNTE QPVHQASIDL
DSLAESPESD FMSAVNEFVI EENLSSPNPI SDPQSPEMMV ESLYSSVINA IDSRRMQDTS
TRGNEGFGDR AALHVQLEKC RAAAQDSHSS IQTIKDDLCH FRTFVQKEQC DLANYLKCTA
VEIRNIIEKV KCSLEITLKE KHQQELQSLK IEYECKLDAL VKDSEENVNK ILKLKENLVS
LEEALQNKDN EFTSIKHEKD AIVCVQQEKD QKLLEMEKIM HTQHCEIKEL KQSREMALED
LKKLHDEKIE SLRAEFQCLE QNHLKELEDT LHIRHTQEFE KVMTDHNMSL EKLKKENQQR
IDQMLESHAS TIQEKEQQLQ ELKLKVSDLS DMRCKLEVEL ALKEAETDEI KILLEESRTQ
QKEMLKSLLE QETENLRTEI SKLNQKIHDN NESYQVGLSE LRALMTIEKD QCISELISRH
EEESNILKAE LDNVTSLHRQ AYEIEKKLKE QIVELQTRLN SELSALEKQK DEKITQQEEK
YEALIQNLEK DKERLVKNHE QDKEHLIQEL NFEKNKAVQT ALDEFKVERE LVEKELLEKV
KHLENQIAKT PAFESAREDS SSLVAELQEK LQEEKAKFLE QLEEQEKRKN EEMQNVRTSL
IAEQQTNFNT VLTREKMRKE NIINDLSDKL KSTMQQQERD KDLIESLSED RARLLEEKKQ
LEEEVSKLRT SSFLSSAPVA AAPELYGACA PELPGEPERS VMETADEGRL DSAMETSMMS
VQENMLSEEK QRIMLLERTL QLKEEENKRL NQRLMSQSLS SVSSRHSEKI AIRDFQVGDL
VLIILDERHD NYVLFTVSPT LYFLHSESLP ALDLKPGEGA SGASRRPWVL GKVMEKEYCQ
AKKAQNRFKV PLGTKFYRVK AVSWNKKV
