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RB1-inducible coiled-coil protein 1 (Coiled-coil-forming protein 1) (FAK family kinase-interacting protein of 200 kDa) (FIP200) (LaXp180)

 RBCC1_MOUSE             Reviewed;        1588 AA.
Q9ESK9; E9QLQ2; Q3TXX2; Q61384; Q8BRY9; Q9JK14;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
12-SEP-2018, entry version 130.
RecName: Full=RB1-inducible coiled-coil protein 1;
AltName: Full=Coiled-coil-forming protein 1;
AltName: Full=FAK family kinase-interacting protein of 200 kDa;
Short=FIP200;
AltName: Full=LaXp180;
Name=Rb1cc1; Synonyms=Cc1, Kiaa0203;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
COLOCALIZATION WITH RB1, AND FUNCTION.
STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
PubMed=12095676; DOI=10.1016/S0378-1119(02)00585-1;
Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A.,
Saeki Y., Okabe H.;
"Isolation, characterization and mapping of the mouse and human RB1CC1
genes.";
Gene 291:29-34(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-1304 AND 1374-1588.
STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1081-1222.
PubMed=7724523; DOI=10.1073/pnas.92.8.3100;
Maucuer A., Camonis J.H., Sobel A.;
"Stathmin interaction with a putative kinase and coiled-coil-forming
protein domains.";
Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1359-1588.
STRAIN=CD-1;
PubMed=11207567; DOI=10.1046/j.1462-5822.2000.00034.x;
Pfeuffer T., Goebel W., Laubinger J., Bachmann M., Kuhn M.;
"LaXp180, a mammalian ActA-binding protein, identified with the yeast
two-hybrid system co-localizes with intracellular Listeria
monocytogenes.";
Cell. Microbiol. 2:101-114(2000).
[6]
DEVELOPMENTAL STAGE.
PubMed=15375585;
Bamba N., Chano T., Taga T., Ohta S., Takeuchi Y., Okabe H.;
"Expression and regulation of RB1CC1 in developing murine and human
tissues.";
Int. J. Mol. Med. 14:583-587(2004).
[7]
FUNCTION.
PubMed=15968549; DOI=10.1007/s00428-004-1183-1;
Watanabe R., Chano T., Inoue H., Isono T., Koiwai O., Okabe H.;
"Rb1cc1 is critical for myoblast differentiation through Rb1
regulation.";
Virchows Arch. 447:643-648(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
FUNCTION, INTERACTION WITH ULK1 AND ATG13, AND SUBCELLULAR LOCATION.
PubMed=19258318; DOI=10.1074/jbc.M900573200;
Ganley I.G., Lam du H., Wang J., Ding X., Chen S., Jiang X.;
"ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential
for autophagy.";
J. Biol. Chem. 284:12297-12305(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; THR-238; SER-243;
SER-261; SER-623; SER-646; SER-649; SER-652 AND SER-1087, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION.
PubMed=19940130; DOI=10.1074/jbc.M109.072389;
Liang C.C., Wang C., Peng X., Gan B., Guan J.L.;
"Neural-specific deletion of FIP200 leads to cerebellar degeneration
caused by increased neuronal death and axon degeneration.";
J. Biol. Chem. 285:3499-3509(2010).
[13]
FUNCTION.
PubMed=21088496; DOI=10.4161/auto.7.2.14125;
Liu F., Guan J.L.;
"FIP200, an essential component of mammalian autophagy is
indispensible for fetal hematopoiesis.";
Autophagy 7:229-230(2011).
[14]
FUNCTION, AND INTERACTION WITH RNF111; SKI AND SMAD7.
PubMed=21795712; DOI=10.1074/jbc.M111.227561;
Koinuma D., Shinozaki M., Nagano Y., Ikushima H., Horiguchi K.,
Goto K., Chano T., Saitoh M., Imamura T., Miyazono K., Miyazawa K.;
"RB1CC1 protein positively regulates transforming growth factor-beta
signaling through the modulation of Arkadia E3 ubiquitin ligase
activity.";
J. Biol. Chem. 286:32502-32512(2011).
[15]
FUNCTION.
PubMed=21525242; DOI=10.1091/mbc.E10-11-0893;
Kageyama S., Omori H., Saitoh T., Sone T., Guan J.L., Akira S.,
Imamoto F., Noda T., Yoshimori T.;
"The LC3 recruitment mechanism is separate from Atg9L1-dependent
membrane formation in the autophagic response against Salmonella.";
Mol. Biol. Cell 22:2290-2300(2011).
[16]
FUNCTION.
PubMed=21807966; DOI=10.1158/1541-7786.MCR-11-0098;
Bae H., Guan J.L.;
"Suppression of autophagy by FIP200 deletion impairs DNA damage repair
and increases cell death upon treatments with anticancer agents.";
Mol. Cancer Res. 9:1232-1241(2011).
[17]
FUNCTION.
PubMed=23285000; DOI=10.1371/journal.pone.0052347;
Chen X., Li M., Chen D., Gao W., Guan J.L., Komatsu M., Yin X.M.;
"Autophagy induced by calcium phosphate precipitates involves
endoplasmic reticulum membranes in autophagosome biogenesis.";
PLoS ONE 7:E52347-E52347(2012).
[18]
FUNCTION, AND INTERACTION WITH ATG16L1.
PubMed=23392225; DOI=10.1038/embor.2013.6;
Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T.,
Akira S., Virgin H.W., Mizushima N.;
"FIP200 regulates targeting of Atg16L1 to the isolation membrane.";
EMBO Rep. 14:284-291(2013).
[19]
FUNCTION, AND INTERACTION WITH ATG16L1.
PubMed=23262492; DOI=10.1038/nsmb.2475;
Gammoh N., Florey O., Overholtzer M., Jiang X.;
"Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-
dependent and -independent autophagy.";
Nat. Struct. Mol. Biol. 20:144-149(2013).
-!- FUNCTION: Involved in autophagy (PubMed:23262492,
PubMed:19258318). Regulates early events but also late events of
autophagosome formation through direct interaction with Atg16L1
(PubMed:23392225, PubMed:23285000, PubMed:19258318). Required for
the formation of the autophagosome-like double-membrane structure
that surrounds the Salmonella-containing vacuole (SCV) during
S.typhimurium infection and subsequent xenophagy
(PubMed:21525242). Involved in repair of DNA damage caused by
ionizing radiation, which subsequently improves cell survival by
decreasing apoptosis (PubMed:21807966). Inhibits PTK2/FAK1 and
PTK2B/PYK2 kinase activity, affecting their downstream signaling
pathways (By similarity). Plays a role as a modulator of TGF-beta-
signaling by restricting substrate specificity of RNF111
(PubMed:21795712). Functions as a DNA-binding transcription factor
(PubMed:12095676). Is a potent regulator of the RB1 pathway
through induction of RB1 expression (PubMed:15968549). Plays a
crucial role in muscular differentiation (PubMed:15968549). Plays
an indispensable role in fetal hematopoiesis and in the regulation
of neuronal homeostasis (PubMed:19940130, PubMed:21088496).
{ECO:0000250|UniProtKB:Q8TDY2, ECO:0000269|PubMed:12095676,
ECO:0000269|PubMed:15968549, ECO:0000269|PubMed:19258318,
ECO:0000269|PubMed:19940130, ECO:0000269|PubMed:21088496,
ECO:0000269|PubMed:21525242, ECO:0000269|PubMed:21795712,
ECO:0000269|PubMed:21807966, ECO:0000269|PubMed:23262492,
ECO:0000269|PubMed:23285000, ECO:0000269|PubMed:23392225}.
-!- SUBUNIT: Part of a complex containing ATG13/KIAA0652, ULK1 and
RB1CC1 (PubMed:19258318). This complex associates with ATG101 (By
similarity). Interacts with PTK2/FAK1 and PTK2B/PYK2 (By
similarity). Interacts with GABARAP and GABARAPL1 (By similarity).
Interacts with ATG16L1; the interaction is required for ULK1
complex-dependent autophagy (PubMed:23392225, PubMed:23262492).
Interacts with RNF111, SKI and SMAD7 (PubMed:21795712). Interacts
with COP1 in the cytoplasm of proliferating cells in response to
UV stimulation (By similarity). Interacts with TP53 (By
similarity). Interacts with C9orf72 (By similarity).
{ECO:0000250|UniProtKB:Q8TDY2, ECO:0000269|PubMed:19258318,
ECO:0000269|PubMed:21795712, ECO:0000269|PubMed:23262492,
ECO:0000269|PubMed:23392225}.
-!- INTERACTION:
Q8C0J2:Atg16l1; NbExp=4; IntAct=EBI-647302, EBI-769195;
Q8C0J2-3:Atg16l1; NbExp=3; IntAct=EBI-647302, EBI-16029274;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12095676}.
Cytoplasm, cytosol {ECO:0000269|PubMed:19258318}. Cytoplasm
{ECO:0000250|UniProtKB:Q8TDY2}. Preautophagosomal structure
{ECO:0000269|PubMed:19258318}. Note=Under starvation conditions,
is localized to puncate structures primarily representing the
isolation membrane that sequesters a portion of the cytoplasm
resulting in the formation of an autophagosome.
{ECO:0000269|PubMed:19258318}.
-!- TISSUE SPECIFICITY: Expressed abundantly in heart and testis, and
moderately in kidney, liver and skeletal muscles. Very low
expression levels in lung and spleen. Colocalizes with RB1 in
various tissues. {ECO:0000269|PubMed:12095676}.
-!- DEVELOPMENTAL STAGE: Abundantly expressed from an early stage of
the embryo throughout development. Ubiquitously expressed,
especially in the musculoskeletal system, heart and neural
tissues. {ECO:0000269|PubMed:15375585}.
-!- SEQUENCE CAUTION:
Sequence=BAC30793.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB050017; BAB16846.2; -; mRNA.
EMBL; AB070619; BAB85610.1; -; mRNA.
EMBL; AC102781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC139064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK041038; BAC30793.1; ALT_INIT; mRNA.
EMBL; AK159066; BAE34792.1; -; mRNA.
EMBL; X82318; CAA57761.1; -; mRNA.
EMBL; AJ242720; CAB92238.1; -; mRNA.
CCDS; CCDS35507.1; -.
PIR; I48282; I48282.
RefSeq; NP_033956.2; NM_009826.4.
UniGene; Mm.293811; -.
SMR; Q9ESK9; -.
BioGrid; 198540; 4.
ComplexPortal; CPX-380; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex.
DIP; DIP-49679N; -.
IntAct; Q9ESK9; 6.
MINT; Q9ESK9; -.
STRING; 10090.ENSMUSP00000027040; -.
iPTMnet; Q9ESK9; -.
PhosphoSitePlus; Q9ESK9; -.
EPD; Q9ESK9; -.
MaxQB; Q9ESK9; -.
PaxDb; Q9ESK9; -.
PeptideAtlas; Q9ESK9; -.
PRIDE; Q9ESK9; -.
Ensembl; ENSMUST00000027040; ENSMUSP00000027040; ENSMUSG00000025907.
GeneID; 12421; -.
KEGG; mmu:12421; -.
UCSC; uc007afr.2; mouse.
CTD; 9821; -.
MGI; MGI:1341850; Rb1cc1.
eggNOG; KOG4572; Eukaryota.
eggNOG; ENOG410XSY4; LUCA.
GeneTree; ENSGT00390000015871; -.
HOGENOM; HOG000154076; -.
HOVERGEN; HBG091209; -.
InParanoid; Q9ESK9; -.
KO; K17589; -.
OMA; AECRQTI; -.
OrthoDB; EOG091G0PNM; -.
TreeFam; TF323750; -.
Reactome; R-MMU-1632852; Macroautophagy.
ChiTaRS; Rb1cc1; mouse.
PRO; PR:Q9ESK9; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000025907; Expressed in 274 organ(s), highest expression level in testis.
CleanEx; MM_RB1CC1; -.
ExpressionAtlas; Q9ESK9; baseline and differential.
Genevisible; Q9ESK9; MM.
GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0032947; F:protein-containing complex scaffold activity; IBA:GO_Central.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:GO_Central.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0061723; P:glycophagy; IBA:GO_Central.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0045793; P:positive regulation of cell size; IMP:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IGI:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019460; Atg11_C.
Pfam; PF10377; ATG11; 1.
1: Evidence at protein level;
Autophagy; Cell cycle; Coiled coil; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Tumor suppressor.
CHAIN 1 1588 RB1-inducible coiled-coil protein 1.
/FTId=PRO_0000097184.
COILED 858 1393 {ECO:0000255}.
COILED 1440 1479 {ECO:0000255}.
MOTIF 565 568 Nuclear localization signal.
COMPBIAS 662 665 Poly-Thr.
MOD_RES 222 222 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TDY2}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TDY2}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TDY2}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TDY2}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 646 646 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1087 1087 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1366 1366 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TDY2}.
MOD_RES 1478 1478 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TDY2}.
CONFLICT 809 809 S -> T (in Ref. 1; BAB16846/BAB85610).
{ECO:0000305}.
CONFLICT 981 981 Q -> E (in Ref. 1; BAB16846/BAB85610).
{ECO:0000305}.
CONFLICT 1222 1222 D -> A (in Ref. 4; CAA57761).
{ECO:0000305}.
CONFLICT 1450 1451 KQ -> NE (in Ref. 5; CAB92238).
{ECO:0000305}.
CONFLICT 1537 1539 Missing (in Ref. 5; CAB92238).
{ECO:0000305}.
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


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