MYCB2_MOUSE
ID MYCB2_MOUSE Reviewed; 4749 AA.
AC Q7TPH6; E9PUJ6; Q6PCM8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=E3 ubiquitin-protein ligase MYCBP2 {ECO:0000305};
DE EC=2.3.2.33 {ECO:0000250|UniProtKB:O75592};
DE AltName: Full=Myc-binding protein 2 {ECO:0000305};
DE AltName: Full=Pam/highwire/rpm-1 protein {ECO:0000303|PubMed:14729956};
DE AltName: Full=Protein Magellan {ECO:0000303|PubMed:18031680};
DE AltName: Full=Protein associated with Myc {ECO:0000303|PubMed:14729956};
GN Name=Mycbp2 {ECO:0000312|MGI:MGI:2179432};
GN Synonyms=Pam {ECO:0000303|PubMed:14729956},
GN Phr1 {ECO:0000303|PubMed:14729956};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-4749 (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP88591.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:14729956};
RX PubMed=14729956; DOI=10.1128/mcb.24.3.1096-1105.2004;
RA Burgess R.W., Peterson K.A., Johnson M.J., Roix J.J., Welsh I.C.,
RA O'Brien T.P.;
RT "Evidence for a conserved function in synapse formation reveals Phr1 as a
RT candidate gene for respiratory failure in newborn mice.";
RL Mol. Cell. Biol. 24:1096-1105(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2365-2390 AND 2904-2913, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3288-4749 (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH59257.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH59257.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH CPNE1 AND CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17901218; DOI=10.1101/gad.1592107;
RA Bloom A.J., Miller B.R., Sanes J.R., DiAntonio A.;
RT "The requirement for Phr1 in CNS axon tract formation reveals the
RT corticostriatal boundary as a choice point for cortical axons.";
RL Genes Dev. 21:2593-2606(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18031680; DOI=10.1016/j.neuron.2007.09.009;
RA Lewcock J.W., Genoud N., Lettieri K., Pfaff S.L.;
RT "The ubiquitin ligase Phr1 regulates axon outgrowth through modulation of
RT microtubule dynamics.";
RL Neuron 56:604-620(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3550, AND IDENTIFICATION BY
RP 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 INTERACTION WITH FBXO45.
RX PubMed=19398581; DOI=10.1128/mcb.00364-09;
RA Saiga T., Fukuda T., Matsumoto M., Tada H., Okano H.J., Okano H.,
RA Nakayama K.I.;
RT "Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal
RT development.";
RL Mol. Cell. Biol. 29:3529-3543(2009).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19371781; DOI=10.1016/j.mcn.2009.04.001;
RA Culican S.M., Bloom A.J., Weiner J.A., DiAntonio A.;
RT "Phr1 regulates retinogeniculate targeting independent of activity and
RT ephrin-A signalling.";
RL Mol. Cell. Neurosci. 41:304-312(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-183;
RP SER-2941; SER-2992 AND THR-3992, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [13]
RP FUNCTION.
RX PubMed=20534529; DOI=10.1073/pnas.1000438107;
RA Yin L., Joshi S., Wu N., Tong X., Lazar M.A.;
RT "E3 ligases Arf-bp1 and Pam mediate lithium-stimulated degradation of the
RT circadian heme receptor Rev-erb alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11614-11619(2010).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21098484; DOI=10.1074/jbc.m110.154765;
RA Holland S., Coste O., Zhang D.D., Pierre S.C., Geisslinger G., Scholich K.;
RT "The ubiquitin ligase MYCBP2 regulates transient receptor potential
RT vanilloid receptor 1 (TRPV1) internalization through inhibition of p38 MAPK
RT signaling.";
RL J. Biol. Chem. 286:3671-3680(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21324225; DOI=10.1017/s0952523810000386;
RA Vo B.Q., Bloom A.J., Culican S.M.;
RT "Phr1 is required for proper retinocollicular targeting of nasal-dorsal
RT retinal ganglion cells.";
RL Vis. Neurosci. 28:175-181(2011).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23665224; DOI=10.1016/j.celrep.2013.04.013;
RA Babetto E., Beirowski B., Russler E.V., Milbrandt J., DiAntonio A.;
RT "The Phr1 ubiquitin ligase promotes injury-induced axon self-destruction.";
RL Cell Rep. 3:1422-1429(2013).
RN [17]
RP FUNCTION.
RX PubMed=23525682; DOI=10.1007/s00429-013-0540-8;
RA James G., Key B., Beverdam A.;
RT "The E3 ubiquitin ligase Mycbp2 genetically interacts with Robo2 to
RT modulate axon guidance in the mouse olfactory system.";
RL Brain Struct. Funct. 219:861-874(2014).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAN AND RANGAP1, AND
RP MUTAGENESIS OF 950-HIS-HIS-951.
RX PubMed=26304119; DOI=10.1074/jbc.m115.646901;
RA Doerr A., Pierre S., Zhang D.D., Henke M., Holland S., Scholich K.;
RT "MYCBP2 is a guanosine exchange factor for Ran protein and determines its
RT localization in neurons of dorsal root ganglia.";
RL J. Biol. Chem. 290:25620-25635(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 1229-1390, X-RAY CRYSTALLOGRAPHY
RP (2.25 ANGSTROMS) OF 1723-1883, DOMAIN PHR, AND DISULFIDE BOND.
RX PubMed=20156452; DOI=10.1016/j.jmb.2010.02.017;
RA Sampathkumar P., Ozyurt S.A., Miller S.A., Bain K.T., Rutter M.E.,
RA Gheyi T., Abrams B., Wang Y., Atwell S., Luz J.G., Thompson D.A.,
RA Wasserman S.R., Emtage J.S., Park E.C., Rongo C., Jin Y., Klemke R.L.,
RA Sauder J.M., Burley S.K.;
RT "Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the
RT loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-
RT 1.";
RL J. Mol. Biol. 397:883-892(2010).
CC -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically
CC mediates ubiquitination of threonine and serine residues on target
CC proteins, instead of ubiquitinating lysine residues (By similarity).
CC Shows esterification activity towards both threonine and serine, with a
CC preference for threonine, and acts via two essential catalytic cysteine
CC residues that relay ubiquitin to its substrate via thioester
CC intermediates (By similarity). Interacts with the E2 enzymes UBE2D1,
CC UBE2D3, UBE2E1 and UBE2L3 (By similarity). Plays a key role in neural
CC development, probably by mediating ubiquitination of threonine residues
CC on target proteins (By similarity). Involved in different processes
CC such as regulation of neurite outgrowth, synaptic growth,
CC synaptogenesis and axon degeneration (PubMed:14729956, PubMed:17901218,
CC PubMed:18031680). Required for the formation of major central nervous
CC system axon tracts (PubMed:17901218, PubMed:18031680). Required for
CC proper axon growth by regulating axon navigation and axon branching:
CC acts by regulating the subcellular location and stability of
CC MAP3K12/DLK (PubMed:18031680). Required for proper localization of
CC retinogeniculate projections but not for eye-specific segregation
CC (PubMed:19371781, PubMed:21324225). Regulates axon guidance in the
CC olfactory system (PubMed:23525682). Involved in Wallerian axon
CC degeneration, an evolutionarily conserved process that drives the loss
CC of damaged axons: acts by promoting destabilization of NMNAT2, probably
CC via ubiquitination of NMNAT2 (PubMed:23665224). Catalyzes
CC ubiquitination of threonine and/or serine residues on NMNAT2,
CC consequences of threonine and/or serine ubiquitination are however
CC unknown (By similarity). Regulates the internalization of TRPV1 in
CC peripheral sensory neurons (PubMed:21098484). May mediate
CC ubiquitination and subsequent proteasomal degradation of TSC2/tuberin
CC (By similarity). Independently of the E3 ubiquitin-protein ligase
CC activity, also acts as a guanosine exchange factor (GEF) for RAN in
CC neurons of dorsal root ganglia (PubMed:26304119). May function as a
CC facilitator or regulator of transcriptional activation by MYC (By
CC similarity). Acts in concert with HUWE1 to regulate the circadian clock
CC gene expression by promoting the lithium-induced ubiquination and
CC degradation of NR1D1 (PubMed:20534529). {ECO:0000250|UniProtKB:O75592,
CC ECO:0000269|PubMed:14729956, ECO:0000269|PubMed:17901218,
CC ECO:0000269|PubMed:18031680, ECO:0000269|PubMed:19371781,
CC ECO:0000269|PubMed:20534529, ECO:0000269|PubMed:21098484,
CC ECO:0000269|PubMed:21324225, ECO:0000269|PubMed:23525682,
CC ECO:0000269|PubMed:23665224, ECO:0000269|PubMed:26304119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.;
CC EC=2.3.2.33; Evidence={ECO:0000250|UniProtKB:O75592};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O75592}.
CC -!- SUBUNIT: Interacts with MYC (By similarity). Interacts with TSC2
CC (tuberin) when TSC2 is in complex with TSC1 (hamartin) (By similarity).
CC Interacts with FBXO45 (PubMed:19398581). Interacts with RAE1 (By
CC similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA
CC domain) (PubMed:12522145). Interacts with (sumoylated) RANGAP1;
CC interaction with sumoylated RANGAP1 inhibits E3 ubiquitin-protein
CC ligase activity and promotes MYCBP2 translocation to the nucleus
CC (PubMed:26304119). Interacts with RAN (PubMed:26304119). Interacts with
CC ATP13A2; the interaction inhibits the ubiquitination of TSC2 by MYCBP2
CC (By similarity). Interacts with USP11 (By similarity).
CC {ECO:0000250|UniProtKB:O75592, ECO:0000269|PubMed:12522145,
CC ECO:0000269|PubMed:19398581, ECO:0000269|PubMed:26304119}.
CC -!- INTERACTION:
CC Q7TPH6; Q63633: Slc12a5; Xeno; NbExp=4; IntAct=EBI-1811542, EBI-1811510;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26304119}. Cell
CC projection, axon {ECO:0000269|PubMed:18031680}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18031680}. Note=Localizes to axon shafts and
CC associates with microtubule cytoskeleton (PubMed:18031680).
CC Translocates to the nucleus following interaction with sumoylated
CC RANGAP1 (PubMed:26304119). {ECO:0000269|PubMed:18031680,
CC ECO:0000269|PubMed:26304119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000303|PubMed:14729956};
CC IsoId=Q7TPH6-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q7TPH6-2; Sequence=VSP_014184;
CC -!- TISSUE SPECIFICITY: Expression is mostly restricted to the nervous
CC system, including expression in motor and sensory axons
CC (PubMed:18031680). During postnatal development, expression is
CC particularly strong in the cerebellum, hippocampus and retina
CC (PubMed:14729956). Lower levels of expression are observed throughout
CC the cerebral cortex (PubMed:14729956). {ECO:0000269|PubMed:14729956,
CC ECO:0000269|PubMed:18031680}.
CC -!- DEVELOPMENTAL STAGE: Dynamically expressed in embryonic nervous system
CC from 8.5 dpc through 18.5 dpc (PubMed:14729956, PubMed:18031680). At
CC 10.5 dpc, shortly after the birth of the first motor neurons, highly
CC expressed in the developing motor columns, dorsal root ganglion and
CC newly formed neurons within the dorsal neural tube (PubMed:18031680).
CC As embryos develop to 11.5 dpc, expression levels increase in the
CC dorsal root ganglion and expression in the spinal cord expandes as the
CC number of postmitotic neurons increase (PubMed:18031680). By 12.5 dpc
CC expression is widespread within the spinal cord (PubMed:18031680).
CC {ECO:0000269|PubMed:14729956, ECO:0000269|PubMed:18031680}.
CC -!- DOMAIN: The PHR domains are compact beta-sandwich folds composed of 11
CC antiparallel strands and decorated with conserved apical loops. They
CC are likely to play a structural role and mediate interactions with
CC substrates or partners. {ECO:0000269|PubMed:20156452}.
CC -!- DOMAIN: The tandem cysteine domain region confers threonine specificity
CC and contains the two essential catalytic cysteine residues that relay
CC ubiquitin. It binds four zinc ions in a C5HC7HC2 configuration.
CC {ECO:0000250|UniProtKB:O75592}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:O75592}.
CC -!- DISRUPTION PHENOTYPE: Lethality caused by defects in neuromuscular
CC development (PubMed:17901218). Mice die at birth without taking a
CC breath: phrenic nerves are markedly narrower and contain fewer axons
CC than controls (PubMed:17901218). Mice display incomplete innervation of
CC the diaphragm by the phrenic nerve (PubMed:14729956, PubMed:17901218).
CC Intercostal muscles are completely innervated, but show dysmorphic
CC nerve terminals (PubMed:14729956, PubMed:17901218). Sensory neuron
CC terminals in the diaphragm are abnormal and neuromuscular junctions
CC show excessive sprouting of nerve terminals, consistent with inadequate
CC presynaptic stimulation of the muscle (PubMed:14729956). Embryos
CC display motor axon misprojections and stalling: motor axons are error-
CC prone and wander inefficiently at choice points within embryos
CC (PubMed:18031680). Conditional knockout mice lacking Mycbp2 in the
CC retina, exhibit no gross retinal developmental defects; mutants retain
CC normal retinal lamination, monocular segregation and spontaneous
CC retinal wave activity, but mutant retinal ganglion cells exhibit
CC ipsilateral projection to an improper region of the dorsal lateral
CC geniculate nucleus (dLGN) (PubMed:19371781, PubMed:21324225).
CC Conditional knockout mice lacking Mycbp2 in peripheral sensory neurons
CC display prolonged thermal hyperalgesia: defects are caused by
CC constitutive activation of MAP kinase p38 (Mapk11, Mapk12, Mapk13
CC and/or Mapk14), leading to inhibit internalization of Trpv1
CC (PubMed:21098484). {ECO:0000269|PubMed:14729956,
CC ECO:0000269|PubMed:17901218, ECO:0000269|PubMed:18031680,
CC ECO:0000269|PubMed:19371781, ECO:0000269|PubMed:21098484,
CC ECO:0000269|PubMed:21324225}.
CC -!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family. {ECO:0000305}.
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DR EMBL; AC114410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY325887; AAP88591.1; -; mRNA.
DR EMBL; BC059257; AAH59257.1; -; mRNA.
DR CCDS; CCDS49559.1; -. [Q7TPH6-2]
DR RefSeq; NP_997098.2; NM_207215.2. [Q7TPH6-2]
DR PDB; 3GBW; X-ray; 1.32 A; A=1229-1390.
DR PDB; 3HWJ; X-ray; 2.25 A; A/B=1723-1883.
DR PDBsum; 3GBW; -.
DR PDBsum; 3HWJ; -.
DR SMR; Q7TPH6; -.
DR BioGRID; 222897; 153.
DR IntAct; Q7TPH6; 142.
DR MINT; Q7TPH6; -.
DR STRING; 10090.ENSMUSP00000124710; -.
DR iPTMnet; Q7TPH6; -.
DR PhosphoSitePlus; Q7TPH6; -.
DR SwissPalm; Q7TPH6; -.
DR EPD; Q7TPH6; -.
DR jPOST; Q7TPH6; -.
DR MaxQB; Q7TPH6; -.
DR PaxDb; Q7TPH6; -.
DR PRIDE; Q7TPH6; -.
DR ProteomicsDB; 287559; -. [Q7TPH6-1]
DR ProteomicsDB; 287560; -. [Q7TPH6-2]
DR ProteomicsDB; 355672; -.
DR Antibodypedia; 24520; 54 antibodies from 12 providers.
DR DNASU; 105689; -.
DR Ensembl; ENSMUST00000159855; ENSMUSP00000124710; ENSMUSG00000033004. [Q7TPH6-2]
DR GeneID; 105689; -.
DR KEGG; mmu:105689; -.
DR CTD; 23077; -.
DR MGI; MGI:2179432; Mycbp2.
DR VEuPathDB; HostDB:ENSMUSG00000033004; -.
DR eggNOG; KOG1428; Eukaryota.
DR GeneTree; ENSGT00940000155756; -.
DR InParanoid; Q7TPH6; -.
DR OMA; NKLCILD; -.
DR OrthoDB; 215263at2759; -.
DR PhylomeDB; Q7TPH6; -.
DR TreeFam; TF313151; -.
DR BRENDA; 2.3.2.33; 3474.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 105689; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Mycbp2; mouse.
DR EvolutionaryTrace; Q7TPH6; -.
DR PRO; PR:Q7TPH6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q7TPH6; protein.
DR Bgee; ENSMUSG00000033004; Expressed in ventromedial nucleus of hypothalamus and 264 other tissues.
DR ExpressionAtlas; Q7TPH6; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:MGI.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IBA:GO_Central.
DR Gene3D; 2.130.10.30; -; 2.
DR Gene3D; 2.60.120.820; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF08005; PHR; 2.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF08239; SH3_3; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond;
KW Guanine-nucleotide releasing factor; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..4749
FT /note="E3 ubiquitin-protein ligase MYCBP2"
FT /id="PRO_0000055964"
FT REPEAT 600..655
FT /note="RCC1 1"
FT /evidence="ECO:0000255"
FT REPEAT 699..755
FT /note="RCC1 2"
FT /evidence="ECO:0000255"
FT REPEAT 907..957
FT /note="RCC1 3"
FT /evidence="ECO:0000255"
FT REPEAT 958..1009
FT /note="RCC1 4"
FT /evidence="ECO:0000255"
FT REPEAT 1011..1066
FT /note="RCC1 5"
FT /evidence="ECO:0000255"
FT REPEAT 2331..2438
FT /note="Filamin"
FT /evidence="ECO:0000255"
FT DOMAIN 3789..3967
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT ZN_FING 4499..4550
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 87..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1386
FT /note="PHR domain 1"
FT REGION 1723..1881
FT /note="PHR domain 2"
FT REGION 2018..2544
FT /note="RAE1 binding"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT REGION 2313..2336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2780..3084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3677..3700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3986..4007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4610..4747
FT /note="Tandem cysteine domain"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2780..2807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2808..2829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2855..2890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2891..2905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2906..2928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2932..2962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3003..3025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3044..3060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3990..4004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4629
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT ACT_SITE 4681
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4658
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4743
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 4682
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 4687
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 4695
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2841
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2905
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 2992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 3162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 3550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 3577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 3992
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4002
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MOD_RES 4003
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT DISULFID 1745..1860
FT /evidence="ECO:0000305|PubMed:20156452"
FT VAR_SEQ 4010..4012
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014184"
FT MUTAGEN 950..951
FT /note="HH->AA: Abolished guanosine exchange factor (GEF)
FT activity for Ran."
FT /evidence="ECO:0000269|PubMed:26304119"
FT CONFLICT 860
FT /note="E -> K (in Ref. 2; AAP88591)"
FT CONFLICT 999
FT /note="G -> C (in Ref. 2; AAP88591)"
FT CONFLICT 1831
FT /note="R -> S (in Ref. 2; AAP88591)"
FT CONFLICT 1987
FT /note="P -> S (in Ref. 2; AAP88591)"
FT CONFLICT 3685
FT /note="E -> G (in Ref. 2; AAP88591)"
FT CONFLICT 4636
FT /note="G -> E (in Ref. 2; AAP88591)"
FT STRAND 1232..1235
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1237..1240
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1252..1260
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1262..1270
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1276..1286
FT /evidence="ECO:0007829|PDB:3GBW"
FT TURN 1287..1291
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1297..1301
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1305..1307
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1314..1325
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1330..1340
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1345..1348
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1350..1353
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1359..1364
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1373..1378
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1381..1385
FT /evidence="ECO:0007829|PDB:3GBW"
FT STRAND 1724..1728
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1730..1732
FT /evidence="ECO:0007829|PDB:3HWJ"
FT HELIX 1737..1739
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1742..1751
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1753..1761
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1767..1775
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1791..1800
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1808..1819
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1826..1835
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1840..1843
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1845..1848
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1854..1858
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1869..1873
FT /evidence="ECO:0007829|PDB:3HWJ"
FT STRAND 1876..1881
FT /evidence="ECO:0007829|PDB:3HWJ"
SQ SEQUENCE 4749 AA; 521232 MW; D225D8DCA55961E7 CRC64;
MMMCAATASP AAASSGPGGD GFFAAATISS SPAPGALFMP VPDGSVAAAG LGLGLPTTDS
RGHYQLLLSG RALADRYRRI YTTALSDRDQ AGSSTGHPAS RNKKILNKKK LKRKQKSKSK
VKTRSKSENV ENTVIIPDIK LHSNPSAFNI YCNVRHCVLE WQKKETSLAA ASKNSVQSGE
SDSDEEEESR EPPIKLPKII EVGLCEVFEL IKETRFSHPS LCLRSLQALL NVLQGQQPEG
LQSEPPEVLE SLFQLLLEIT VRSTGMNDST GQSLTALSCA CLFSLVASWG ETGRTLQAIS
AILTNNGSHA CQTIQVPTIL NSLQRSVQAV LVGKIQVQDW FSNGIKKAAL MHKWPLKEVS
VDEDDQCLLQ NDGFFLYLLC KDGLYKIGSG YSGTVRGHIY NSTSRIRNRK EKKSWLGYAQ
GYLLYRDLNN HSMTAIRISP ETLEQDGTVL LPDCHTEGQN ILFTDGEYIN QIAASRDDGF
VVRIFATSTE PVLQQELQLK LARKCLHACG ISLFDLEKDL HIISTGFDEE SAILGAGREF
ALMKTANGKI YYTGKYQSLG IKQGGPSAGK WVELPITKSP KIVHFSVGHD GSHALLVAED
GSVFFTGSAS KGEDGESTKS RRQSKPYKPK KIIKMEGKIV VYTACNNGSS SVISKDGELY
MFGKDAIYSD SSSLVSDLKG HFVTQVAMGK AHTCVLMKNG EVWTFGVNNK GQCGRDTGAM
NQGGKGFGVE NMATAMDEDL EEELDEKDEK SMMCPPGMHK WKLEQCMVCT VCGDCTGYGA
SCVSSGRPDR VPGGICGCGS GESGCAVCGC CKACARELDG QEARQRGILD AVKEMIPLDL
LLAVPVPGVN IEEHLQLRQE EKRQRVIRRH RLEDGRGPLV FAGPIFMNHR EQALARLRSH
PAQLKHKRDK HKDGSGDRGE KDASKITTYP PGSVRFDCEL RAVQVSCGFH HSVVLMENGD
VYTFGYGQHG QLGHGDVNSR GCPTLVQALP GPSTQVTAGS NHTAVLLMDG QVFTFGSFSK
GQLGRPILDI PYWNAKPAPM PNIGSKYGRK ATWIGASGDQ TFLRIDEALI NSHVLATSEI
FASKHIIGLV PASISEPPPF KCLLINKVDG SCKTFNDSEQ EDLQGFGVCL DPVYDVLWRF
RPSTRELWCY NAVVADARLP SATDMQSRCS ILSPELALPT GSRALTTRSH AALHILGCLD
TLAAMQDLKM GIASTEEETQ AVMKVYSKED YSVVNRFESH GGGWGYSAHS VEAIRFSADT
DILLGGLGLF GGRGEYTAKI KLFELGPDGG DHETDGDLLA ETDVLAYDCA AREKYAMMFD
EPVLLQAGWW YVAWARVSGP SSDCGSHGQA SITTDDGVIF QFKSSKKSNN GTDVNAGQIP
QLLYRLPTSD GSTSKGKQQT SEPVHILKRS FARTVSVECF ESLLSILHWS WTTLVLGVEE
LRGLKGFQFT ATLLDLERLR FVGTCCLRLL RVYTCEIYPV SATGKAVVEE TSKLAECIGK
TRTLLRKILS EGVDHCMVKL DNDPQGYLSQ PLRLLEAVLQ ECHNTFTACF HSFYPTPALQ
WACLCDLLNC LDQEANFKTS SSRLLAAVMS ALCHTSVKLT SLFPIAYDGE VLLRSIVKQV
STENDSTLVH RFPLLVGHME KLSQSEENIS GMTSFREVLE KMLVIVVLPV RNSLRRESEL
FSSHLVSNTC GLLASIVSEL TASALGSEVD GLNSLHSVKA SANRFTKTSQ GRSWNTGNGS
PDAICFAVDK PGIVVVGFAV YGGGGIHEYE LEVLVDDSEH AGDSTHSHRW TSLELVKGTY
TTDDSPSDIA EIRLDKVVPL KENVKYAVRL RNYGSRTANG DGGMTTVQCP DGVTFTFSTC
SLSSNGTNQT RGQIPQILYY RSEFDGDLQS QLLSKANEED KNCSRALSVV STVVRAAKDL
LHRALAVDAD DIPELLSSSS LFSMLLPLII AYIGPVAAAI PKVAVEVFGL VQQLLPSVAI
LNQKYAPPAF NPNQSTDSTT GNQPEQGLSA CTTSNHYAVI ESEHPYKPAC VMHYKVTFPE
CVRWMTIEFD PQCGTAQSED VIRLLIPVRT IQNSGYGAKL TSVHENLNSW VELKKYSGSS
GWPTMVLVLP GNEALFSLET ASDYVKDDKA SFYGFKCFAI GYEFSPGPDE GVIQLEKELA
NLGGVCAAAL MKKDLALPVG NELEEDLEIL EEAALQVCKT HSGILGKGLA LSHSPTILEA
LEGNLPLQIQ SNEQSFLDDF IACVPGSSGG RLARWLQPDS YADPQKTSLI LNKDDIRCGW
PTTITVQTKD QYGDVVHVPN MKVEVKAVPV SQKKTSLQQD QGKKCQRIPG SPSAAASSAD
MTFGGLASPK LDVSYEPMIV KEARYIAITM MKVYENYSFE ELRFASPTPK RPSENMLIRV
NNDGTYCANW TPGAIGLYTV HVTIDGIEID AGLEVKVKDP PKGMIPPGTQ LVKPKADPQP
NKIRKFVAKD SAGLRIRSHP SLQSEQIGIV RVNGTITFID EIHNDDGVWL RLNEETIKKY
VPNMNGYTEA WCLSFNQHLG KSLLVPVDNI FNASQGVRDL DVFSWTSKAF FPQEPKTNTD
DFFKDMNSCG PQEATMQERD HPFLRGGPGM YKVVKTGPSG HNIRSCPNLR GIPIGMLVLG
NKVKAVGEVT NSEGAWVQLD KNSMVEFCES DEGEAWSLAR DRGGNQYLRH EDEQVLLDQN
SQPPPPSPFS VQAFNKGASC SAQGFDYGLG NNKGDQLSAI LNSIQSRPNL PAPSIFDQAA
KPPSSLVHSP FVFGQPLSFQ QRQLQSDRGT ISTSSRPVST SGKSELPSKH SRSVKPDGHV
SRTPADQKKP RGTEGLSASE SLMLKSDAAK LRSDSHSRSL SPNHNTLQTL KSDGRTSSGF
RAESPGPGSR SSSPKPKPLP TPRSSPSGAS SPRSSSPQDK NLPQKSTAPA KTKLDPPRER
SKSDSYTLDP DTLRKKKMPL TEPLRGRSTS PKPKPVPKDP KDSPGSENRA PSPHVVQENL
HSEVVEVCTS STLKTNGVTD STCDDSGDLK SVDEGSNKVH FSIGKAPLKD EQEMRASPKI
SRKCANRHTR PKKEKSNFLF KGDGTKSLEP AKQAMSPSVA ECARAVFASF LWHEGIVHDA
MACSSFLKFN PDLSKEHAPI RSSLNSQPPT EEKEIKLKNR HSLEISSALN MFNIAPHGPD
ISKMGSINKN KVLSMLKEPP LHEKCEDGKS EATFEMSMHH TMKSKSPLPL TLQHLVAFWE
DISLATIKAA SQNMIFPSPG SCAVLKKKEC EKENKKTKKE KKKKEKTEIR PRGNLFGEMA
QLAVGGPEKD TICELCGESH PYPVTYHMRQ AHPGCGRYAG GQGYNSIGHF CGGWAGNCGD
GGMGGSTWYL VCDRCREKYL REKQAAAREK VKQSRRKPMQ VKTPRALPTM EAHQVIKANA
LFLLSLSSAA EPSILCYHPA KPFQSQLPIV KEGVSEDLPV KMPCLYLQTL ARHHHENFVG
YQDDNLFQDE MRYLRSTSVP APYISVTPDA SPNVFEEPES NMKSMPPSLE TSPITDTDLA
KRTVFQRSYS VVASEYDKQH SILPARVKAI PRRRVNSGDT VGSSLLRHPS PELSRLISAH
SSLSKGERNF QWPVLAFVIQ HHDLEGLEIA MKQALRKSAC RVFAMEAFNW LLCNVIQTTS
LHDILWHFVA ALTPSPVEAE EDEDEDNKSN KENAEQEKDT RVCEHPLSDI VIAGEAAHPL
PHTFHRLLQT ISDLMMSLPS GSSLQQMALR CWSLKFKQSD HQFLHQSNVF HHINNILSKS
DDGDSEESFS ISVQSGFEAM SQELCIVMCL KDLTSIVDIK TSSRPAMIGS LTDGSTETFW
ESGDEDKNKT KNITINCVKG INARYVSVHV DNSRDLGNKV TSMTFLTGKA VEELCRIKQV
DLDSRHIGWV TSELPGGDNQ IIKIELKGPE NTLRVRQVKV LGWKDGESTK IAGQISASVA
QQRSCEAETL RVFRLITSQV FGKLISGDAE PTPEQEEKAL LSSPEGEEKV YNATSDADLK
EHMVGIIFSR SKLTNLQKQV CAHIVQAIRM EATRVREEWE HAISSKENAN SQPSDEDASS
DAYCFELLSM VLALSGSNVG RQYLAQQLTL LQDLFSLLHT ASPRVQRQVT SLLRRVLPEV
TPNRLASIIG VKSLPPADIS DIIHSTEKGD WNKLGILDMF LGCIAKALTV QLKAKGTTIT
GTAGTTVGKG VTTVTLPMIF NSSYLRRGES HWWMKGSTPT QISEIIIRLI KDMAAGHLSE
AWSRVTKNAI AETIIALTKM EEEFRSPVRC IATTRLWLAL ASLCVLDQDH VDRLSSGRWM
GKDGQQKQMP MCDNHDDGET AAIILCNICG NLCTDCDRFL HLHRRTKTHQ RQVFKEEEEA
IKVDLHEGCG RTKLFWLMAL ADSKTMKAMV EFREHTGKPT TSSSEACRFC GSRSGTELSA
VGSVCSDADC QEYAKIACSK THPCGHPCGG VRNEEHCLPC LHGCDKSATT LKQDADDMCM
ICFTEALSAA PAIQLDCSHV FHLQCCRRVL ENRWLGPRIT FGFISCPICK NKINHIVLKD
LLDPIKELYE DVRRKALMRL EYEGLHKSEA ITTPGVRFYN DAAGYAMNRY AYYVCYKCRK
AYFGGEARCD AEAGQGDDYD PRELICGACS DVSRAQMCPK HGTDFLEYKC RYCCSVAVFF
CFGTTHFCNA CHDDFQRMTS IPKEELPHCP AGPKGKQLEG TECPLHVVHP PTGEEFALGC
GVCRNAHTF
