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E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.27) (Myc-binding protein 2) (Pam/highwire/rpm-1 protein) (Protein associated with Myc) (RING-type E3 ubiquitin transferase MYCBP2)

 MYCB2_MOUSE             Reviewed;        4711 AA.
Q7TPH6; Q6PCM8;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
25-APR-2018, entry version 140.
RecName: Full=E3 ubiquitin-protein ligase MYCBP2;
EC=2.3.2.27;
AltName: Full=Myc-binding protein 2;
AltName: Full=Pam/highwire/rpm-1 protein;
AltName: Full=Protein associated with Myc;
AltName: Full=RING-type E3 ubiquitin transferase MYCBP2 {ECO:0000305};
Name=Mycbp2 {ECO:0000250|UniProtKB:O75592};
Synonyms=Pam {ECO:0000303|PubMed:14729956},
Phr1 {ECO:0000312|EMBL:AAP88591.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAP88591.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP88591.1};
TISSUE=Embryo {ECO:0000269|PubMed:14729956};
PubMed=14729956; DOI=10.1128/MCB.24.3.1096-1105.2004;
Burgess R.W., Peterson K.A., Johnson M.J., Roix J.J., Welsh I.C.,
O'Brien T.P.;
"Evidence for a conserved function in synapse formation reveals Phr1
as a candidate gene for respiratory failure in newborn mice.";
Mol. Cell. Biol. 24:1096-1105(2004).
[2]
PROTEIN SEQUENCE OF 2327-2352 AND 2866-2875, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[3] {ECO:0000305, ECO:0000312|EMBL:AAH59257.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3250-4711 (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH59257.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH59257.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH CPNE1 AND CPNE4.
PubMed=12522145; DOI=10.1074/jbc.M212632200;
Tomsig J.L., Snyder S.L., Creutz C.E.;
"Identification of targets for calcium signaling through the copine
family of proteins. Characterization of a coiled-coil copine-binding
motif.";
J. Biol. Chem. 278:10048-10054(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3512, AND 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).
[7]
INTERACTION WITH FBXO45.
PubMed=19398581; DOI=10.1128/MCB.00364-09;
Saiga T., Fukuda T., Matsumoto M., Tada H., Okano H.J., Okano H.,
Nakayama K.I.;
"Fbxo45 forms a novel ubiquitin ligase complex and is required for
neuronal development.";
Mol. Cell. Biol. 29:3529-3543(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-143; SER-145;
SER-2903; SER-2954 AND THR-3954, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
[9]
X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 1191-1352, X-RAY
CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1685-1845, DOMAIN PHR, AND
DISULFIDE BOND.
PubMed=20156452; DOI=10.1016/j.jmb.2010.02.017;
Sampathkumar P., Ozyurt S.A., Miller S.A., Bain K.T., Rutter M.E.,
Gheyi T., Abrams B., Wang Y., Atwell S., Luz J.G., Thompson D.A.,
Wasserman S.R., Emtage J.S., Park E.C., Rongo C., Jin Y., Klemke R.L.,
Sauder J.M., Burley S.K.;
"Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the
loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog
RPM-1.";
J. Mol. Biol. 397:883-892(2010).
-!- FUNCTION: E3 ubiquitin-protein ligase which mediates
ubiquitination and subsequent proteasomal degradation of
TSC2/tuberin. Interacts with the E2 enzymes UBE2D1, UBE2D3 and
UBE2L3 (By similarity). May have a role during synaptogenesis;
candidate for respiratory distress and ventilatory disorders that
arise from defective neuronal control of breathing. May function
as a facilitator or regulator of transcriptional activation by
MYC. {ECO:0000250, ECO:0000269|PubMed:14729956}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via
VWFA domain) (PubMed:12522145). Interacts with MYC (By
similarity). Interacts with TSC2 (tuberin) when TSC2 is in complex
with TSC1 (hamartin) (By similarity). Interacts with FBXO45
(PubMed:19398581). Interacts with RAE1 (By similarity).
{ECO:0000250|UniProtKB:O75592, ECO:0000269|PubMed:12522145,
ECO:0000269|PubMed:19398581}.
-!- INTERACTION:
Q63633:Slc12a5 (xeno); NbExp=4; IntAct=EBI-1811542, EBI-1811510;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000303|PubMed:14729956};
IsoId=Q7TPH6-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q7TPH6-2; Sequence=VSP_014184;
-!- TISSUE SPECIFICITY: Dynamically expressed in embryonic nervous
system from E8.5 through E18.5. During postnatal development,
expression is particularly strong in the cerebellum, hippocampus
and retina. Lower levels of expression are observed throughout the
cerebral cortex. {ECO:0000269|PubMed:14729956}.
-!- DOMAIN: The PHR domains are compact beta-sandwich folds composed
of 11 antiparallel strands and decorated with conserved apical
loops. They are likely to play a structural role and mediate
interactions with substrates or partners.
{ECO:0000269|PubMed:20156452}.
-!- PTM: Autoubiquitinated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display incomplete innervation of the
diaphragm by the phrenic nerve. Intercostal muscles are completely
innervated, but show dysmorphic nerve terminals. Sensory neuron
terminals in the diaphragm are abnormal and neuromuscular
junctions show excessive sprouting of nerve terminals, consistent
with inadequate presynaptic stimulation of the muscle.
{ECO:0000269|PubMed:14729956}.
-!- SIMILARITY: Belongs to the highwire family. {ECO:0000305}.
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EMBL; AY325887; AAP88591.1; -; mRNA.
EMBL; BC059257; AAH59257.1; -; mRNA.
RefSeq; NP_997098.2; NM_207215.2.
UniGene; Mm.6478; -.
PDB; 3GBW; X-ray; 1.32 A; A=1191-1352.
PDB; 3HWJ; X-ray; 2.25 A; A/B=1685-1845.
PDBsum; 3GBW; -.
PDBsum; 3HWJ; -.
ProteinModelPortal; Q7TPH6; -.
SMR; Q7TPH6; -.
BioGrid; 222897; 146.
IntAct; Q7TPH6; 141.
STRING; 10090.ENSMUSP00000124710; -.
iPTMnet; Q7TPH6; -.
PhosphoSitePlus; Q7TPH6; -.
EPD; Q7TPH6; -.
PaxDb; Q7TPH6; -.
PRIDE; Q7TPH6; -.
DNASU; 105689; -.
GeneID; 105689; -.
KEGG; mmu:105689; -.
CTD; 23077; -.
MGI; MGI:2179432; Mycbp2.
eggNOG; KOG1428; Eukaryota.
eggNOG; ENOG410XP1T; LUCA.
HOGENOM; HOG000112908; -.
HOVERGEN; HBG053153; -.
InParanoid; Q7TPH6; -.
KO; K10693; -.
PhylomeDB; Q7TPH6; -.
UniPathway; UPA00143; -.
ChiTaRS; Mycbp2; mouse.
EvolutionaryTrace; Q7TPH6; -.
PRO; PR:Q7TPH6; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MYCBP2; -.
CleanEx; MM_PAM; -.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:MGI.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI.
GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:MGI.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:MGI.
GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.30; -; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.120.820; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR004939; APC_su10/DOC_dom.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR012983; PHR.
InterPro; IPR038648; PHR_sf.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
InterPro; IPR003646; SH3-like_bac-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF03256; ANAPC10; 1.
Pfam; PF00630; Filamin; 1.
Pfam; PF08005; PHR; 2.
Pfam; PF00415; RCC1; 1.
Pfam; PF08239; SH3_3; 1.
Pfam; PF13639; zf-RING_2; 1.
PRINTS; PR00633; RCCNDNSATION.
SMART; SM01337; APC10; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF50985; SSF50985; 2.
SUPFAM; SSF81296; SSF81296; 2.
PROSITE; PS51284; DOC; 1.
PROSITE; PS50194; FILAMIN_REPEAT; 1.
PROSITE; PS00626; RCC1_2; 1.
PROSITE; PS50012; RCC1_3; 3.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 4711 E3 ubiquitin-protein ligase MYCBP2.
/FTId=PRO_0000055964.
REPEAT 562 617 RCC1 1. {ECO:0000255}.
REPEAT 661 717 RCC1 2. {ECO:0000255}.
REPEAT 869 919 RCC1 3. {ECO:0000255}.
REPEAT 920 971 RCC1 4. {ECO:0000255}.
REPEAT 973 1028 RCC1 5. {ECO:0000255}.
REPEAT 2293 2400 Filamin. {ECO:0000255}.
DOMAIN 3751 3929 DOC. {ECO:0000255|PROSITE-
ProRule:PRU00614}.
ZN_FING 4461 4512 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 4615 4665 B box-type.
REGION 1197 1348 PHR domain 1.
REGION 1685 1843 PHR domain 2.
REGION 1980 2506 RAE1 binding.
{ECO:0000250|UniProtKB:O75592}.
COMPBIAS 65 88 Lys-rich. {ECO:0000255}.
COMPBIAS 728 776 Cys-rich. {ECO:0000255}.
COMPBIAS 2754 2878 Ser-rich. {ECO:0000255}.
COMPBIAS 2847 2955 Pro-rich. {ECO:0000255}.
COMPBIAS 3228 3248 Lys-rich. {ECO:0000255}.
COMPBIAS 3296 3327 Gly-rich. {ECO:0000255}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1583 1583 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2803 2803 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2821 2821 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2823 2823 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2867 2867 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2873 2873 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2903 2903 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2905 2905 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2954 2954 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 3019 3019 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3124 3124 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3512 3512 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 3539 3539 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3954 3954 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 3964 3964 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3965 3965 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
DISULFID 1707 1822 {ECO:0000305|PubMed:20156452}.
VAR_SEQ 3972 3974 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014184.
CONFLICT 3647 3647 G -> E (in Ref. 3; AAH59257).
{ECO:0000305}.
CONFLICT 4598 4598 E -> G (in Ref. 3; AAH59257).
{ECO:0000305}.
STRAND 1194 1197 {ECO:0000244|PDB:3GBW}.
STRAND 1199 1202 {ECO:0000244|PDB:3GBW}.
STRAND 1214 1222 {ECO:0000244|PDB:3GBW}.
STRAND 1224 1232 {ECO:0000244|PDB:3GBW}.
STRAND 1238 1248 {ECO:0000244|PDB:3GBW}.
TURN 1249 1253 {ECO:0000244|PDB:3GBW}.
STRAND 1259 1263 {ECO:0000244|PDB:3GBW}.
STRAND 1267 1269 {ECO:0000244|PDB:3GBW}.
STRAND 1276 1287 {ECO:0000244|PDB:3GBW}.
STRAND 1292 1302 {ECO:0000244|PDB:3GBW}.
STRAND 1307 1310 {ECO:0000244|PDB:3GBW}.
STRAND 1312 1315 {ECO:0000244|PDB:3GBW}.
STRAND 1321 1326 {ECO:0000244|PDB:3GBW}.
STRAND 1335 1340 {ECO:0000244|PDB:3GBW}.
STRAND 1343 1347 {ECO:0000244|PDB:3GBW}.
STRAND 1686 1690 {ECO:0000244|PDB:3HWJ}.
STRAND 1692 1694 {ECO:0000244|PDB:3HWJ}.
HELIX 1699 1701 {ECO:0000244|PDB:3HWJ}.
STRAND 1704 1713 {ECO:0000244|PDB:3HWJ}.
STRAND 1715 1723 {ECO:0000244|PDB:3HWJ}.
STRAND 1729 1737 {ECO:0000244|PDB:3HWJ}.
STRAND 1753 1762 {ECO:0000244|PDB:3HWJ}.
STRAND 1770 1781 {ECO:0000244|PDB:3HWJ}.
STRAND 1788 1797 {ECO:0000244|PDB:3HWJ}.
STRAND 1802 1805 {ECO:0000244|PDB:3HWJ}.
STRAND 1807 1810 {ECO:0000244|PDB:3HWJ}.
STRAND 1816 1820 {ECO:0000244|PDB:3HWJ}.
STRAND 1831 1835 {ECO:0000244|PDB:3HWJ}.
STRAND 1838 1843 {ECO:0000244|PDB:3HWJ}.
SEQUENCE 4711 AA; 517738 MW; 03C9A3975EED7552 CRC64;
MPVPDGSVAA AGLGLGLPTT DSRGHYQLLL SGRALADRYR RIYTTALSDR DQAGSSTGHP
ASRNKKILNK KKLKRKQKSK SKVKTRSKSE NVENTVIIPD IKLHSNPSAF NIYCNVRHCV
LEWQKKETSL AAASKNSVQS GESDSDEEEE SREPPIKLPK IIEVGLCEVF ELIKETRFSH
PSLCLRSLQA LLNVLQGQQP EGLQSEPPEV LESLFQLLLE ITVRSTGMND STGQSLTALS
CACLFSLVAS WGETGRTLQA ISAILTNNGS HACQTIQVPT ILNSLQRSVQ AVLVGKIQVQ
DWFSNGIKKA ALMHKWPLKE VSVDEDDQCL LQNDGFFLYL LCKDGLYKIG SGYSGTVRGH
IYNSTSRIRN RKEKKSWLGY AQGYLLYRDL NNHSMTAIRI SPETLEQDGT VLLPDCHTEG
QNILFTDGEY INQIAASRDD GFVVRIFATS TEPVLQQELQ LKLARKCLHA CGISLFDLEK
DLHIISTGFD EESAILGAGR EFALMKTANG KIYYTGKYQS LGIKQGGPSA GKWVELPITK
SPKIVHFSVG HDGSHALLVA EDGSVFFTGS ASKGEDGEST KSRRQSKPYK PKKIIKMEGK
IVVYTACNNG SSSVISKDGE LYMFGKDAIY SDSSSLVSDL KGHFVTQVAM GKAHTCVLMK
NGEVWTFGVN NKGQCGRDTG AMNQGGKGFG VENMATAMDE DLEEELDEKD EKSMMCPPGM
HKWKLEQCMV CTVCGDCTGY GASCVSSGRP DRVPGGICGC GSGESGCAVC GCCKACAREL
DGQEARQRGI LDAVKEMIPL DLLLAVPVPG VNIEEHLQLR QKEKRQRVIR RHRLEDGRGP
LVFAGPIFMN HREQALARLR SHPAQLKHKR DKHKDGSGDR GEKDASKITT YPPGSVRFDC
ELRAVQVSCG FHHSVVLMEN GDVYTFGYGQ HGQLGHGDVN SRGCPTLVQA LPGPSTQVTA
CSNHTAVLLM DGQVFTFGSF SKGQLGRPIL DIPYWNAKPA PMPNIGSKYG RKATWIGASG
DQTFLRIDEA LINSHVLATS EIFASKHIIG LVPASISEPP PFKCLLINKV DGSCKTFNDS
EQEDLQGFGV CLDPVYDVLW RFRPSTRELW CYNAVVADAR LPSATDMQSR CSILSPELAL
PTGSRALTTR SHAALHILGC LDTLAAMQDL KMGIASTEEE TQAVMKVYSK EDYSVVNRFE
SHGGGWGYSA HSVEAIRFSA DTDILLGGLG LFGGRGEYTA KIKLFELGPD GGDHETDGDL
LAETDVLAYD CAAREKYAMM FDEPVLLQAG WWYVAWARVS GPSSDCGSHG QASITTDDGV
IFQFKSSKKS NNGTDVNAGQ IPQLLYRLPT SDGSTSKGKQ QTSEPVHILK RSFARTVSVE
CFESLLSILH WSWTTLVLGV EELRGLKGFQ FTATLLDLER LRFVGTCCLR LLRVYTCEIY
PVSATGKAVV EETSKLAECI GKTRTLLRKI LSEGVDHCMV KLDNDPQGYL SQPLRLLEAV
LQECHNTFTA CFHSFYPTPA LQWACLCDLL NCLDQEANFK TSSSRLLAAV MSALCHTSVK
LTSLFPIAYD GEVLLRSIVK QVSTENDSTL VHRFPLLVGH MEKLSQSEEN ISGMTSFREV
LEKMLVIVVL PVRNSLRRES ELFSSHLVSN TCGLLASIVS ELTASALGSE VDGLNSLHSV
KASANRFTKT SQGRSWNTGN GSPDAICFAV DKPGIVVVGF AVYGGGGIHE YELEVLVDDS
EHAGDSTHSH RWTSLELVKG TYTTDDSPSD IAEIRLDKVV PLKENVKYAV RLSNYGSRTA
NGDGGMTTVQ CPDGVTFTFS TCSLSSNGTN QTRGQIPQIL YYRSEFDGDL QSQLLSKANE
EDKNCSRALS VVSTVVRAAK DLLHRALAVD ADDIPELLSS SSLFSMLLPL IIAYIGPVAA
AIPKVAVEVF GLVQQLLPSV AILNQKYASP AFNPNQSTDS TTGNQPEQGL SACTTSNHYA
VIESEHPYKP ACVMHYKVTF PECVRWMTIE FDPQCGTAQS EDVIRLLIPV RTIQNSGYGA
KLTSVHENLN SWVELKKYSG SSGWPTMVLV LPGNEALFSL ETASDYVKDD KASFYGFKCF
AIGYEFSPGP DEGVIQLEKE LANLGGVCAA ALMKKDLALP VGNELEEDLE ILEEAALQVC
KTHSGILGKG LALSHSPTIL EALEGNLPLQ IQSNEQSFLD DFIACVPGSS GGRLARWLQP
DSYADPQKTS LILNKDDIRC GWPTTITVQT KDQYGDVVHV PNMKVEVKAV PVSQKKTSLQ
QDQGKKCQRI PGSPSAAASS ADMTFGGLAS PKLDVSYEPM IVKEARYIAI TMMKVYENYS
FEELRFASPT PKRPSENMLI RVNNDGTYCA NWTPGAIGLY TVHVTIDGIE IDAGLEVKVK
DPPKGMIPPG TQLVKPKADP QPNKIRKFVA KDSAGLRIRS HPSLQSEQIG IVRVNGTITF
IDEIHNDDGV WLRLNEETIK KYVPNMNGYT EAWCLSFNQH LGKSLLVPVD NIFNASQGVR
DLDVFSWTSK AFFPQEPKTN TDDFFKDMNS CGPQEATMQE RDHPFLRGGP GMYKVVKTGP
SGHNIRSCPN LRGIPIGMLV LGNKVKAVGE VTNSEGAWVQ LDKNSMVEFC ESDEGEAWSL
ARDRGGNQYL RHEDEQVLLD QNSQPPPPSP FSVQAFNKGA SCSAQGFDYG LGNNKGDQLS
AILNSIQSRP NLPAPSIFDQ AAKPPSSLVH SPFVFGQPLS FQQRQLQSDR GTISTSSRPV
STSGKSELPS KHSRSVKPDG HVSRTPADQK KPRGTEGLSA SESLMLKSDA AKLRSDSHSR
SLSPNHNTLQ TLKSDGRTSS GFRAESPGPG SRSSSPKPKP LPTPRSSPSG ASSPRSSSPQ
DKNLPQKSTA PAKTKLDPPR ERSKSDSYTL DPDTLRKKKM PLTEPLRGRS TSPKPKPVPK
DPKDSPGSEN RAPSPHVVQE NLHSEVVEVC TSSTLKTNGV TDSTCDDSGD LKSVDEGSNK
VHFSIGKAPL KDEQEMRASP KISRKCANRH TRPKKEKSNF LFKGDGTKSL EPAKQAMSPS
VAECARAVFA SFLWHEGIVH DAMACSSFLK FNPDLSKEHA PIRSSLNSQP PTEEKEIKLK
NRHSLEISSA LNMFNIAPHG PDISKMGSIN KNKVLSMLKE PPLHEKCEDG KSEATFEMSM
HHTMKSKSPL PLTLQHLVAF WEDISLATIK AASQNMIFPS PGSCAVLKKK ECEKENKKTK
KEKKKKEKTE IRPRGNLFGE MAQLAVGGPE KDTICELCGE SHPYPVTYHM RQAHPGCGRY
AGGQGYNSIG HFCGGWAGNC GDGGMGGSTW YLVCDRCREK YLREKQAAAR EKVKQSRRKP
MQVKTPRALP TMEAHQVIKA NALFLLSLSS AAEPSILCYH PAKPFQSQLP IVKEGVSEDL
PVKMPCLYLQ TLARHHHENF VGYQDDNLFQ DEMRYLRSTS VPAPYISVTP DASPNVFEEP
ESNMKSMPPS LETSPITDTD LAKRTVFQRS YSVVASEYDK QHSILPARVK AIPRRRVNSG
DTVGSSLLRH PSPELSRLIS AHSSLSKGER NFQWPVLAFV IQHHDLEGLE IAMKQALRKS
ACRVFAMEAF NWLLCNVIQT TSLHDILWHF VAALTPSPVE AEEDEDGDNK SNKENAEQEK
DTRVCEHPLS DIVIAGEAAH PLPHTFHRLL QTISDLMMSL PSGSSLQQMA LRCWSLKFKQ
SDHQFLHQSN VFHHINNILS KSDDGDSEES FSISVQSGFE AMSQELCIVM CLKDLTSIVD
IKTSSRPAMI GSLTDGSTET FWESGDEDKN KTKNITINCV KGINARYVSV HVDNSRDLGN
KVTSMTFLTG KAVEELCRIK QVDLDSRHIG WVTSELPGGD NQIIKIELKG PENTLRVRQV
KVLGWKDGES TKIAGQISAS VAQQRSCEAE TLRVFRLITS QVFGKLISGD AEPTPEQEEK
ALLSSPEGEE KVYNATSDAD LKEHMVGIIF SRSKLTNLQK QVCAHIVQAI RMEATRVREE
WEHAISSKEN ANSQPSDEDA SSDAYCFELL SMVLALSGSN VGRQYLAQQL TLLQDLFSLL
HTASPRVQRQ VTSLLRRVLP EVTPNRLASI IGVKSLPPAD ISDIIHSTEK GDWNKLGILD
MFLGCIAKAL TVQLKAKGTT ITGTAGTTVG KGVTTVTLPM IFNSSYLRRG ESHWWMKGST
PTQISEIIIR LIKDMAAGHL SEAWSRVTKN AIAETIIALT KMEEEFRSPV RCIATTRLWL
ALASLCVLDQ DHVDRLSSGR WMGKDGQQKQ MPMCDNHDDG ETAAIILCNI CGNLCTDCDR
FLHLHRRTKT HQRQVFKEEE EAIKVDLHEG CGRTKLFWLM ALADSKTMKA MVEFREHTGK
PTTSSSEACR FCGSRSGTEL SAVGSVCSDA DCQEYAKIAC SKTHPCGHPC GGVRNEEHCL
PCLHGCDKSA TTLKQDADDM CMICFTEALS AAPAIQLDCS HVFHLQCCRR VLENRWLGPR
ITFGFISCPI CKNKINHIVL KDLLDPIKEL YEDVRRKALM RLEYEGLHKS EAITTPGVRF
YNDAAGYAMN RYAYYVCYKC RKAYFGGEAR CDAEAGQEDD YDPRELICGA CSDVSRAQMC
PKHGTDFLEY KCRYCCSVAV FFCFGTTHFC NACHDDFQRM TSIPKEELPH CPAGPKGKQL
EGTECPLHVV HPPTGEEFAL GCGVCRNAHT F


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