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E3 ubiquitin-protein ligase UBR2 (EC 2.3.2.27) (N-recognin-2) (RING-type E3 ubiquitin transferase UBR2) (Ubiquitin-protein ligase E3-alpha-2) (Ubiquitin-protein ligase E3-alpha-II)

 UBR2_MOUSE              Reviewed;        1755 AA.
Q6WKZ8; Q6DIB9; Q80U31; Q8BUL9; Q8CGW0; Q8K2I6; Q8R0V7; Q8R130;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2005, sequence version 2.
12-SEP-2018, entry version 127.
RecName: Full=E3 ubiquitin-protein ligase UBR2;
EC=2.3.2.27;
AltName: Full=N-recognin-2;
AltName: Full=RING-type E3 ubiquitin transferase UBR2;
AltName: Full=Ubiquitin-protein ligase E3-alpha-2;
AltName: Full=Ubiquitin-protein ligase E3-alpha-II;
Name=Ubr2; Synonyms=Kiaa0349;
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] (ISOFORM 2), INTERACTION WITH UBE2B,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
PHENOTYPE.
PubMed=14585983; DOI=10.1128/MCB.23.22.8255-8271.2003;
Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W.,
Sheng J., Xie Y., Varshavsky A.;
"Female lethality and apoptosis of spermatocytes in mice lacking the
UBR2 ubiquitin ligase of the N-end rule pathway.";
Mol. Cell. Biol. 23:8255-8271(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=C3H/HeN;
PubMed=15548684; DOI=10.1158/0008-5472.CAN-04-2102;
Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W.,
Boyle W.J., Lacey D.L., Han H.Q.;
"Regulation of protein catabolism by muscle-specific and cytokine-
inducible ubiquitin ligase E3alpha-II during cancer cachexia.";
Cancer Res. 64:8193-8198(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Brain, Mammary gland, and Salivary gland;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Thymus;
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).
[6]
TISSUE SPECIFICITY.
PubMed=16311597; DOI=10.1038/ng1681;
Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K.,
Durie P.R., Beier M., Hulskamp G., Guzman C., Rehder H., Beemer F.A.,
Hamel B.C.J., Vanlieferinghen P., Gershoni-Baruch R., Vieira M.W.,
Dumic M., Auslender R., Gil-da-Silva-Lopes V.L., Steinlicht S.,
Rauh M., Shalev S.A., Thiel C., Winterpacht A., Kwon Y.T.,
Varshavsky A., Reis A.;
"Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway,
causes pancreatic dysfunction, malformations and mental retardation
(Johanson-Blizzard syndrome).";
Nat. Genet. 37:1345-1350(2005).
[7]
DISRUPTION PHENOTYPE.
PubMed=16488448; DOI=10.1016/j.mrfmmm.2005.12.016;
Ouyang Y., Kwon Y.T., An J.Y., Eller D., Tsai S.-C., Diaz-Perez S.,
Troke J.J., Teitell M.A., Marahrens Y.;
"Loss of Ubr2, an E3 ubiquitin ligase, leads to chromosome fragility
and impaired homologous recombinational repair.";
Mutat. Res. 596:64-75(2006).
[8]
DISRUPTION PHENOTYPE.
PubMed=16606826; DOI=10.1073/pnas.0601700103;
An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., Kwon Y.T.;
"Impaired neurogenesis and cardiovascular development in mice lacking
the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.";
Proc. Natl. Acad. Sci. U.S.A. 103:6212-6217(2006).
[9]
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).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2B AND HISTONE
H2A.
PubMed=20080676; DOI=10.1073/pnas.0910267107;
An J.Y., Kim E.-A., Jiang Y., Zakrzewska A., Kim D.E., Lee M.J.,
Mook-Jung I., Zhang Y., Kwon Y.T.;
"UBR2 mediates transcriptional silencing during spermatogenesis via
histone ubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 107:1912-1917(2010).
[11]
INTERACTION WITH TEX19.1 AND TEX19.2.
PubMed=21103378; DOI=10.1371/journal.pone.0014017;
Yang F., Cheng Y., An J.Y., Kwon Y.T., Eckardt S., Leu N.A.,
McLaughlin K.J., Wang P.J.;
"The ubiquitin ligase Ubr2, a recognition E3 component of the N-end
rule pathway, stabilizes Tex19.1 during spermatogenesis.";
PLoS ONE 5:E14017-E14017(2010).
[12]
FUNCTION, INTERACTION WITH L1RE1, AND TISSUE SPECIFICITY.
PubMed=28806172; DOI=10.7554/eLife.26152;
MacLennan M., Garcia-Canadas M., Reichmann J., Khazina E., Wagner G.,
Playfoot C.J., Salvador-Palomeque C., Mann A.R., Peressini P.,
Sanchez L., Dobie K., Read D., Hung C.C., Eskeland R., Meehan R.R.,
Weichenrieder O., Garcia-Perez J.L., Adams I.R.;
"Mobilization of LINE-1 retrotransposons is restricted by Tex19.1 in
mouse embryonic stem cells.";
Elife 6:0-0(2017).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28708824; DOI=10.1371/journal.pgen.1006904;
Crichton J.H., Playfoot C.J., MacLennan M., Read D., Cooke H.J.,
Adams I.R.;
"Tex19.1 promotes Spo11-dependent meiotic recombination in mouse
spermatocytes.";
PLoS Genet. 13:E1006904-E1006904(2017).
-!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
N-end rule pathway. Recognizes and binds to proteins bearing
specific N-terminal residues that are destabilizing according to
the N-end rule, leading to their ubiquitination and subsequent
degradation. Plays a critical role in chromatin inactivation and
chromosome-wide transcriptional silencing during meiosis via
ubiquitination of histone H2A. Binds leucine and is a negative
regulator of the leucine-mTOR signaling pathway, thereby
controlling cell growth (By similarity). Required for
spermatogenesis, promotes, with Tex19.1, SPO11-dependent
recombination foci to accumulate and drive robust homologous
chromosome synapsis (PubMed:28708824). Polyubiquitinates LINE-1
retrotransposon encoded, LIRE1, which induces degradation,
inhibiting LINE-1 retranstoposon mobilization (PubMed:28806172).
{ECO:0000250, ECO:0000269|PubMed:14585983,
ECO:0000269|PubMed:20080676, ECO:0000269|PubMed:28708824,
ECO:0000269|PubMed:28806172}.
-!- 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 UBE2B; promotes the UBE2B-H2A interaction
and the ubiquitination of histone H2A by UBE2B and UBR2. Interacts
with RECQL4 (By similarity). Interacts with Tex19.1 and Tex19.2;
does not lead to Tex19.1 degradation and stabilizes it. Interacts
with L1RE1 (PubMed:28806172). {ECO:0000250,
ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:20080676,
ECO:0000269|PubMed:21103378, ECO:0000269|PubMed:28806172}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14585983,
ECO:0000269|PubMed:20080676}. Note=Associated with chromatin
during meiosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6WKZ8-1; Sequence=Displayed;
Name=2;
IsoId=Q6WKZ8-2; Sequence=VSP_015173;
Name=3;
IsoId=Q6WKZ8-3; Sequence=VSP_015172, VSP_015173;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also
expressed in heart, kidney and testis. Expressed in acinar cells
of the pancreas. In testes, expressed primarily in spermatocytes.
Expressed in cerebellum (PubMed:28806172).
{ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:15548684,
ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:28806172}.
-!- INDUCTION: In models of cancer cachexia, induced specifically at
the onset and during the progression of muscle wasting.
{ECO:0000269|PubMed:15548684}.
-!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a
His ligand in place of the fourth Cys of the classical motif.
-!- DOMAIN: The UBR-type zinc finger forms a pocket that mediates
recognition of type 1 N-degrons. It exhibits preference for
Arginine in first position, has poor affinity for histidine, and
doesn't bind acetylated peptides (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Male mice are viable but not fertile, due to
massive apoptosis of spermatocytes. They have a reduction of
testis weight of 68% and no detectable sperm in their epididymis.
The seminiferous tubules contain reduced numbers of post-meiotic
round, elongated spermatids and accumulation of pyknotic and
zygotene-like nuclei. Female mice show severe prenatal lethality,
but the rare surviving are fertile. Fibroblast cells display
spontaneous chromosome instability and fragility (PubMed:14585983,
PubMed:16488448, PubMed:28708824). UBR1 and UBR2 double knockout
embryos die at midgestation, with defects in neurogenesis and
cardiovascular development. These defects included reduced
proliferation as well as precocious migration and differentiation
of neural progenitor cells (PubMed:16606826).
{ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:16488448,
ECO:0000269|PubMed:16606826, ECO:0000269|PubMed:28708824}.
-!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH25617.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH31403.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC65536.3; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AY280958; AAQ17202.1; -; mRNA.
EMBL; AY061885; AAL32102.1; -; mRNA.
EMBL; AK122254; BAC65536.3; ALT_SEQ; Unassigned_DNA.
EMBL; BC025617; AAH25617.1; ALT_INIT; mRNA.
EMBL; BC026391; AAH26391.1; -; mRNA.
EMBL; BC031403; AAH31403.1; ALT_INIT; mRNA.
EMBL; BC075642; AAH75642.1; -; mRNA.
EMBL; AK083320; BAC38864.1; -; mRNA.
CCDS; CCDS28845.1; -. [Q6WKZ8-1]
CCDS; CCDS50127.1; -. [Q6WKZ8-2]
RefSeq; NP_001170845.1; NM_001177374.1. [Q6WKZ8-2]
RefSeq; NP_666190.2; NM_146078.3. [Q6WKZ8-1]
UniGene; Mm.28234; -.
ProteinModelPortal; Q6WKZ8; -.
SMR; Q6WKZ8; -.
BioGrid; 230327; 2.
ELM; Q6WKZ8; -.
IntAct; Q6WKZ8; 1.
MINT; Q6WKZ8; -.
STRING; 10090.ENSMUSP00000108961; -.
iPTMnet; Q6WKZ8; -.
PhosphoSitePlus; Q6WKZ8; -.
PaxDb; Q6WKZ8; -.
PeptideAtlas; Q6WKZ8; -.
PRIDE; Q6WKZ8; -.
Ensembl; ENSMUST00000113335; ENSMUSP00000108961; ENSMUSG00000023977. [Q6WKZ8-2]
Ensembl; ENSMUST00000113337; ENSMUSP00000108963; ENSMUSG00000023977. [Q6WKZ8-1]
GeneID; 224826; -.
KEGG; mmu:224826; -.
UCSC; uc012aus.1; mouse. [Q6WKZ8-1]
UCSC; uc012auu.1; mouse. [Q6WKZ8-3]
CTD; 23304; -.
MGI; MGI:1861099; Ubr2.
eggNOG; KOG1140; Eukaryota.
eggNOG; ENOG410XPQU; LUCA.
GeneTree; ENSGT00530000063055; -.
HOVERGEN; HBG080426; -.
InParanoid; Q6WKZ8; -.
KO; K10626; -.
OMA; MQGMDPI; -.
PhylomeDB; Q6WKZ8; -.
TreeFam; TF323875; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q6WKZ8; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023977; Expressed in 253 organ(s), highest expression level in ear vesicle.
ExpressionAtlas; Q6WKZ8; baseline and differential.
Genevisible; Q6WKZ8; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000151; C:ubiquitin ligase complex; IGI:MGI.
GO; GO:0070728; F:leucine binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071233; P:cellular response to leucine; ISS:UniProtKB.
GO; GO:0006342; P:chromatin silencing; IDA:UniProtKB.
GO; GO:0033522; P:histone H2A ubiquitination; IDA:UniProtKB.
GO; GO:0007141; P:male meiosis I; IMP:MGI.
GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
Gene3D; 3.30.1390.10; -; 1.
InterPro; IPR003769; ClpS_core.
InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
InterPro; IPR039164; UBR1-like.
InterPro; IPR036390; WH_DNA-bd_sf.
InterPro; IPR003126; Znf_UBR.
PANTHER; PTHR21497; PTHR21497; 1.
Pfam; PF02617; ClpS; 1.
Pfam; PF02207; zf-UBR; 1.
SMART; SM00396; ZnF_UBR1; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF54736; SSF54736; 1.
PROSITE; PS51157; ZF_UBR; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Metal-binding; Nucleus; Reference proteome; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8IWV8}.
CHAIN 2 1755 E3 ubiquitin-protein ligase UBR2.
/FTId=PRO_0000056141.
ZN_FING 97 168 UBR-type. {ECO:0000255|PROSITE-
ProRule:PRU00508}.
ZN_FING 1108 1214 RING-type; atypical.
COILED 1019 1054 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8IWV8}.
VAR_SEQ 1 197 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_015172.
VAR_SEQ 397 426 RQLQRDFMEDDHERAVSVTALSVQFFTAPT -> ERLQRDY
VTDDHDREFSVADLSVQIFTVPS (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:14585983,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015173.
CONFLICT 59 59 Q -> L (in Ref. 1; AAQ17202).
{ECO:0000305}.
CONFLICT 137 137 R -> Q (in Ref. 1; AAQ17202 and 3;
BAC65536). {ECO:0000305}.
CONFLICT 143 143 S -> W (in Ref. 1; AAQ17202).
{ECO:0000305}.
CONFLICT 271 271 S -> P (in Ref. 2; AAL32102).
{ECO:0000305}.
CONFLICT 429 435 RMLLTEE -> PNAPHRKK (in Ref. 1;
AAQ17202). {ECO:0000305}.
CONFLICT 656 656 L -> P (in Ref. 1; AAQ17202).
{ECO:0000305}.
CONFLICT 979 979 A -> S (in Ref. 1; AAQ17202).
{ECO:0000305}.
CONFLICT 1050 1050 S -> F (in Ref. 5; BAC38864).
{ECO:0000305}.
CONFLICT 1332 1332 C -> W (in Ref. 1; AAQ17202).
{ECO:0000305}.
CONFLICT 1619 1619 C -> S (in Ref. 4; AAH26391).
{ECO:0000305}.
SEQUENCE 1755 AA; 199155 MW; E6D413D674FBBFDA CRC64;
MASEMEPEVQ AIDRSLLECS AEEIAGRWLQ ATDLNREVYQ HLAHCVPKIY CRGPNPFPQK
EDTLAQHILL GPMEWYICAE DPALGFPKLE QANKPSHLCG RVFKVGEPTY SCRDCAVDPT
CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHKLSS SEVVEEEDPL
VHLSEDVIAR TYNIFAIMFR YAVDILTWEK ESELPEDLEV AEKSDTYYCM LFNDEVHTYE
QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC DQAKTVIVRN TSRQTKPLKV
QVMHSSVAAH QNFGLKALSW LGSVIGYSDG LRRILCQVGL QEGPDGENSS LVDRLMLNDS
KLWKGARSVY HQLFMSSLLM DLKYKKLFAL RFAKNYRQLQ RDFMEDDHER AVSVTALSVQ
FFTAPTLARM LLTEENLMTV IIKAFMDHLK HRDAQGRFQF ERYTALQAFK FRRVQSLILD
LKYVLISKPT EWSDELRQKF LQGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL
QMKLTHVISM VQDWCALDEK VLIEAYKKCL AVLTQCHGGF TDGEQPITLS ICGHSVETIR
YCVSQEKVSI HLPISRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA
QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDIVMLQT GVSMMDPNHF LMIMLSRFEL
YQLFSTPDYG KRFSSEVTHK DVVQQNNTLI EEMLYLIIML VGERFNPGVG QVAATDEIKR
EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIESVAHF KKPGLTGRGM YELKPECAKE
FNLYFYHFSR AEQSKAEEAQ RKLKRENKED TALPPPALPP FCPLFASLVN ILQCDVMLYI
MGTILQWAVE HHGSAWSESM LQRVLHLIGM ALQEEKHHLE NAVEGHVQTF TFTQKISKPG
DAPHNSPSIL AMLETLQNAP SLEAHKDMIR WLLKMFNAIK KIRECSSSSP VAEAEGTIME
ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DTSASATLDS
SPPVSDAALT ALGPAQTQVP EPRQFVTCIL CQEEQEVTVG SRAMVLAAFV QRSTVLSKDR
TKTIADPEKY DPLFMHPDLS CGTHTGSCGH VMHAHCWQRY FDSVQAKEQR RQQRLRLHTS
YDVENGEFLC PLCECLSNTV IPLLLPPRSI LSRRLNFSDQ PDLAQWTRAV TQQIKVVQML
RRKHNAADTS SSEDTEAMNI IPIPEGFRPD FYPRNPYSDS IKEMLTTFGT AAYKVGLKVH
PNEGDPRVPI LCWGTCAYTI QSIERILSDE EKPVFGPLPC RLDDCLRSLT RFAAAHWTVA
LLPVVQGHFC KLFASLVPSD SYEDLPCILD IDMFHLLVGL VLAFPALQCQ DFSGSSLATG
DLHIFHLVTM AHIVQILLTS CTEENGMDQE NPTGEEELAI LSLHKTLHQY TGSALKEAPS
GWHLWRSVRA AIMPFLKCSA LFFHYLNGVP APPDLQVSGT SHFEHLCNYL SLPTNLIHLF
QENSDIMNSL IESWCQNSEV KRYLNGERGA ISYPRGANKL IDLPEDYSSL INQASNFSCP
KSGGDKSRAP TLCLVCGSLL CSQSYCCQAE LEGEDVGACT AHTYSCGSGA GIFLRVRECQ
VLFLAGKTKG CFYSPPYLDD YGETDQGLRR GNPLHLCQER FRKIQKLWQQ HSITEEIGHA
QEANQTLVGI DWQHL


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