UBE2O_MOUSE
ID UBE2O_MOUSE Reviewed; 1288 AA.
AC Q6ZPJ3; A2A7X3; Q60800; Q6PCR9; Q7TPN2; Q8BLE8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme UBE2O;
DE EC=2.3.2.24;
DE AltName: Full=E2/E3 hybrid ubiquitin-protein ligase UBE2O;
DE AltName: Full=Ubiquitin carrier protein O;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 O;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 of 230 kDa;
DE Short=Ubiquitin-conjugating enzyme E2-230K;
DE AltName: Full=Ubiquitin-protein ligase O;
GN Name=Ube2o; Synonyms=Kiaa1734;
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 MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-628, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Reticulocyte;
RX PubMed=7761435; DOI=10.1073/pnas.92.11.4982;
RA Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J.,
RA Pickart C.M., Finley D.;
RT "Induction of ubiquitin-conjugating enzymes during terminal erythroid
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1288.
RC STRAIN=FVB/N; TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 867-1288.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=8634298; DOI=10.1021/bi952105y;
RA Berleth E.S., Pickart C.M.;
RT "Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis involving a
RT thiol relay?";
RL Biochemistry 35:1664-1671(1996).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND
RP SER-836, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-394; SER-436;
RP SER-833; THR-835 AND SER-836, 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 [11]
RP INTERACTION WITH UBR2.
RX PubMed=31268597; DOI=10.15252/embj.2019101996;
RA Xu H., Shi J., Gao H., Liu Y., Yang Z., Shao F., Dong N.;
RT "The N-end rule ubiquitin ligase UBR2 mediates NLRP1B inflammasome
RT activation by anthrax lethal toxin.";
RL EMBO J. 38:e101996-e101996(2019).
CC -!- FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both E2
CC and E3 ligase activities and mediates monoubiquitination of target
CC proteins. Negatively regulates TRAF6-mediated NF-kappa-B activation
CC independently of its E2 activity. Acts as a positive regulator of BMP7
CC signaling by mediating monoubiquitination of SMAD6, thereby regulating
CC adipogenesis. Mediates monoubiquitination at different sites of the
CC nuclear localization signal (NLS) of BAP1, leading to cytoplasmic
CC retention of BAP1. Also able to monoubiquitinate the NLS of other
CC chromatin-associated proteins, such as INO80 and CXXC1, affecting their
CC subcellular location. Acts as a regulator of retrograde transport by
CC assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate
CC 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal
CC F-actin assembly. {ECO:0000250|UniProtKB:Q9C0C9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:Q9C0C9,
CC ECO:0000255|PROSITE-ProRule:PRU00388};
CC -!- ACTIVITY REGULATION: Inhibited by inorganic arsenite such as
CC phenylarsenoxides. {ECO:0000269|PubMed:8634298}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA
CC domain) (PubMed:12522145). Interacts with UBR2 (PubMed:31268597).
CC {ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:31268597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0C9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9C0C9}. Note=Mainly localizes to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q9C0C9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in reticulocytes.
CC {ECO:0000269|PubMed:7761435}.
CC -!- INDUCTION: By EPO/Erythropoietin which induces erythroid
CC differentiation. {ECO:0000269|PubMed:7761435}.
CC -!- PTM: Phosphorylated. Phosphorylation affects subcellular location.
CC {ECO:0000250|UniProtKB:Q9C0C9}.
CC -!- PTM: Ubiquitinated: autoubiquitinates, possibly affecting its
CC subcellular location. {ECO:0000250|UniProtKB:Q9C0C9}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69916.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH59193.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC32345.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98241.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129431; BAC98241.1; ALT_INIT; mRNA.
DR EMBL; AL607039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U20780; AAA69916.1; ALT_FRAME; mRNA.
DR EMBL; BC059193; AAH59193.1; ALT_INIT; mRNA.
DR EMBL; AK045398; BAC32345.1; ALT_INIT; mRNA.
DR CCDS; CCDS25670.1; -.
DR PIR; I49264; I49264.
DR RefSeq; NP_776116.2; NM_173755.3.
DR AlphaFoldDB; Q6ZPJ3; -.
DR SMR; Q6ZPJ3; -.
DR BioGRID; 229895; 15.
DR IntAct; Q6ZPJ3; 5.
DR MINT; Q6ZPJ3; -.
DR STRING; 10090.ENSMUSP00000080791; -.
DR iPTMnet; Q6ZPJ3; -.
DR PhosphoSitePlus; Q6ZPJ3; -.
DR SwissPalm; Q6ZPJ3; -.
DR EPD; Q6ZPJ3; -.
DR jPOST; Q6ZPJ3; -.
DR MaxQB; Q6ZPJ3; -.
DR PaxDb; Q6ZPJ3; -.
DR PeptideAtlas; Q6ZPJ3; -.
DR PRIDE; Q6ZPJ3; -.
DR ProteomicsDB; 298182; -.
DR Antibodypedia; 32408; 171 antibodies from 36 providers.
DR DNASU; 217342; -.
DR Ensembl; ENSMUST00000082152; ENSMUSP00000080791; ENSMUSG00000020802.
DR GeneID; 217342; -.
DR KEGG; mmu:217342; -.
DR UCSC; uc007mlm.1; mouse.
DR CTD; 63893; -.
DR MGI; MGI:2444266; Ube2o.
DR VEuPathDB; HostDB:ENSMUSG00000020802; -.
DR eggNOG; KOG0895; Eukaryota.
DR GeneTree; ENSGT00940000160755; -.
DR HOGENOM; CLU_002088_1_0_1; -.
DR InParanoid; Q6ZPJ3; -.
DR OMA; KDHSDYQ; -.
DR OrthoDB; 808738at2759; -.
DR PhylomeDB; Q6ZPJ3; -.
DR TreeFam; TF325556; -.
DR BRENDA; 2.3.2.25; 3474.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 217342; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Ube2o; mouse.
DR PRO; PR:Q6ZPJ3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6ZPJ3; protein.
DR Bgee; ENSMUSG00000020802; Expressed in blood and 227 other tissues.
DR Genevisible; Q6ZPJ3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..1288
FT /note="(E3-independent) E2 ubiquitin-conjugating enzyme
FT UBE2O"
FT /id="PRO_0000280638"
FT DOMAIN 950..1110
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 809..879
FT /evidence="ECO:0000255"
FT COMPBIAS 402..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1037
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 835
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT CONFLICT 309
FT /note="C -> S (in Ref. 3; AAA69916)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..319
FT /note="SPP -> CPR (in Ref. 3; AAA69916)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="Q -> H (in Ref. 3; AAA69916)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="A -> G (in Ref. 4; BAC32345)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160
FT /note="L -> P (in Ref. 1; BAC98241 and 4; AAH59193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1288 AA; 140834 MW; D2BCE5F36A687CE1 CRC64;
MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG SQRLLFSHDL
VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG GAGHEEGRAS PLRRGYVRVQ
WYPEGVKQHV KETKLKLEDR SVVPRDVVRH MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY
PVNSKDLQHI WPFMYGDYIA YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP
HVSDSGLFFD DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK
VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY VFPAKVEPAK
IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ CPRDHSMEDP DKKGEARAGS
EIGSASPEEQ PDGSASPVEM QDEGSEELQE TCEPLPPFLL KEGGDDGLHS AEQDADDEAA
DDTDDTSSVT SSASSTTSSQ SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA
VEVVTTMTSA DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG
VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT TDIVIRIGNT
EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ HLYNIESEIE ESDYDSVEGS
SSGASSDEWE DDSDSWETDN GLVDDEHPKI EELAAILPAE QPTAPEEDKG VVISEEAATA
AIQGAVAMAA PVAGLMEKAG KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE
PEKPTREKKF LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP
SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK FFSTVRKEMA
LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL FDIQLPNIYP AVPPHFCYLS
QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG
FDSDRGLQEG YENSRCYNEM ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE
SWLETHAMQE RAQVMPNGAL KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG
GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI GFPLFPLSKG
FIKSIRGVLT QFRAALLEAG MPESTEDK
