UBE4B_MOUSE
ID UBE4B_MOUSE Reviewed; 1173 AA.
AC Q9ES00; Q6DID4; Q9EQE0;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ubiquitin conjugation factor E4 B {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
DE AltName: Full=RING-type E3 ubiquitin transferase E4 B;
DE AltName: Full=Ubiquitin fusion degradation protein 2 {ECO:0000303|PubMed:11027338};
GN Name=Ube4b {ECO:0000312|MGI:MGI:1927086};
GN Synonyms=Ufd2 {ECO:0000312|MGI:MGI:1927086},
GN Ufd2a {ECO:0000312|MGI:MGI:1927086};
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 {ECO:0000312|EMBL:AAG17287.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/Ola; TISSUE=Brain;
RX PubMed=11027338; DOI=10.1073/pnas.97.21.11377;
RA Conforti L., Tarlton A., Mack T.G.A., Mi W., Buckmaster E.A., Wagner D.,
RA Perry V.H., Coleman M.P.;
RT "A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow
RT Wallerian degeneration (WldS) mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11377-11382(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH VCP, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell;
RX PubMed=12504083; DOI=10.1016/s0006-291x(02)02834-6;
RA Kaneko C., Hatakeyama S., Matsumoto M., Yada M., Nakayama K., Nakayama K.;
RT "Characterization of the mouse gene for the U-box-type ubiquitin ligase
RT UFD2a.";
RL Biochem. Biophys. Res. Commun. 300:297-304(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, AND MUTAGENESIS OF PRO-1140.
RX PubMed=11435423; DOI=10.1074/jbc.m102755200;
RA Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
RT "U box proteins as a new family of ubiquitin-protein ligases.";
RL J. Biol. Chem. 276:33111-33120(2001).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND ROLE IN DELAY OF WALLERIAN DEGENERATION.
RX PubMed=11770485; DOI=10.1038/nn770;
RA Mack T.G.A., Reiner M., Beirowski B., Mi W., Emanuelli M., Wagner D.,
RA Thomson D., Gillingwater T., Court F., Conforti L., Fernando F.S.,
RA Tarlton A., Andressen C., Addicks K., Magni G., Ribchester R.R.,
RA Perry V.H., Coleman M.P.;
RT "Wallerian degeneration of injured axons and synapses is delayed by a
RT Ube4b/Nmnat chimeric gene.";
RL Nat. Neurosci. 4:1199-1206(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-88; SER-90; SER-101;
RP SER-103; SER-674 AND SER-840, 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).
CC -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases
CC (PubMed:11435423). May also function as an E4 ligase mediating the
CC assembly of polyubiquitin chains on substrates ubiquitinated by another
CC E3 ubiquitin ligase (By similarity). May regulate myosin assembly in
CC striated muscles together with STUB1 and VCP/p97 by targeting myosin
CC chaperone UNC45B for proteasomal degradation (By similarity).
CC {ECO:0000250|UniProtKB:O95155, ECO:0000250|UniProtKB:P54860,
CC ECO:0000269|PubMed:11435423}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11435423};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11435423}.
CC -!- SUBUNIT: Interacts with VCP (PubMed:12504083). Interacts with
CC STUB1/CHIP and UNC45B (By similarity). {ECO:0000250|UniProtKB:O95155,
CC ECO:0000269|PubMed:12504083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11435423,
CC ECO:0000269|PubMed:11770485, ECO:0000269|PubMed:12504083}. Nucleus
CC {ECO:0000269|PubMed:11435423}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in neuronal tissues. Also
CC detected in liver, heart, brain, kidney and testis.
CC {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12504083}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000269|PubMed:11435423}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. Cleaved
CC efficiently at Asp-123 by caspase-6 and granzyme B. Cleaved with
CC approximately 10-fold less efficiency at Asp-109 by caspase-3 and
CC caspase-7 (By similarity). {ECO:0000250|UniProtKB:O95155}.
CC -!- MISCELLANEOUS: In strain C57BL/Ola, a 85 kb region on chromosome 4
CC containing Nmnat1 and Ube4b is triplicated. Ube4b becomes linked to
CC Nmnat1 and encodes a fusion protein located in the nucleus which is
CC responsible for the delayed Wallerian degeneration of injured axons in
CC C57BL/Ola. {ECO:0000269|PubMed:11770485}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000305}.
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DR EMBL; AF260924; AAG17285.1; ALT_TERM; mRNA.
DR EMBL; AF260926; AAG17287.1; -; mRNA.
DR EMBL; AF260927; AAG38492.1; -; Genomic_DNA.
DR EMBL; AB083274; BAC56586.1; -; Genomic_DNA.
DR EMBL; AK029914; BAC26672.1; -; mRNA.
DR EMBL; AL606973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075620; AAH75620.1; -; mRNA.
DR CCDS; CCDS18958.1; -.
DR RefSeq; NP_071305.2; NM_022022.3.
DR PDB; 2KR4; NMR; -; A=1092-1173.
DR PDBsum; 2KR4; -.
DR AlphaFoldDB; Q9ES00; -.
DR BMRB; Q9ES00; -.
DR SMR; Q9ES00; -.
DR BioGRID; 211009; 19.
DR IntAct; Q9ES00; 2.
DR STRING; 10090.ENSMUSP00000099501; -.
DR iPTMnet; Q9ES00; -.
DR PhosphoSitePlus; Q9ES00; -.
DR EPD; Q9ES00; -.
DR jPOST; Q9ES00; -.
DR MaxQB; Q9ES00; -.
DR PaxDb; Q9ES00; -.
DR PeptideAtlas; Q9ES00; -.
DR PRIDE; Q9ES00; -.
DR ProteomicsDB; 298448; -.
DR Antibodypedia; 13520; 186 antibodies from 31 providers.
DR DNASU; 63958; -.
DR Ensembl; ENSMUST00000103212; ENSMUSP00000099501; ENSMUSG00000028960.
DR GeneID; 63958; -.
DR KEGG; mmu:63958; -.
DR UCSC; uc012dpr.1; mouse.
DR CTD; 10277; -.
DR MGI; MGI:1927086; Ube4b.
DR VEuPathDB; HostDB:ENSMUSG00000028960; -.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00390000009300; -.
DR HOGENOM; CLU_003224_2_0_1; -.
DR InParanoid; Q9ES00; -.
DR OMA; LRWELHS; -.
DR OrthoDB; 194967at2759; -.
DR PhylomeDB; Q9ES00; -.
DR TreeFam; TF300802; -.
DR BRENDA; 2.3.2.B12; 3474.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 63958; 16 hits in 76 CRISPR screens.
DR ChiTaRS; Ube4b; mouse.
DR PRO; PR:Q9ES00; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9ES00; protein.
DR Bgee; ENSMUSG00000028960; Expressed in embryonic post-anal tail and 275 other tissues.
DR ExpressionAtlas; Q9ES00; baseline and differential.
DR Genevisible; Q9ES00; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931; PTHR13931; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1173
FT /note="Ubiquitin conjugation factor E4 B"
FT /id="PRO_0000194994"
FT DOMAIN 1098..1171
FT /note="U-box"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 109..110
FT /note="Cleavage; by caspase-3 and caspase-7"
FT /evidence="ECO:0000250"
FT SITE 123..124
FT /note="Cleavage; by caspase-6 and granzyme B"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95155"
FT MUTAGEN 1140
FT /note="P->A: Loss of E3 ubiquitin protein ligase activity."
FT /evidence="ECO:0000269|PubMed:11435423"
FT CONFLICT 298
FT /note="L -> P (in Ref. 1; AAG17287)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="E -> D (in Ref. 1; AAG17287 and 2; BAC56586)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="S -> T (in Ref. 3; BAC26672)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="C -> Y (in Ref. 1; AAG17287)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="E -> K (in Ref. 3; BAC26672)"
FT /evidence="ECO:0000305"
FT TURN 1101..1103
FT /evidence="ECO:0007829|PDB:2KR4"
FT TURN 1106..1108
FT /evidence="ECO:0007829|PDB:2KR4"
FT STRAND 1113..1117
FT /evidence="ECO:0007829|PDB:2KR4"
FT STRAND 1123..1125
FT /evidence="ECO:0007829|PDB:2KR4"
FT HELIX 1126..1135
FT /evidence="ECO:0007829|PDB:2KR4"
FT TURN 1140..1142
FT /evidence="ECO:0007829|PDB:2KR4"
FT HELIX 1148..1150
FT /evidence="ECO:0007829|PDB:2KR4"
FT HELIX 1155..1170
FT /evidence="ECO:0007829|PDB:2KR4"
SQ SEQUENCE 1173 AA; 133318 MW; FC4879E47672E983 CRC64;
MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS QSLGLNVHNM
TPATSPIGAA GVAHRSQSSE GVSSLSSSPS NSLETQSQSL SRSQSMDIDG VSCEKSMSQV
DVDSGIENME VDENDRREKR SLSDKEPSSG PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL
SSLSAQFKQN PKEVFSDFKD LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIATAARSPD
RNLMLNTGSS SGTSPMFCNM GSFSTSSLSS LGASGGASNW DSYSDHFTIE TCKETDMLNY
LIECFDRVGI EEKKAPKMCS QPAVSQLLSN IRSQCISHTA LVLQGSLTQP RSLQQPSFLV
PYMLCRNLPY GFIQELVRTT HQDEEVFKQI FIPILQGLAL AAKECSLESD YFKYPLMALG
ELCETKFGKT HPMCNLVASL PLWLPKSLSP GSGRELQRLS YLGAFFSFSV FAEDDAKVVE
KYFSGPAITL ENTRVVSQSL QHYLELGRQE LFKILHSILL NGETREAALS YMAALVNANM
KKAQMQADDR LVSTDGFMLN LLWVLQQLST KIKLETVDPT YIFHPRCRIT LPNDETRINA
TMEDVNERLT ELYGDQPPFS EPKFPTECFF LTLHAHHLSI LPSCRRYIRR LRAIRELNRT
VEDLKNNESQ WKDSPLATRH REMLKRCKTQ LKKLVRCKAC ADAGLLDESF LRRCLNFYGL
LIQLMLRILD PAYPDVTLPL NSEVPKVFAA LPEFYVEDVA EFLFFIVQYS PQVLYEPCTQ
DIVMFLVVML CNQNYIRNPY LVAKLVEVMF MTNPSVQPRT QKFFEMIENH PLSTKLLVPS
LMKFYTDVEH TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM
LINDTTFLLD ESLESLKRIH EVQEEMKNKE QWDQLPRDQQ QARQSQLAQD ERVSRSYLAL
ATETVDMFHL LTKQVQKPFL RPELGPRLAA MLNFNLQQLC GPKCRDLKVE NPEKYGFEPK
KLLDQLTDIY LQLDCARFAK AIADDQRSYS KELFEEVISK MRKAGIKSTI AIEKFKLLAE
KVEEIVAKNA RAEIDYSDAP DEFRDPLMDT LMTDPVRLPS GTVMDRSIIL RHLLNSPTDP
FNRQMLTESM LEPVPELKEQ IQAWMREKQS SDH
