MPP10_HUMAN
ID MPP10_HUMAN Reviewed; 681 AA.
AC O00566; A0AVJ8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=U3 small nucleolar ribonucleoprotein protein MPP10;
DE AltName: Full=M phase phosphoprotein 10;
GN Name=MPHOSPH10; Synonyms=MPP10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-681.
RC TISSUE=Blood;
RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Mammary cancer, and Placenta;
RX PubMed=9450966; DOI=10.1091/mbc.9.2.437;
RA Westendorf J.M., Konstantinov K.N., Wormsley S., Shu M.-D.,
RA Matsumoto-Taniura N., Pirollet F., Klier F.G., Gerace L., Baserga S.J.;
RT "M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein
RT component.";
RL Mol. Biol. Cell 9:437-449(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IMP3 AND IMP4.
RX PubMed=12655004; DOI=10.1093/nar/gkg300;
RA Granneman S., Gallagher J.E.G., Vogelzangs J., Horstman W.,
RA van Venrooij W.J., Baserga S.J., Pruijn G.J.M.;
RT "The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which
RT only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes.";
RL Nucleic Acids Res. 31:1877-1887(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-171;
RP SER-242; SER-275 AND SER-289, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-171 AND
RP SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-171 AND SER-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-139; SER-163;
RP SER-167; SER-171 AND SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-139; SER-163;
RP SER-167; SER-171; SER-242; SER-275 AND SER-289, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167 AND SER-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-382 AND LYS-632, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-632, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350; LYS-382; LYS-394; LYS-555;
RP LYS-632 AND LYS-649, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein
CC (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal
CC RNA processing.
CC -!- SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4
CC and MPHOSPH10. Interacts with IMP3 and IMP4.
CC {ECO:0000269|PubMed:12655004}.
CC -!- INTERACTION:
CC O00566; Q13895: BYSL; NbExp=3; IntAct=EBI-5235884, EBI-358049;
CC O00566; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-5235884, EBI-11962928;
CC O00566; Q9NV31: IMP3; NbExp=2; IntAct=EBI-5235884, EBI-747481;
CC O00566; Q96G21: IMP4; NbExp=2; IntAct=EBI-5235884, EBI-8641721;
CC O00566; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-5235884, EBI-10288852;
CC O00566; P62136: PPP1CA; NbExp=2; IntAct=EBI-5235884, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:9450966}. Chromosome
CC {ECO:0000269|PubMed:9450966}. Note=Fibrillar region of the nucleolus
CC (PubMed:9450966). After dissolution of the nucleolus in early M phase
CC becomes associated with chromosomes through metaphase and anaphase
CC (PubMed:9450966). In telophase localized to small cellular prenucleolar
CC bodies that not always contain fibrillarin (PubMed:9450966). The
CC reassociation with nucleolus is preceeded by the arrival of fibrillarin
CC (PubMed:9450966). {ECO:0000269|PubMed:9450966}.
CC -!- PTM: Phosphorylated in M (mitotic) phase.
CC -!- SIMILARITY: Belongs to the MPP10 family. {ECO:0000305}.
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DR EMBL; X98494; CAA67120.1; -; mRNA.
DR EMBL; BC126389; AAI26390.1; -; mRNA.
DR CCDS; CCDS1916.1; -.
DR RefSeq; NP_005782.1; NM_005791.2.
DR PDB; 7MQ8; EM; 3.60 A; NA=1-681.
DR PDB; 7MQ9; EM; 3.87 A; NA=1-681.
DR PDB; 7MQA; EM; 2.70 A; NA=1-681.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; O00566; -.
DR SMR; O00566; -.
DR BioGRID; 115494; 178.
DR ComplexPortal; CPX-2478; MPP10 complex.
DR CORUM; O00566; -.
DR IntAct; O00566; 35.
DR MINT; O00566; -.
DR STRING; 9606.ENSP00000244230; -.
DR iPTMnet; O00566; -.
DR PhosphoSitePlus; O00566; -.
DR SwissPalm; O00566; -.
DR BioMuta; MPHOSPH10; -.
DR SWISS-2DPAGE; O00566; -.
DR EPD; O00566; -.
DR jPOST; O00566; -.
DR MassIVE; O00566; -.
DR MaxQB; O00566; -.
DR PaxDb; O00566; -.
DR PeptideAtlas; O00566; -.
DR PRIDE; O00566; -.
DR ProteomicsDB; 47979; -.
DR Antibodypedia; 31197; 140 antibodies from 24 providers.
DR DNASU; 10199; -.
DR Ensembl; ENST00000244230.7; ENSP00000244230.2; ENSG00000124383.9.
DR GeneID; 10199; -.
DR KEGG; hsa:10199; -.
DR MANE-Select; ENST00000244230.7; ENSP00000244230.2; NM_005791.3; NP_005782.1.
DR UCSC; uc002sht.3; human.
DR CTD; 10199; -.
DR DisGeNET; 10199; -.
DR GeneCards; MPHOSPH10; -.
DR HGNC; HGNC:7213; MPHOSPH10.
DR HPA; ENSG00000124383; Low tissue specificity.
DR MIM; 605503; gene.
DR neXtProt; NX_O00566; -.
DR OpenTargets; ENSG00000124383; -.
DR PharmGKB; PA30919; -.
DR VEuPathDB; HostDB:ENSG00000124383; -.
DR eggNOG; KOG2600; Eukaryota.
DR GeneTree; ENSGT00390000011359; -.
DR HOGENOM; CLU_011271_3_1_1; -.
DR InParanoid; O00566; -.
DR OMA; HFAEDFG; -.
DR OrthoDB; 435993at2759; -.
DR PhylomeDB; O00566; -.
DR TreeFam; TF105794; -.
DR PathwayCommons; O00566; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; O00566; -.
DR SIGNOR; O00566; -.
DR BioGRID-ORCS; 10199; 720 hits in 1085 CRISPR screens.
DR ChiTaRS; MPHOSPH10; human.
DR GeneWiki; MPHOSPH10; -.
DR GenomeRNAi; 10199; -.
DR Pharos; O00566; Tbio.
DR PRO; PR:O00566; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00566; protein.
DR Bgee; ENSG00000124383; Expressed in calcaneal tendon and 210 other tissues.
DR ExpressionAtlas; O00566; baseline and differential.
DR Genevisible; O00566; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0034457; C:Mpp10 complex; IPI:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; NAS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; NAS:UniProtKB.
DR InterPro; IPR012173; Mpp10.
DR PANTHER; PTHR17039; PTHR17039; 1.
DR Pfam; PF04006; Mpp10; 1.
DR PIRSF; PIRSF017300; snoRNP_Mpp10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Coiled coil; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT CHAIN 1..681
FT /note="U3 small nucleolar ribonucleoprotein protein MPP10"
FT /id="PRO_0000121535"
FT REGION 105..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..138
FT /evidence="ECO:0000255"
FT COILED 205..239
FT /evidence="ECO:0000255"
FT COILED 284..324
FT /evidence="ECO:0000255"
FT COILED 348..382
FT /evidence="ECO:0000255"
FT COILED 469..490
FT /evidence="ECO:0000255"
FT COILED 574..604
FT /evidence="ECO:0000255"
FT COILED 648..670
FT /evidence="ECO:0000255"
FT COMPBIAS 105..143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..592
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 382
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 394
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 69
FT /note="E -> A (in dbSNP:rs10199088)"
FT /id="VAR_053511"
FT VARIANT 115
FT /note="R -> H (in dbSNP:rs13010513)"
FT /id="VAR_053512"
FT VARIANT 140
FT /note="D -> N (in dbSNP:rs10175940)"
FT /id="VAR_053513"
FT VARIANT 229
FT /note="E -> D (in dbSNP:rs1813160)"
FT /id="VAR_024539"
FT VARIANT 425
FT /note="L -> M (in dbSNP:rs3732240)"
FT /id="VAR_022000"
FT VARIANT 634
FT /note="E -> K (in dbSNP:rs6574)"
FT /id="VAR_014470"
FT VARIANT 639
FT /note="A -> T (in dbSNP:rs4852764)"
FT /id="VAR_053514"
SQ SEQUENCE 681 AA; 78864 MW; EDF27859D735D4E2 CRC64;
MAPQVWRRRT LERCLTEVGK ATGRPECFLT IQEGLASKFT SLTKVLYDFN KILENGRIHG
SPLQKLVIEN FDDEQIWQQL ELQNEPILQY FQNAVSETIN DEDISLLPES EEQEREEDGS
EIEADDKEDL EDLEEEEVSD MGNDDPEMGE RAENSSKSDL RKSPVFSDED SDLDFDISKL
EQQSKVQNKG QGKPREKSIV DDKFFKLSEM EAYLENIEKE EERKDDNDEE EEDIDFFEDI
DSDEDEGGLF GSKKLKSGKS SRNLKYKDFF DPVESDEDIT NVHDDELDSN KEDDEIAEEE
AEELSISETD EDDDLQENED NKQHKESLKR VTFALPDDAE TEDTGVLNVK KNSDEVKSSF
EKRQEKMNEK IASLEKELLE KKPWQLQGEV TAQKRPENSL LEETLHFDHA VRMAPVITEE
TTLQLEDIIK QRIRDQAWDD VVRKEKPKED AYEYKKRLTL DHEKSKLSLA EIYEQEYIKL
NQQKTAEEEN PEHVEIQKMM DSLFLKLDAL SNFHFIPKPP VPEIKVVSNL PAITMEEVAP
VSVSDAALLA PEEIKEKNKA GDIKTAAEKT ATDKKRERRK KKYQKRMKIK EKEKRRKLLE
KSSVDQAGKY SKTVASEKLK QLTKTGKASF IKDEGKDKAL KSSQAFFSKL QDQVKMQIND
AKKTEKKKKK RQDISVHKLK L
