SYCP2_MOUSE
ID SYCP2_MOUSE Reviewed; 1500 AA.
AC Q9CUU3; A2AJW2; Q1G7B6;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Synaptonemal complex protein 2;
DE Short=SCP-2;
DE AltName: Full=Synaptonemal complex lateral element protein;
GN Name=Sycp2; Synonyms=Scp2;
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 [MRNA], FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE,
RP INTERACTION WITH SYCP3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16717126; DOI=10.1083/jcb.200603063;
RA Yang F., De La Fuente R., Leu N.A., Baumann C., McLaughlin K.J., Wang P.J.;
RT "Mouse SYCP2 is required for synaptonemal complex assembly and chromosomal
RT synapsis during male meiosis.";
RL J. Cell Biol. 173:497-507(2006).
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 [LARGE SCALE MRNA] OF 1-544.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 FUNCTION.
RX PubMed=11463847; DOI=10.1128/mcb.21.16.5667-5677.2001;
RA Pelttari J., Hoja M.-R., Yuan L., Liu J.-G., Brundell E., Moens P.,
RA Santucci-Darmanin S., Jessberger R., Barbero J.L., Heyting C., Hoeoeg C.;
RT "A meiotic chromosomal core consisting of cohesin complex proteins recruits
RT DNA recombination proteins and promotes synapsis in the absence of an axial
RT element in mammalian meiotic cells.";
RL Mol. Cell. Biol. 21:5667-5677(2001).
RN [5]
RP INTERACTION WITH TEX11.
RX PubMed=18316482; DOI=10.1101/gad.1613608;
RA Yang F., Gell K., van der Heijden G.W., Eckardt S., Leu N.A., Page D.C.,
RA Benavente R., Her C., Hoog C., McLaughlin K.J., Wang P.J.;
RT "Meiotic failure in male mice lacking an X-linked factor.";
RL Genes Dev. 22:682-691(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-458; THR-464;
RP SER-487; THR-496; SER-500; SER-509; SER-518; SER-527; THR-608; THR-633;
RP SER-650; SER-741; SER-914; THR-916; SER-1115; SER-1117; SER-1124; SER-1133;
RP SER-1140; SER-1144; SER-1156; SER-1159; SER-1164; THR-1168; SER-1183;
RP SER-1275; SER-1277 AND THR-1313, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D.,
RA Hoeoeg C.;
RT "Phosphorylation of chromosome core components may serve as axis marks for
RT the status of chromosomal events during mammalian meiosis.";
RL PLoS Genet. 8:E1002485-E1002485(2012).
CC -!- FUNCTION: Major component of the axial/lateral elements of synaptonemal
CC complexes (SCS) during meiotic prophase. Plays a role in the assembly
CC of synaptonemal complexes (PubMed:16717126). Required for normal
CC meiotic chromosome synapsis during oocyte and spermatocyte development
CC and for normal male and female fertility (PubMed:16717126). Required
CC for insertion of SYCP3 into synaptonemal complexes (PubMed:16717126).
CC May be involved in the organization of chromatin by temporarily binding
CC to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in
CC order to be incorporated into the axial/lateral elements.
CC {ECO:0000269|PubMed:11463847, ECO:0000269|PubMed:16717126}.
CC -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC (PubMed:16717126). Heterodimer with SYCP3 (PubMed:16717126). Interacts
CC with SMC1A and SMC3 (By similarity). Interacts with TEX11
CC (PubMed:18316482). {ECO:0000250|UniProtKB:O70608,
CC ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:18316482}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16717126}. Chromosome
CC {ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22346761}. Note=In
CC axial/lateral elements of the tripartite segments of synaptonemal
CC complexes. {ECO:0000269|PubMed:16717126}.
CC -!- TISSUE SPECIFICITY: Detected in testis and spermatocytes (at protein
CC level). {ECO:0000269|PubMed:16717126}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}.
CC -!- DISRUPTION PHENOTYPE: Mice appear healthy, but males are completely
CC sterile, due to defective meiotic chromosome synapsis during
CC spermatocyte development. Testes weight is much reduced in mutant mice.
CC Females display reduced fertility. {ECO:0000269|PubMed:16717126}.
CC -!- SIMILARITY: Belongs to the SYCP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK014411; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; DQ103262; AAZ80470.1; -; mRNA.
DR EMBL; AL772217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK014411; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS38370.1; -.
DR RefSeq; NP_796165.2; NM_177191.3.
DR RefSeq; XP_017174510.1; XM_017319021.1.
DR PDB; 5IWZ; X-ray; 2.10 A; A=1-390.
DR PDBsum; 5IWZ; -.
DR AlphaFoldDB; Q9CUU3; -.
DR SMR; Q9CUU3; -.
DR BioGRID; 236115; 3.
DR CORUM; Q9CUU3; -.
DR IntAct; Q9CUU3; 1.
DR MINT; Q9CUU3; -.
DR STRING; 10090.ENSMUSP00000079909; -.
DR iPTMnet; Q9CUU3; -.
DR PhosphoSitePlus; Q9CUU3; -.
DR PaxDb; Q9CUU3; -.
DR PRIDE; Q9CUU3; -.
DR ProteomicsDB; 254504; -.
DR Antibodypedia; 58383; 94 antibodies from 18 providers.
DR DNASU; 320558; -.
DR Ensembl; ENSMUST00000081134; ENSMUSP00000079909; ENSMUSG00000060445.
DR GeneID; 320558; -.
DR KEGG; mmu:320558; -.
DR UCSC; uc008ohn.1; mouse.
DR CTD; 10388; -.
DR MGI; MGI:1933281; Sycp2.
DR VEuPathDB; HostDB:ENSMUSG00000060445; -.
DR eggNOG; ENOG502QVM5; Eukaryota.
DR GeneTree; ENSGT00530000063859; -.
DR HOGENOM; CLU_004101_0_0_1; -.
DR InParanoid; Q9CUU3; -.
DR OMA; MAHERNV; -.
DR OrthoDB; 285929at2759; -.
DR PhylomeDB; Q9CUU3; -.
DR TreeFam; TF332368; -.
DR BioGRID-ORCS; 320558; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Scp2; mouse.
DR PRO; PR:Q9CUU3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CUU3; protein.
DR Bgee; ENSMUSG00000060445; Expressed in spermatocyte and 36 other tissues.
DR ExpressionAtlas; Q9CUU3; baseline and differential.
DR Genevisible; Q9CUU3; MM.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0048808; P:male genitalia morphogenesis; IMP:MGI.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
DR GO; GO:0140013; P:meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI.
DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI.
DR InterPro; IPR024832; SYCP2.
DR InterPro; IPR024835; SYCP2-like.
DR InterPro; IPR041322; SYCP2_ARLD.
DR InterPro; IPR040560; SYCP2_SLD.
DR PANTHER; PTHR15607; PTHR15607; 1.
DR PANTHER; PTHR15607:SF12; PTHR15607:SF12; 1.
DR Pfam; PF18581; SYCP2_ARLD; 1.
DR Pfam; PF18584; SYCP2_SLD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA-binding; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1500
FT /note="Synaptonemal complex protein 2"
FT /id="PRO_0000072367"
FT REGION 512..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1388..1429
FT /evidence="ECO:0000255"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 633
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 916
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1168
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 1216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 1232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 166..182
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 194..209
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:5IWZ"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 349..362
FT /evidence="ECO:0007829|PDB:5IWZ"
FT STRAND 365..375
FT /evidence="ECO:0007829|PDB:5IWZ"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:5IWZ"
SQ SEQUENCE 1500 AA; 172123 MW; 3706CF5214C51829 CRC64;
MPVRPDLQQL EKCIDDALRK NDFKPLLALL QIDICEDVKI KCSKQFLRKL DDLICRELNK
KDIQTVSSIL ISIGRCSKNI FILGQAGLQT MIKQGLVQKM VSWFENSKEI ILNQQQSKDE
AVMNMIEDLF DLLMVIYDIS DEGKNQVLES FIPQICALVI DSRVNFCIQQ EALKKMNLML
DRIPQDANKI LSNQEMLTLM SNMGERILDV GDYELQVGIV EALCRMTTEK RRQELAYEWF
SMDFIANAFK EIKDCEFETD CRIFLNLVNG ILGDKRRVYT FPCLSAFLGK YELQIPSDEK
LEEFWIDFNL GSHTLSFYIA GDEEDHQWEA VTVPEEKVQM YNIEVRESKK LLTLTLKNIV
KISKKEGKEL LFYFDESLEI TNVTKKVFGG NKYKEFTRKQ GISVAKTSIH VLFDASGSQI
LVPESQPSPV KENLIHLKEK SDIQKKLVNP LELGNSSSQD EITTPSRKKM SEASMIVPDT
DRYTVRSPIL LINTSTPRRS REPLQAINSV EKAVSKTSES GMDYAASPKS RQSDGRKRWN
NRANHNKTTA VIQNKQYEDN ESPDQNFNEI EDTLSNVSSA VGKVDKPVLP GVLDISKNTT
HSRWACWTPV TTIKLCNNQR SRALPGDTCT QDTGVNKKCT KQKSVSDDDS EETQKGKYSK
DVIKCNKSDE AEFCERNIQE QNHPKYSQKK NTANAKKSDW HIESETTYKS VLLNKTTEES
LIYKKTCVLS KDVNTTICDK SPSRKSKRNH TKSRKELMSE LTSCELEEIP VRENSKGKRF
TGASESLINQ ISRRYNPSDS MMSTRKLKEP QDGSGFSKKP DLQFNKVQRK SYRKLKATVV
NVTSECPLDD VYNFSLNGAD EPVIKLGIQE FQATTREASM DNSLKLVKNH DEHDPFLKTK
DKRMLSYEKK TLLSDTETEC GCDDSKTDIS WLKEPKTKRL MDYSRNKNTT KYKSRKSRSS
MEKGQPRPTM VLNKNSMKND YEVVVDGRTR LPRRATKTKK NYKDLSTSES ESESEKECSY
LFKDKLPTKE ETIHSRAQTK KLPEKQQKVF NSEALKGQPS EEQKNSSRLR EGREDSLCLS
SASVSRSSSS VEVMRCTEKI TERDFTQDYD YITKSLSPYP KAPSPEFLNG NNSVVGRGQS
PRISETSAMC VRKSYSPASG PPFSPRHTPT KNNSVVNMKK ANSVINNQRT QHCNSYSDVS
SNSSEKLYME PESPESCDNH MQNKREGNHA ASPLSLSSEK IEKMWFDMPS ENTHVSGPSQ
RGSKRRMYLE DDELSNSNEA EVEEAEEREH LLSKKRCQWE NSDQHTFKTS LSTPDFSVPK
DWQQELQGAG MFYDNISSDY KRKTDSQHKI MDDFTTKTLK LTQQHLMAMT SQAQGRRDEN
VEKFQVTLLD ELEKVEKDSQ TLRDLEKELV DIEEKLVQKM RAYHRCERER FRVLKTSLDK
SFLVYNSVYE ESVFTSEMCL MKANMKMLQD KLLKEMHEEE VLNIRRGLQS LFKAHEGNDA
