ID PUM2_MOUSE Reviewed; 1066 AA. AC Q80U58; Q80UZ9; Q91YW4; Q925A0; Q9ERC7; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 02-FEB-2004, sequence version 2. DT 12-AUG-2020, entry version 150. DE RecName: Full=Pumilio homolog 2; GN Name=Pum2; Synonyms=Kiaa0235; 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] (ISOFORM 1), RNA-BINDING, AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=11780640; RA White E.K., Moore-Jarrett T., Ruley H.E.; RT "PUM2, a novel murine puf protein, and its consensus RNA-binding site."; RL RNA 7:1855-1866(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=12667987; DOI=10.1016/s1079-9796(03)00003-2; RA Spassov D.S., Jurecic R.; RT "Mouse Pum1 and Pum2 genes, members of the Pumilio family of RNA-binding RT proteins, show differential expression in fetal and adult hematopoietic RT stem cells and progenitors."; RL Blood Cells Mol. Dis. 30:55-69(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II. RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Mammary tumor; 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 INTERACTION WITH NANOS3, AND TISSUE SPECIFICITY. RX PubMed=18089289; DOI=10.1016/j.ydbio.2007.11.011; RA Lolicato F., Marino R., Paronetto M.P., Pellegrini M., Dolci S., RA Geremia R., Grimaldi P.; RT "Potential role of Nanos3 in maintaining the undifferentiated spermatogonia RT population."; RL Dev. Biol. 313:725-738(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-136 AND SER-587, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Lung, 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 [8] RP SUBCELLULAR LOCATION. RX PubMed=19861488; DOI=10.1530/rep-09-0373; RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.; RT "Functional reconstruction of NANOS3 expression in the germ cell lineage by RT a novel transgenic reporter reveals distinct subcellular localizations of RT NANOS3."; RL Reproduction 139:381-393(2010). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 706-1056. RX PubMed=19540345; DOI=10.1016/j.jsb.2009.06.007; RA Jenkins H.T., Baker-Wilding R., Edwards T.A.; RT "Structure and RNA binding of the mouse Pumilio-2 Puf domain."; RL J. Struct. Biol. 167:271-276(2009). CC -!- FUNCTION: Sequence-specific RNA-binding protein that acts as a post- CC transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds CC to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'- CC UGUANAUA-3', that is related to the Nanos Response Element (NRE). CC Mediates post-transcriptional repression of transcripts via different CC mechanisms: acts via direct recruitment of the CCR4-POP2-NOT CC deadenylase leading to translational inhibition and mRNA degradation. CC Also mediates deadenylation-independent repression by promoting CC accessibility of miRNAs. Acts as a post-transcriptional repressor of CC E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. CC Plays a role in cytoplasmic sensing of viral infection. Represses a CC program of genes necessary to maintain genomic stability such as key CC mitotic, DNA repair and DNA replication factors. Its ability to repress CC those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA CC activated by DNA damage) which, due to its high abundance and multitude CC of PUMILIO binding sites, is able to sequester a significant fraction CC of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. CC May support proliferation and self-renewal of stem cells. Binds CC specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA CC MIR199A expression at a postranscriptional level (By similarity). CC {ECO:0000250|UniProtKB:Q8TB72}. CC -!- SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ, DAZL CC and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By CC similarity). Interacts with SNAPIN. Recruits the CCR4-POP2-NOT CC deadenylase leading to translational inhibition and mRNA degradation. CC Interacts with DDX20. In case of viral infection, interacts with DHX58 CC (By similarity). {ECO:0000250|UniProtKB:Q8TB72}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19861488}. CC Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Cytoplasm, CC perinuclear region {ECO:0000250}. Note=The cytoplasmic granules are CC stress granules which are a dense aggregation in the cytosol composed CC of proteins and RNAs that appear when the cell is under stress. CC Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ CC cells (By similarity). Colocalizes with NANOS3 in the stress granules CC (PubMed:19861488). {ECO:0000250|UniProtKB:Q8TB72, CC ECO:0000269|PubMed:19861488}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q80U58-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80U58-2; Sequence=VSP_009322, VSP_009323; CC Name=3; CC IsoId=Q80U58-3; Sequence=VSP_009321, VSP_009322, VSP_009323; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in embryonic stem CC cells, heart, kidney, lung, skin, intestine, spleen and thymus. CC Expressed at intermediate level in brain and liver. Weakly or not CC expressed in muscles and stomach. Expressed at various stages of CC myeloid and lymphoid cell development. In the testis expressed in the CC spermatogoni, spermatocytes, spermatids and Sertoli cells. CC {ECO:0000269|PubMed:11780640, ECO:0000269|PubMed:12667987, CC ECO:0000269|PubMed:18089289}. CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by packing CC together to form a right-handed superhelix that approximates a half CC donut. RNA-binding occurs on the concave side of the surface CC (PubMed:19540345). PUM2 is composed of 8 pumilio repeats of 36 CC residues; each repeat binds a single nucleotide in its RNA target. CC Residues at positions 12 and 16 of the pumilio repeat bind each RNA CC base via hydrogen bonding or van der Waals contacts with the Watson- CC Crick edge, while the amino acid at position 13 makes a stacking CC interaction. The recognition of RNA by pumilio repeats is base CC specific: cysteine and glutamine at position 12 and 16, respectively, CC bind adenine; asparagine and glutamine bind uracil; and serine and CC glutamate bind guanine (By similarity). {ECO:0000250|UniProtKB:Q14671, CC ECO:0000269|PubMed:19540345}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65507.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY027917; AAK21966.1; -; mRNA. DR EMBL; AF315590; AAG31805.1; -; mRNA. DR EMBL; AK122225; BAC65507.1; ALT_INIT; mRNA. DR EMBL; BC013765; AAH13765.1; -; mRNA. DR EMBL; BC041773; AAH41773.1; -; mRNA. DR CCDS; CCDS25802.1; -. [Q80U58-1] DR CCDS; CCDS49026.1; -. [Q80U58-2] DR RefSeq; NP_001153691.1; NM_001160219.1. [Q80U58-1] DR RefSeq; NP_001153694.1; NM_001160222.1. [Q80U58-2] DR RefSeq; NP_109648.2; NM_030723.2. [Q80U58-1] DR RefSeq; XP_006515340.1; XM_006515277.2. [Q80U58-1] DR RefSeq; XP_006515341.1; XM_006515278.3. [Q80U58-1] DR RefSeq; XP_006515342.1; XM_006515279.2. [Q80U58-1] DR RefSeq; XP_006515348.1; XM_006515285.3. [Q80U58-2] DR PDB; 3GVO; X-ray; 1.60 A; A=706-1056. DR PDB; 3GVT; X-ray; 2.80 A; A/B=706-1056. DR PDBsum; 3GVO; -. DR PDBsum; 3GVT; -. DR SMR; Q80U58; -. DR BioGRID; 219850; 5. DR IntAct; Q80U58; 4. DR MINT; Q80U58; -. DR STRING; 10090.ENSMUSP00000131074; -. DR iPTMnet; Q80U58; -. DR PhosphoSitePlus; Q80U58; -. DR EPD; Q80U58; -. DR jPOST; Q80U58; -. DR PaxDb; Q80U58; -. DR PeptideAtlas; Q80U58; -. DR PRIDE; Q80U58; -. DR Antibodypedia; 12999; 419 antibodies. DR Ensembl; ENSMUST00000163569; ENSMUSP00000131074; ENSMUSG00000020594. [Q80U58-1] DR Ensembl; ENSMUST00000168361; ENSMUSP00000128292; ENSMUSG00000020594. [Q80U58-1] DR Ensembl; ENSMUST00000169089; ENSMUSP00000132122; ENSMUSG00000020594. [Q80U58-2] DR Ensembl; ENSMUST00000178015; ENSMUSP00000137020; ENSMUSG00000020594. [Q80U58-2] DR GeneID; 80913; -. DR KEGG; mmu:80913; -. DR UCSC; uc007mzw.2; mouse. [Q80U58-3] DR UCSC; uc007mzy.2; mouse. [Q80U58-1] DR UCSC; uc007naa.2; mouse. [Q80U58-2] DR CTD; 23369; -. DR MGI; MGI:1931751; Pum2. DR eggNOG; KOG1488; Eukaryota. DR GeneTree; ENSGT00940000157575; -. DR InParanoid; Q80U58; -. DR KO; K17943; -. DR OrthoDB; 207351at2759; -. DR PhylomeDB; Q80U58; -. DR TreeFam; TF318160; -. DR BioGRID-ORCS; 80913; 0 hits in 18 CRISPR screens. DR ChiTaRS; Pum2; mouse. DR EvolutionaryTrace; Q80U58; -. DR PRO; PR:Q80U58; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; Q80U58; protein. DR Bgee; ENSMUSG00000020594; Expressed in bone marrow and 308 other tissues. DR ExpressionAtlas; Q80U58; baseline and differential. DR Genevisible; Q80U58; MM. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0035198; F:miRNA binding; ISO:MGI. DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISO:MGI. DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI. DR GO; GO:0010608; P:posttranscriptional regulation of gene expression; IMP:MGI. DR GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; ISS:UniProtKB. DR GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB. DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0034063; P:stress granule assembly; IDA:MGI. DR CDD; cd07920; Pumilio; 1. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR033133; PUM-HD. DR InterPro; IPR033712; Pumilio_RNA-bd. DR InterPro; IPR001313; Pumilio_RNA-bd_rpt. DR Pfam; PF00806; PUF; 8. DR SMART; SM00025; Pumilio; 8. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS50302; PUM; 8. DR PROSITE; PS50303; PUM_HD; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Translation regulation. FT CHAIN 1..1066 FT /note="Pumilio homolog 2" FT /id="PRO_0000075920" FT DOMAIN 706..1048 FT /note="PUM-HD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318" FT REPEAT 726..761 FT /note="Pumilio 1" FT REPEAT 762..797 FT /note="Pumilio 2" FT REPEAT 798..835 FT /note="Pumilio 3" FT REPEAT 836..871 FT /note="Pumilio 4" FT REPEAT 872..907 FT /note="Pumilio 5" FT REPEAT 908..943 FT /note="Pumilio 6" FT REPEAT 944..979 FT /note="Pumilio 7" FT REPEAT 980..1022 FT /note="Pumilio 8" FT REGION 1..260 FT /note="Interaction with SNAPIN" FT /evidence="ECO:0000250" FT REGION 741..745 FT /note="Adenine-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 777..781 FT /note="Uracil-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 813..817 FT /note="Adenine-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 851..855 FT /note="Non-specific-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 887..891 FT /note="Adenine-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 923..927 FT /note="Uracil-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 959..963 FT /note="Guanine-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT REGION 1002..1006 FT /note="Uracil-nucleotide binding in RNA target" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT COMPBIAS 277..486 FT /note="Ala-rich" FT COMPBIAS 358..404 FT /note="Gln-rich" FT COMPBIAS 520..687 FT /note="Ser-rich" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TB72" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT MOD_RES 136 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TB72" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TB72" FT MOD_RES 183 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8TB72" FT MOD_RES 395 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8TB72" FT MOD_RES 587 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 592 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT MOD_RES 674 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT MOD_RES 684 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14671" FT MOD_RES 700 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TB72" FT VAR_SEQ 1..56 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12693553" FT /id="VSP_009321" FT VAR_SEQ 574..652 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12693553, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009322" FT VAR_SEQ 829..830 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12693553, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009323" FT CONFLICT 461 FT /note="M -> I (in Ref. 3; BAC65507)" FT /evidence="ECO:0000305" FT CONFLICT 547 FT /note="G -> A (in Ref. 2; AAG31805)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="F -> C (in Ref. 2; AAG31805)" FT /evidence="ECO:0000305" FT CONFLICT 559..560 FT /note="LG -> VR (in Ref. 2; AAG31805)" FT /evidence="ECO:0000305" FT CONFLICT 570 FT /note="F -> C (in Ref. 2; AAG31805)" FT /evidence="ECO:0000305" FT CONFLICT 592 FT /note="S -> A (in Ref. 2; AAG31805)" FT /evidence="ECO:0000305" FT CONFLICT 628 FT /note="S -> G (in Ref. 2; AAG31805)" FT /evidence="ECO:0000305" FT HELIX 709..715 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 724..727 FT /evidence="ECO:0000244|PDB:3GVO" FT TURN 728..730 FT /evidence="ECO:0000244|PDB:3GVT" FT HELIX 731..735 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 738..748 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 753..763 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 764..766 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 767..771 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 776..786 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 789..799 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 803..807 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 812..822 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 825..828 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 831..834 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 835..837 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 841..846 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 850..860 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 863..865 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 867..872 FT /evidence="ECO:0000244|PDB:3GVO" FT TURN 873..876 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 877..881 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 886..896 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 899..910 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 913..917 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 922..932 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 935..943 FT /evidence="ECO:0000244|PDB:3GVO" FT TURN 944..947 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 949..953 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 958..968 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 971..982 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 991..997 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 1001..1011 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 1014..1024 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 1025..1027 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 1028..1031 FT /evidence="ECO:0000244|PDB:3GVO" FT TURN 1035..1037 FT /evidence="ECO:0000244|PDB:3GVO" FT HELIX 1038..1047 FT /evidence="ECO:0000244|PDB:3GVO" SQ SEQUENCE 1066 AA; 114314 MW; 027AC00FA91B055E CRC64; MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GTSHHSMSQP IMVQRRSGQS FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGTFGTRD AETDGPEKGD QKGKASPFEE DQNRDLKQDD EDSKINGRGL PNGMDADCKD FNRTPGSRQA SPTEVVERLG PSTNPPEGLG PLPNPTANKP LVEEFSNPET QNLDAMDQVG LDSLQFDYPG NQVPMDSSGA TVGLFDYNSQ QQLFQRTSAL TVQQLTAAQQ QQYALAAAQQ PHIAGVFSAG LAPAAFVPNP YIISAAPPGT DPYTAAGLAA AATLAGPAVV PPQYYGVPWG VYPANLFQQQ AAAAASNTAN QQAASQAQPG QQQVLRPGAG QRPITPSQGQ QGQQAESLAA AANPTLAFGQ SLAAGMPGYQ VLAPTAYYDQ TGALVVGPGA RTGLGAPVRL MAPTPVLISS TAAQAAAAAA AAGGTANSLT GSTNGLFRPI GTQPPQQQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS HGPGQPGSAS LGFGSGSSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQIVF NEILQAAYQL MTDVFGNYVI QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL ALSQHKFASN VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY ANYVVQKMID MAEPAQRKII MHKIRPHITT LRKYTYGKHI LAKLEKYYLK NSPDLGPIGG PPNGML //