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 20-JUN-2018, entry version 135. DE RecName: Full=Pumilio homolog 2; GN Name=Pum2; Synonyms=Kiaa0235; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT 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- RT binding proteins, show differential expression in fetal and adult RT hematopoietic 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: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly 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 RT project: 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 RT spermatogonia population."; RL Dev. Biol. 313:725-738(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION RP BY 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, RP AND 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 RT 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 RT lineage by a novel transgenic reporter reveals distinct subcellular RT localizations of 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 CC post-transcriptional repressor by binding the 3'-UTR of mRNA CC targets. Binds to an RNA consensus sequence, the Pumilio Response CC Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos CC Response Element (NRE). Mediates post-transcriptional repression CC of transcripts via different mechanisms: acts via direct CC recruitment of the CCR4-POP2-NOT deadenylase leading to CC translational inhibition and mRNA degradation. Also mediates CC deadenylation-independent repression by promoting accessibility of CC miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by CC binding to its 3'-UTR and facilitating miRNA regulation. Plays a CC role in cytoplasmic sensing of viral infection. Represses a CC program of genes necessary to maintain genomic stability such as CC key mitotic, DNA repair and DNA replication factors. Its ability CC to repress those target mRNAs is regulated by the lncRNA NORAD CC (non-coding RNA activated by DNA damage) which, due to its high CC abundance and multitude of PUMILIO binding sites, is able to CC sequester a significant fraction of PUM1 and PUM2 in the CC cytoplasm. May regulate DCUN1D3 mRNA levels. May support CC proliferation and self-renewal of stem cells. Binds specifically CC to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A CC expression at a postranscriptional level (By similarity). CC {ECO:0000250|UniProtKB:Q8TB72}. CC -!- SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ, CC DAZL 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 CC degradation. Interacts with DDX20. In case of viral infection, CC interacts with DHX58 (By similarity). CC {ECO:0000250|UniProtKB:Q80U58, 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 CC are stress granules which are a dense aggregation in the cytosol CC composed of proteins and RNAs that appear when the cell is under CC stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear CC region of germ cells (By similarity). Colocalizes with NANOS3 in CC the stress granules (PubMed:19861488). CC {ECO:0000250|UniProtKB:Q8TB72, 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 Note=No experimental confirmation available.; 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 CC the 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 CC packing together to form a right-handed superhelix that CC approximates a half donut. RNA-binding occurs on the concave side CC of the surface (PubMed:19540345). PUM2 is composed of 8 pumilio CC repeats of 36 residues; each repeat binds a single nucleotide in CC its RNA target. Residues at positions 12 and 16 of the pumilio CC repeat bind each RNA base via hydrogen bonding or van der Waals CC contacts with the Watson-Crick edge, while the amino acid at CC position 13 makes a stacking interaction. The recognition of RNA CC by pumilio repeats is base specific: cysteine and glutamine at CC position 12 and 16, respectively, bind adenine; asparagine and CC glutamine bind uracil; and serine and glutamate bind guanine (By CC similarity). {ECO:0000250|UniProtKB:Q14671, CC ECO:0000269|PubMed:19540345}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65507.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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 UniGene; Mm.341243; -. 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 ProteinModelPortal; Q80U58; -. DR SMR; Q80U58; -. DR BioGrid; 219850; 4. DR IntAct; Q80U58; 3. DR MINT; Q80U58; -. DR STRING; 10090.ENSMUSP00000128292; -. DR iPTMnet; Q80U58; -. DR PhosphoSitePlus; Q80U58; -. DR PaxDb; Q80U58; -. DR PeptideAtlas; Q80U58; -. DR PRIDE; Q80U58; -. 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 eggNOG; COG5099; LUCA. DR GeneTree; ENSGT00390000017241; -. DR HOGENOM; HOG000238461; -. DR HOVERGEN; HBG049462; -. DR InParanoid; Q80U58; -. DR KO; K17943; -. DR OMA; QRTNALT; -. DR OrthoDB; EOG091G04QO; -. DR PhylomeDB; Q80U58; -. DR TreeFam; TF318160; -. DR ChiTaRS; Pum2; mouse. DR EvolutionaryTrace; Q80U58; -. DR PRO; PR:Q80U58; -. DR Proteomes; UP000000589; Chromosome 12. DR Bgee; ENSMUSG00000020594; -. DR CleanEx; MM_PUM2; -. DR ExpressionAtlas; Q80U58; baseline and differential. DR Genevisible; Q80U58; MM. 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: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; Complete proteome; Cytoplasm; KW Methylation; Phosphoprotein; Reference proteome; Repeat; RNA-binding; KW Translation regulation. FT CHAIN 1 1066 Pumilio homolog 2. FT /FTId=PRO_0000075920. FT DOMAIN 706 1048 PUM-HD. {ECO:0000255|PROSITE- FT ProRule:PRU00318}. FT REPEAT 726 761 Pumilio 1. FT REPEAT 762 797 Pumilio 2. FT REPEAT 798 835 Pumilio 3. FT REPEAT 836 871 Pumilio 4. FT REPEAT 872 907 Pumilio 5. FT REPEAT 908 943 Pumilio 6. FT REPEAT 944 979 Pumilio 7. FT REPEAT 980 1022 Pumilio 8. FT REGION 1 260 Interaction with SNAPIN. {ECO:0000250}. FT REGION 741 745 Adenine-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT REGION 777 781 Uracil-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT REGION 813 817 Adenine-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT REGION 851 855 Non-specific-nucleotide binding in RNA FT target. {ECO:0000250|UniProtKB:Q14671}. FT REGION 887 891 Adenine-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT REGION 923 927 Uracil-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT REGION 959 963 Guanine-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT REGION 1002 1006 Uracil-nucleotide binding in RNA target. FT {ECO:0000250|UniProtKB:Q14671}. FT COMPBIAS 277 486 Ala-rich. FT COMPBIAS 358 404 Gln-rich. FT COMPBIAS 520 687 Ser-rich. FT MOD_RES 67 67 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8TB72}. FT MOD_RES 70 70 Phosphoserine. FT {ECO:0000250|UniProtKB:Q14671}. FT MOD_RES 82 82 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 102 102 Phosphoserine. FT {ECO:0000250|UniProtKB:Q14671}. FT MOD_RES 136 136 Phosphoserine. FT {ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 177 177 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8TB72}. FT MOD_RES 181 181 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8TB72}. FT MOD_RES 183 183 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q8TB72}. FT MOD_RES 395 395 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q8TB72}. FT MOD_RES 587 587 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 592 592 Phosphoserine. FT {ECO:0000250|UniProtKB:Q14671}. FT MOD_RES 674 674 Omega-N-methylarginine. FT {ECO:0000250|UniProtKB:Q14671}. FT MOD_RES 684 684 Phosphoserine. FT {ECO:0000250|UniProtKB:Q14671}. FT MOD_RES 700 700 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8TB72}. FT VAR_SEQ 1 56 Missing (in isoform 3). FT {ECO:0000303|PubMed:12693553}. FT /FTId=VSP_009321. FT VAR_SEQ 574 652 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:12693553, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_009322. FT VAR_SEQ 829 830 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:12693553, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_009323. FT CONFLICT 461 461 M -> I (in Ref. 3; BAC65507). FT {ECO:0000305}. FT CONFLICT 547 547 G -> A (in Ref. 2; AAG31805). FT {ECO:0000305}. FT CONFLICT 553 553 F -> C (in Ref. 2; AAG31805). FT {ECO:0000305}. FT CONFLICT 559 560 LG -> VR (in Ref. 2; AAG31805). FT {ECO:0000305}. FT CONFLICT 570 570 F -> C (in Ref. 2; AAG31805). FT {ECO:0000305}. FT CONFLICT 592 592 S -> A (in Ref. 2; AAG31805). FT {ECO:0000305}. FT CONFLICT 628 628 S -> G (in Ref. 2; AAG31805). FT {ECO:0000305}. FT HELIX 709 715 {ECO:0000244|PDB:3GVO}. FT HELIX 724 727 {ECO:0000244|PDB:3GVO}. FT TURN 728 730 {ECO:0000244|PDB:3GVT}. FT HELIX 731 735 {ECO:0000244|PDB:3GVO}. FT HELIX 738 748 {ECO:0000244|PDB:3GVO}. FT HELIX 753 763 {ECO:0000244|PDB:3GVO}. FT HELIX 764 766 {ECO:0000244|PDB:3GVO}. FT HELIX 767 771 {ECO:0000244|PDB:3GVO}. FT HELIX 776 786 {ECO:0000244|PDB:3GVO}. FT HELIX 789 799 {ECO:0000244|PDB:3GVO}. FT HELIX 803 807 {ECO:0000244|PDB:3GVO}. FT HELIX 812 822 {ECO:0000244|PDB:3GVO}. FT HELIX 825 828 {ECO:0000244|PDB:3GVO}. FT HELIX 831 834 {ECO:0000244|PDB:3GVO}. FT HELIX 835 837 {ECO:0000244|PDB:3GVO}. FT HELIX 841 846 {ECO:0000244|PDB:3GVO}. FT HELIX 850 860 {ECO:0000244|PDB:3GVO}. FT HELIX 863 865 {ECO:0000244|PDB:3GVO}. FT HELIX 867 872 {ECO:0000244|PDB:3GVO}. FT TURN 873 876 {ECO:0000244|PDB:3GVO}. FT HELIX 877 881 {ECO:0000244|PDB:3GVO}. FT HELIX 886 896 {ECO:0000244|PDB:3GVO}. FT HELIX 899 910 {ECO:0000244|PDB:3GVO}. FT HELIX 913 917 {ECO:0000244|PDB:3GVO}. FT HELIX 922 932 {ECO:0000244|PDB:3GVO}. FT HELIX 935 943 {ECO:0000244|PDB:3GVO}. FT TURN 944 947 {ECO:0000244|PDB:3GVO}. FT HELIX 949 953 {ECO:0000244|PDB:3GVO}. FT HELIX 958 968 {ECO:0000244|PDB:3GVO}. FT HELIX 971 982 {ECO:0000244|PDB:3GVO}. FT HELIX 991 997 {ECO:0000244|PDB:3GVO}. FT HELIX 1001 1011 {ECO:0000244|PDB:3GVO}. FT HELIX 1014 1024 {ECO:0000244|PDB:3GVO}. FT HELIX 1025 1027 {ECO:0000244|PDB:3GVO}. FT HELIX 1028 1031 {ECO:0000244|PDB:3GVO}. FT TURN 1035 1037 {ECO:0000244|PDB:3GVO}. FT HELIX 1038 1047 {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 //