SLN12_HUMAN
ID SLN12_HUMAN Reviewed; 578 AA.
AC Q8IYM2; A8K711; Q9NP47;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ribonuclease SLFN12 {ECO:0000305|PubMed:34272366};
DE EC=3.1.-.- {ECO:0000269|PubMed:34272366, ECO:0000269|PubMed:35104454};
DE AltName: Full=Schlafen family member 12 {ECO:0000312|HGNC:HGNC:25500};
GN Name=SLFN12 {ECO:0000312|HGNC:HGNC:25500};
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 [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-43 AND ARG-168.
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 [3]
RP FUNCTION, INTERACTION WITH SERPINB12, AND MUTAGENESIS OF ASP-233.
RX PubMed=30045019; DOI=10.1159/000492019;
RA Basson M.D., Wang Q., Chaturvedi L.S., More S., Vomhof-DeKrey E.E.,
RA Al-Marsoummi S., Sun K., Kuhn L.A., Kovalenko P., Kiupel M.;
RT "Schlafen 12 Interaction with SerpinB12 and Deubiquitylases Drives Human
RT Enterocyte Differentiation.";
RL Cell. Physiol. Biochem. 48:1274-1290(2018).
RN [4]
RP FUNCTION, INTERACTION WITH PDE3A, AND MUTAGENESIS OF LYS-213.
RX PubMed=31420216; DOI=10.1016/j.molcel.2019.06.040;
RA Li D., Chen J., Ai Y., Gu X., Li L., Che D., Jiang Z., Li L., Chen S.,
RA Huang H., Wang J., Cai T., Cao Y., Qi X., Wang X.;
RT "Estrogen-Related Hormones Induce Apoptosis by Stabilizing Schlafen-12
RT Protein Turnover.";
RL Mol. Cell 75:1103-1116(2019).
RN [5]
RP FUNCTION, INTERACTION WITH PDE3A, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP SER-368 AND SER-573, AND PHOSPHORYLATION AT SER-368 AND SER-573.
RX PubMed=35104454; DOI=10.1016/j.chembiol.2022.01.006;
RA Yan B., Ding Z., Zhang W., Cai G., Han H., Ma Y., Cao Y., Wang J., Chen S.,
RA Ai Y.;
RT "Multiple PDE3A modulators act as molecular glues promoting PDE3A-SLFN12
RT interaction and induce SLFN12 dephosphorylation and cell death.";
RL Cell Chem. Biol. 0:0-0(2022).
RN [6] {ECO:0007744|PDB:7LRC, ECO:0007744|PDB:7LRD, ECO:0007744|PDB:7LRE}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS); STRUCTURE BY ELECTRON MICROSCOPY
RP (2.76 ANGSTROMS) IN COMPLEX WITH PDE3A, FUNCTION, INTERACTION WITH PDE3A,
RP SUBUNIT, REGION, AND MUTAGENESIS OF GLU-200 AND GLU-205.
RX PubMed=34272366; DOI=10.1038/s41467-021-24495-w;
RA Garvie C.W., Wu X., Papanastasiou M., Lee S., Fuller J., Schnitzler G.R.,
RA Horner S.W., Baker A., Zhang T., Mullahoo J.P., Westlake L., Hoyt S.H.,
RA Toetzl M., Ranaghan M.J., de Waal L., McGaunn J., Kaplan B., Piccioni F.,
RA Yang X., Lange M., Tersteegen A., Raymond D., Lewis T.A., Carr S.A.,
RA Cherniack A.D., Lemke C.T., Meyerson M., Greulich H.;
RT "Structure of PDE3A-SLFN12 complex reveals requirements for activation of
RT SLFN12 RNase.";
RL Nat. Commun. 12:4375-4375(2021).
RN [7] {ECO:0007744|PDB:7EG0, ECO:0007744|PDB:7EG4}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 2-568 IN COMPLEX WITH
RP PDE3A, AND FUNCTION.
RX PubMed=34707099; DOI=10.1038/s41467-021-26546-8;
RA Chen J., Liu N., Huang Y., Wang Y., Sun Y., Wu Q., Li D., Gao S.,
RA Wang H.W., Huang N., Qi X., Wang X.;
RT "Structure of PDE3A-SLFN12 complex and structure-based design for a potent
RT apoptosis inducer of tumor cells.";
RL Nat. Commun. 12:6204-6204(2021).
CC -!- FUNCTION: Ribonuclease which is part of an E2/17beta-estradiol-induced
CC pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex
CC in the cytosol, promoting the dephosphorylation of SLFN12 and
CC activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity.
CC This apoptotic pathway might be relevant in tissues with high
CC concentration of E2 and be for instance involved in placenta remodeling
CC (PubMed:31420216, PubMed:35104454, PubMed:34272366, PubMed:34707099).
CC May play a role in cell differentiation (PubMed:30045019).
CC {ECO:0000269|PubMed:30045019, ECO:0000269|PubMed:31420216,
CC ECO:0000269|PubMed:34272366, ECO:0000269|PubMed:34707099,
CC ECO:0000269|PubMed:35104454}.
CC -!- SUBUNIT: Homodimer (PubMed:34272366). Interacts with PDE3A; direct low
CC affinity interaction which is stimulated by binding of 17beta-
CC estradiol/E2 to PDE3A and that positively regulates the ribonuclease
CC activity of SLFN12 (PubMed:31420216, PubMed:35104454, PubMed:34272366,
CC PubMed:34707099). Interacts with SERPINB12; as part of a pathway
CC regulating cell differentiation (PubMed:30045019).
CC {ECO:0000269|PubMed:30045019, ECO:0000269|PubMed:31420216,
CC ECO:0000269|PubMed:34272366, ECO:0000269|PubMed:34707099,
CC ECO:0000269|PubMed:35104454}.
CC -!- INTERACTION:
CC Q8IYM2; P01019: AGT; NbExp=3; IntAct=EBI-2822550, EBI-751728;
CC Q8IYM2; P06307: CCK; NbExp=3; IntAct=EBI-2822550, EBI-6624398;
CC Q8IYM2; P03952: KLKB1; NbExp=3; IntAct=EBI-2822550, EBI-10087153;
CC Q8IYM2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2822550, EBI-21591415;
CC Q8IYM2; P02545: LMNA; NbExp=3; IntAct=EBI-2822550, EBI-351935;
CC Q8IYM2; P06858: LPL; NbExp=3; IntAct=EBI-2822550, EBI-715909;
CC Q8IYM2; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-2822550, EBI-721769;
CC Q8IYM2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2822550, EBI-5280197;
CC Q8IYM2; P62826: RAN; NbExp=3; IntAct=EBI-2822550, EBI-286642;
CC Q8IYM2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2822550, EBI-5235340;
CC Q8IYM2; O15269-2: SPTLC1; NbExp=3; IntAct=EBI-2822550, EBI-25912901;
CC Q8IYM2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2822550, EBI-12806590;
CC Q8IYM2; P40337-2: VHL; NbExp=3; IntAct=EBI-2822550, EBI-12157263;
CC Q8IYM2; P54577: YARS1; NbExp=3; IntAct=EBI-2822550, EBI-1048893;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35104454}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:35104454}.
CC -!- PTM: Phosphorylation at Ser-368 and Ser-573 negatively regulates the
CC ribonuclease activity (PubMed:35104454). Dephosphorylation is induced
CC by the interaction with PDE3A and stimulates the rRNA ribonuclease
CC activity (PubMed:35104454). {ECO:0000269|PubMed:35104454}.
CC -!- SIMILARITY: Belongs to the Schlafen family. Subgroup II subfamily.
CC {ECO:0000305}.
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DR EMBL; AK001122; BAA91512.1; -; mRNA.
DR EMBL; AK291826; BAF84515.1; -; mRNA.
DR EMBL; BC035605; AAH35605.1; -; mRNA.
DR CCDS; CCDS11295.1; -.
DR RefSeq; NP_001275938.1; NM_001289009.1.
DR RefSeq; NP_060512.3; NM_018042.4.
DR RefSeq; XP_005258052.1; XM_005257995.4.
DR RefSeq; XP_011523269.1; XM_011524967.2.
DR RefSeq; XP_016880298.1; XM_017024809.1.
DR RefSeq; XP_016880299.1; XM_017024810.1.
DR PDB; 7EG0; EM; 3.40 A; B/D=2-568.
DR PDB; 7EG1; EM; 3.20 A; B/D=2-568.
DR PDB; 7EG4; EM; 3.20 A; B/D=2-568.
DR PDB; 7LRC; EM; 2.97 A; A/D=1-578.
DR PDB; 7LRD; EM; 3.22 A; A/C=1-578.
DR PDB; 7LRE; EM; 2.76 A; A/B=1-578.
DR PDBsum; 7EG0; -.
DR PDBsum; 7EG1; -.
DR PDBsum; 7EG4; -.
DR PDBsum; 7LRC; -.
DR PDBsum; 7LRD; -.
DR PDBsum; 7LRE; -.
DR AlphaFoldDB; Q8IYM2; -.
DR SMR; Q8IYM2; -.
DR BioGRID; 120416; 6.
DR IntAct; Q8IYM2; 21.
DR MINT; Q8IYM2; -.
DR STRING; 9606.ENSP00000378063; -.
DR iPTMnet; Q8IYM2; -.
DR PhosphoSitePlus; Q8IYM2; -.
DR BioMuta; SLFN12; -.
DR DMDM; 143585256; -.
DR EPD; Q8IYM2; -.
DR jPOST; Q8IYM2; -.
DR MassIVE; Q8IYM2; -.
DR PaxDb; Q8IYM2; -.
DR PeptideAtlas; Q8IYM2; -.
DR PRIDE; Q8IYM2; -.
DR ProteomicsDB; 71204; -.
DR Antibodypedia; 43970; 124 antibodies from 24 providers.
DR DNASU; 55106; -.
DR Ensembl; ENST00000304905.10; ENSP00000302077.5; ENSG00000172123.13.
DR Ensembl; ENST00000394562.5; ENSP00000378063.1; ENSG00000172123.13.
DR Ensembl; ENST00000452764.3; ENSP00000394903.2; ENSG00000172123.13.
DR GeneID; 55106; -.
DR KEGG; hsa:55106; -.
DR MANE-Select; ENST00000304905.10; ENSP00000302077.5; NM_018042.5; NP_060512.3.
DR UCSC; uc002hji.6; human.
DR CTD; 55106; -.
DR DisGeNET; 55106; -.
DR GeneCards; SLFN12; -.
DR HGNC; HGNC:25500; SLFN12.
DR HPA; ENSG00000172123; Low tissue specificity.
DR MIM; 614955; gene.
DR neXtProt; NX_Q8IYM2; -.
DR OpenTargets; ENSG00000172123; -.
DR PharmGKB; PA144596359; -.
DR VEuPathDB; HostDB:ENSG00000172123; -.
DR eggNOG; ENOG502RU3F; Eukaryota.
DR GeneTree; ENSGT00410000025651; -.
DR HOGENOM; CLU_034558_0_0_1; -.
DR InParanoid; Q8IYM2; -.
DR OMA; CMEKKNI; -.
DR OrthoDB; 211385at2759; -.
DR PhylomeDB; Q8IYM2; -.
DR TreeFam; TF337168; -.
DR PathwayCommons; Q8IYM2; -.
DR SignaLink; Q8IYM2; -.
DR BioGRID-ORCS; 55106; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; SLFN12; human.
DR GenomeRNAi; 55106; -.
DR Pharos; Q8IYM2; Tbio.
DR PRO; PR:Q8IYM2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IYM2; protein.
DR Bgee; ENSG00000172123; Expressed in monocyte and 115 other tissues.
DR ExpressionAtlas; Q8IYM2; baseline and differential.
DR Genevisible; Q8IYM2; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.950.30; -; 1.
DR InterPro; IPR029684; Schlafen.
DR InterPro; IPR007421; Schlafen_AlbA_2_dom.
DR InterPro; IPR038461; Schlafen_AlbA_2_dom_sf.
DR PANTHER; PTHR12155; PTHR12155; 1.
DR Pfam; PF04326; AlbA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..578
FT /note="Ribonuclease SLFN12"
FT /id="PRO_0000282984"
FT REGION 551..560
FT /note="Mediates interaction with PDE3A"
FT /evidence="ECO:0000269|PubMed:34272366"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35104454"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35104454"
FT VARIANT 43
FT /note="S -> R (in dbSNP:rs1849733)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031447"
FT VARIANT 168
FT /note="C -> R (in dbSNP:rs2586514)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031448"
FT VARIANT 448
FT /note="S -> P (in dbSNP:rs12946189)"
FT /id="VAR_053877"
FT MUTAGEN 200
FT /note="E->A: Decreased ribosomal RNA ribonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:34272366"
FT MUTAGEN 205
FT /note="E->A: Decreased ribosomal RNA ribonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:34272366"
FT MUTAGEN 213
FT /note="K->R: Loss of function in the E2-induced apoptotic
FT signaling pathway."
FT /evidence="ECO:0000269|PubMed:31420216"
FT MUTAGEN 233
FT /note="D->Q: Loss of interaction with SERPINB2."
FT /evidence="ECO:0000269|PubMed:30045019"
FT MUTAGEN 368
FT /note="S->A: Increased ribonuclease activity; when
FT associated with A-573."
FT /evidence="ECO:0000269|PubMed:35104454"
FT MUTAGEN 368
FT /note="S->E: Decreased ribonuclease activity; when
FT associated with E-573."
FT /evidence="ECO:0000269|PubMed:35104454"
FT MUTAGEN 573
FT /note="S->A: Increased ribonuclease activity; when
FT associated with A-368."
FT /evidence="ECO:0000269|PubMed:35104454"
FT MUTAGEN 573
FT /note="S->E: Decreased ribonuclease activity; when
FT associated with E-368."
FT /evidence="ECO:0000269|PubMed:35104454"
FT CONFLICT 361
FT /note="T -> A (in Ref. 1; BAA91512)"
FT /evidence="ECO:0000305"
FT STRAND 11..21
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 34..53
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 211..232
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 297..307
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7EG1"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:7EG1"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:7EG1"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:7EG4"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:7EG1"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 418..426
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 440..451
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 467..482
FT /evidence="ECO:0007829|PDB:7LRE"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:7LRE"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 527..540
FT /evidence="ECO:0007829|PDB:7LRE"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:7LRE"
FT HELIX 552..558
FT /evidence="ECO:0007829|PDB:7LRC"
SQ SEQUENCE 578 AA; 66972 MW; 858DEC808A50E753 CRC64;
MNISVDLETN YAELVLDVGR VTLGENSRKK MKDCKLRKKQ NESVSRAMCA LLNSGGGVIK
AEIENEDYSY TKDGIGLDLE NSFSNILLFV PEYLDFMQNG NYFLIFVKSW SLNTSGLRIT
TLSSNLYKRD ITSAKVMNAT AALEFLKDMK KTRGRLYLRP ELLAKRPCVD IQEENNMKAL
AGVFFDRTEL DRKEKLTFTE STHVEIKNFS TEKLLQRIKE ILPQYVSAFA NTDGGYLFIG
LNEDKEIIGF KAEMSDLDDL EREIEKSIRK MPVHHFCMEK KKINYSCKFL GVYDKGSLCG
YVCALRVERF CCAVFAKEPD SWHVKDNRVM QLTRKEWIQF MVEAEPKFSS SYEEVISQIN
TSLPAPHSWP LLEWQRQRHH CPGLSGRITY TPENLCRKLF LQHEGLKQLI CEEMDSVRKG
SLIFSRSWSV DLGLQENHKV LCDALLISQD SPPVLYTFHM VQDEEFKGYS TQTALTLKQK
LAKIGGYTKK VCVMTKIFYL SPEGMTSCQY DLRSQVIYPE SYYFTRRKYL LKALFKALKR
LKSLRDQFSF AENLYQIIGI DCFQKNDKKM FKSCRRLT
