ID RELN_MOUSE Reviewed; 3461 AA. AC Q60841; Q9CUA6; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 25-NOV-2008, entry version 82. DE RecName: Full=Reelin; DE EC=3.4.21.-; DE AltName: Full=Reeler protein; DE Flags: Precursor; GN Name=Reln; Synonyms=Rl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX MEDLINE=95231649; PubMed=7715726; DOI=10.1038/374719a0; RA D'Arcangelo G., Miao G.G., Chen S.-C., Soares H.D., Morgan J.I., RA Curran T.; RT "A protein related to extracellular matrix proteins deleted in the RT mouse mutant reeler."; RL Nature 374:719-723(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=98086481; PubMed=9417911; DOI=10.1006/geno.1997.4983; RA Royaux I., Lambert de Rouvroit C., D'Arcangelo G., Demirov D., RA Goffinet A.M.; RT "Genomic organization of the mouse reelin gene."; RL Genomics 46:240-250(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2152-3461 (ISOFORM 1). RC STRAIN=BALB/c; TISSUE=Brain; RX MEDLINE=95375789; PubMed=7647795; DOI=10.1038/ng0595-77; RA Hirotsune S., Takahara T., Sasaki N., Hirose K., Yoshiki A., RA Ohashi T., Kusakabe M., Murakami Y., Muramatsu M., Watanabe S., RA Nakao K., Katsuki M., Hayashizaki Y.; RT "The reeler gene encodes a protein with an EGF-like motif expressed by RT pioneer neurons."; RL Nat. Genet. 10:77-83(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3044-3461 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Testis; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP CHARACTERIZATION. RX MEDLINE=97141547; PubMed=8987733; RA D'Arcangelo G., Nakajima K., Miyata T., Ogawa M., Mikoshiba K., RA Curran T.; RT "Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal RT antibody."; RL J. Neurosci. 17:23-31(1997). RN [6] RP CHARACTERIZATION. RX MEDLINE=21634904; PubMed=11689558; DOI=10.1074/jbc.M106996200; RA Quattrocchi C.C., Wannenes F., Persico A.M., Ciafre S.A., RA D'Arcangelo G., Farace M.G., Keller F.; RT "Reelin is a serine protease of the extracellular matrix."; RL J. Biol. Chem. 277:303-309(2002). RN [7] RP TISSUE SPECIFICITY. RX MEDLINE=97325946; PubMed=9182958; RA Schiffmann S.N., Bernier B., Goffinet A.M.; RT "Reelin mRNA expression during mouse brain development."; RL Eur. J. Neurosci. 9:1055-1071(1997). RN [8] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX MEDLINE=99263436; PubMed=10328932; DOI=10.1006/exnr.1999.7019; RA Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V., RA Goffinet A.M.; RT "Evolutionarily conserved, alternative splicing of reelin during brain RT development."; RL Exp. Neurol. 156:229-238(1999). RN [9] RP INTERACTION WITH VLDLR AND APOER2. RX MEDLINE=20036019; PubMed=10571241; DOI=10.1016/S0896-6273(00)80861-2; RA Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C., RA Cooper J.A., Herz J.; RT "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces RT tyrosine phosphorylation of disabled-1 and modulates tau RT phosphorylation."; RL Neuron 24:481-489(1999). RN [10] RP FUNCTION. RX MEDLINE=20359755; PubMed=10880573; DOI=10.1073/pnas.150040497; RA Yip J.W., Yip Y.P.L., Nakajima K., Capriotti C.; RT "Reelin controls position of autonomic neurons in the spinal cord."; RL Proc. Natl. Acad. Sci. U.S.A. 97:8612-8616(2000). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1273, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17203969; DOI=10.1021/pr0604155; RA Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; RT "Protein phosphorylation and expression profiling by Yin-yang RT multidimensional liquid chromatography (Yin-yang MDLC) mass RT spectrometry."; RL J. Proteome Res. 6:250-262(2007). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1222-1597, DISULFIDE BONDS, RP AND CALCIUM-BINDING. RX PubMed=16858396; DOI=10.1038/sj.emboj.7601240; RA Nogi T., Yasui N., Hattori M., Iwasaki K., Takagi J.; RT "Structure of a signaling-competent reelin fragment revealed by X-ray RT crystallography and electron tomography."; RL EMBO J. 25:3675-3683(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1948-2662, DISULFIDE BONDS, RP GLYCOSYLATION AT ASN-2145; ASN-2269; ASN-2317 AND ASN-2569, RP CALCIUM-BINDING, ZINC-BINDING SITES, AND MUTAGENESIS OF LYS-2360 AND RP LYS-2467. RX PubMed=17548821; DOI=10.1073/pnas.0700438104; RA Yasui N., Nogi T., Kitao T., Nakano Y., Hattori M., Takagi J.; RT "Structure of a receptor-binding fragment of reelin and mutational RT analysis reveal a recognition mechanism similar to endocytic RT receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 104:9988-9993(2007). CC -!- FUNCTION: Extracellular matrix serine protease that plays a role CC in layering of neurons in the cerebral cortex and cerebellum. CC Regulates microtubule function in neurons and neuronal migration. CC Affects migration of sympathetic preganglionic neurons in the CC spinal cord, where it seems to act as a barrier to neuronal CC migration. Enzymatic activity is important for the modulation of CC cell adhesion. Binding to the extracellular domains of lipoprotein CC receptors VLDLR and ApoER2 induces tyrosine phosphorylation of CC Dab1 and modulation of Tau phosphorylation. CC -!- SUBUNIT: Binds to the ectodomains of VLDLR and ApoER2. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q60841-1; Sequence=Displayed; CC Name=2; CC IsoId=Q60841-2; Sequence=VSP_005577; CC Name=3; CC IsoId=Q60841-3; Sequence=VSP_005578; CC -!- TISSUE SPECIFICITY: The major isoform 1 is neuron-specific. It is CC abundantly produced during brain ontogenesis by the Cajal-Retzius CC cells and other pioneer neurons located in the telencephalic CC marginal zone and by granule cells of the external granular layer CC of the cerebellum. Expression is located in deeper layers in the CC developing hippocampus and olfactory bulb, low levels of CC expression are also detected in the immature striatum. At early CC developmental stages, expressed also in hypothalamic CC differentiation fields, tectum and spinal cord. A moderate to low CC level of expression occurs in the septal area, striatal fields, CC habenular nuclei, some thalamic nuclei, particularly the lateral CC geniculate, the retina and some nuclei of the reticular formation CC in the central field of the medulla. Very low levels found in CC liver and kidney. No expression in radial glial cells, cortical CC plate, Purkinje cells and inferior olivary neurons. The minor CC isoform 2 is only expressed in non neuronal cells. The minor CC isoform 3 is found in the same cells as isoform 1, but is almost CC undetectable in retina and brain stem. CC -!- DEVELOPMENTAL STAGE: First detected at embryonic day 11.5. CC Expression increases up to birth and remains high from postnatal CC day 2 to 11 in both cerebellum and fore/midbrain. Expression CC declines thereafter and is largely brain specific in the adult. CC -!- DOMAIN: The basic C-terminal region is essential for secretion. CC -!- PTM: N-glycosylated and to a lesser extent also O-glycosylated. CC -!- DISEASE: Defects in Reln are the cause of the autosomal recessive CC reeler (rl) phenotype which is characterized by impaired motor CC coordination, tremors and ataxia. Neurons in affected mice fail to CC reach their correct locations in the developing brain, disrupting CC the organization of the cerebellar and cerebral cortices and other CC laminated regions. CC -!- SIMILARITY: Belongs to the reelin family. CC -!- SIMILARITY: Contains 16 BNR repeats. CC -!- SIMILARITY: Contains 8 EGF-like domains. CC -!- SIMILARITY: Contains 1 reelin domain. 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; U24703; AAB91599.1; -; mRNA. DR EMBL; D63520; BAA09788.1; ALT_INIT; mRNA. DR EMBL; AK017094; BAB30592.1; -; mRNA. DR PIR; S58870; S58870. DR RefSeq; NP_035391.2; -. DR UniGene; Mm.425236; -. DR PDB; 2DDU; X-ray; 2.05 A; A=1222-1597. DR PDB; 2E26; X-ray; 2.00 A; A=1948-2662. DR PDBsum; 2DDU; -. DR PDBsum; 2E26; -. DR SMR; Q60841; 1294-1597. DR PhosphoSite; Q60841; -. DR Ensembl; ENSMUSG00000042453; Mus musculus. DR GeneID; 19699; -. DR KEGG; mmu:19699; -. DR MGI; MGI:103022; Reln. DR HOGENOM; Q60841; -. DR HOVERGEN; Q60841; -. DR NextBio; 297056; -. DR ArrayExpress; Q60841; -. DR CleanEx; MM_RELN; -. DR GermOnline; ENSMUSG00000042453; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0030425; C:dendrite; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase ac...; IDA:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0007411; P:axon guidance; IMP:MGI. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0021800; P:cerebral cortex tangential migration; IMP:MGI. DR GO; GO:0010001; P:glial cell differentiation; IMP:MGI. DR GO; GO:0001764; P:neuron migration; IMP:MGI. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI. DR GO; GO:0051057; P:positive regulation of small GTPase mediate...; IDA:MGI. DR GO; GO:0048265; P:response to pain; IMP:MGI. DR GO; GO:0021511; P:spinal cord patterning; IMP:MGI. DR InterPro; IPR002860; BNR. DR InterPro; IPR006210; EGF. DR InterPro; IPR000742; EGF_3. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR013032; EGF_like_reg_CS. DR InterPro; IPR002861; Reeler. DR Pfam; PF02012; BNR; 15. DR Pfam; PF07974; EGF_2; 7. DR Pfam; PF02014; Reeler; 1. DR SMART; SM00181; EGF; 5. DR PROSITE; PS00022; EGF_1; 7. DR PROSITE; PS01186; EGF_2; 6. DR PROSITE; PS50026; EGF_3; 5. DR PROSITE; PS51019; REELIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; KW Developmental protein; EGF-like domain; Extracellular matrix; KW Glycoprotein; Hydrolase; Metal-binding; Phosphoprotein; Protease; KW Repeat; Secreted; Serine protease; Signal; Zinc. FT SIGNAL 1 26 Potential. FT CHAIN 27 3461 Reelin. FT /FTId=PRO_0000030305. FT DOMAIN 27 191 Reelin. FT REPEAT 593 604 BNR 1. FT DOMAIN 671 702 EGF-like 1. FT REPEAT 799 810 BNR 2. FT REPEAT 952 963 BNR 3. FT DOMAIN 1030 1061 EGF-like 2. FT REPEAT 1157 1168 BNR 4. FT REPEAT 1323 1334 BNR 5. FT DOMAIN 1409 1442 EGF-like 3. FT REPEAT 1535 1546 BNR 6. FT REPEAT 1686 1697 BNR 7. FT DOMAIN 1765 1796 EGF-like 4. FT REPEAT 1884 1895 BNR 8. FT REPEAT 2043 2054 BNR 9. FT DOMAIN 2129 2161 EGF-like 5. FT REPEAT 2250 2261 BNR 10. FT REPEAT 2399 2410 BNR 11. FT DOMAIN 2478 2509 EGF-like 6. FT REPEAT 2598 2609 BNR 12. FT REPEAT 2778 2789 BNR 13. FT DOMAIN 2853 2884 EGF-like 7. FT REPEAT 2979 2990 BNR 14. FT REPEAT 3143 3155 BNR 15. FT DOMAIN 3228 3260 EGF-like 8. FT REPEAT 3363 3374 BNR 16. FT COMPBIAS 3432 3461 Arg-rich (basic). FT METAL 2061 2061 Zinc 1. FT METAL 2074 2074 Zinc 1. FT METAL 2179 2179 Zinc 1. FT METAL 2264 2264 Zinc 1. FT METAL 2397 2397 Zinc 2. FT METAL 2399 2399 Zinc 2. FT METAL 2460 2460 Zinc 2. FT MOD_RES 1273 1273 Phosphothreonine. FT CARBOHYD 141 141 N-linked (GlcNAc...) (Potential). FT CARBOHYD 258 258 N-linked (GlcNAc...) (Potential). FT CARBOHYD 290 290 N-linked (GlcNAc...) (Potential). FT CARBOHYD 306 306 N-linked (GlcNAc...) (Potential). FT CARBOHYD 629 629 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1267 1267 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1447 1447 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1503 1503 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1600 1600 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1750 1750 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1921 1921 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2145 2145 N-linked (GlcNAc...). FT CARBOHYD 2269 2269 N-linked (GlcNAc...). FT CARBOHYD 2317 2317 N-linked (GlcNAc...). FT CARBOHYD 2569 2569 N-linked (GlcNAc...). FT CARBOHYD 2962 2962 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3016 3016 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3073 3073 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3185 3185 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3412 3412 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3439 3439 N-linked (GlcNAc...) (Potential). FT DISULFID 540 581 By similarity. FT DISULFID 609 614 By similarity. FT DISULFID 675 685 By similarity. FT DISULFID 692 701 By similarity. FT DISULFID 895 937 By similarity. FT DISULFID 968 975 By similarity. FT DISULFID 1034 1044 By similarity. FT DISULFID 1051 1060 By similarity. FT DISULFID 1271 1310 FT DISULFID 1339 1348 FT DISULFID 1633 1673 By similarity. FT DISULFID 1702 1709 By similarity. FT DISULFID 1983 2030 FT DISULFID 2059 2070 FT DISULFID 2133 2143 FT DISULFID 2137 2149 FT DISULFID 2151 2160 FT DISULFID 2195 2235 FT DISULFID 2348 2387 FT DISULFID 2393 2559 FT DISULFID 2482 2492 FT DISULFID 2486 2497 FT DISULFID 2499 2508 FT DISULFID 2544 2584 FT DISULFID 2794 2801 By similarity. FT DISULFID 2919 2966 By similarity. FT DISULFID 3160 3170 By similarity. FT DISULFID 3232 3242 By similarity. FT DISULFID 3236 3248 By similarity. FT DISULFID 3250 3259 By similarity. FT DISULFID 3296 3346 By similarity. FT VAR_SEQ 3429 3461 Missing (in isoform 3). FT /FTId=VSP_005578. FT VAR_SEQ 3429 3430 Missing (in isoform 2). FT /FTId=VSP_005577. FT MUTAGEN 2360 2360 K->A: Abolishes ApoER2-binding. FT MUTAGEN 2467 2467 K->A: Abolishes ApoER2-binding. FT CONFLICT 3066 3066 Missing (in Ref. 4; BAB30592). FT STRAND 1958 1960 FT STRAND 1963 1965 FT HELIX 1968 1970 FT STRAND 1971 1973 FT STRAND 1978 1980 FT STRAND 1996 1999 FT STRAND 2005 2011 FT STRAND 2014 2016 FT STRAND 2020 2032 FT STRAND 2040 2047 FT STRAND 2053 2056 FT STRAND 2059 2061 FT STRAND 2078 2080 FT STRAND 2089 2095 FT TURN 2096 2099 FT STRAND 2102 2113 FT STRAND 2122 2131 FT HELIX 2134 2139 FT STRAND 2140 2144 FT TURN 2145 2147 FT STRAND 2148 2151 FT STRAND 2155 2157 FT STRAND 2170 2172 FT STRAND 2174 2176 FT STRAND 2178 2187 FT STRAND 2189 2193 FT STRAND 2197 2201 FT STRAND 2203 2206 FT STRAND 2212 2216 FT STRAND 2226 2233 FT STRAND 2236 2238 FT STRAND 2247 2254 FT STRAND 2260 2265 FT TURN 2269 2272 FT STRAND 2275 2280 FT HELIX 2283 2285 FT STRAND 2287 2296 FT STRAND 2299 2301 FT STRAND 2307 2315 FT STRAND 2324 2326 FT STRAND 2328 2330 FT TURN 2333 2335 FT STRAND 2336 2338 FT STRAND 2343 2345 FT STRAND 2354 2357 FT STRAND 2364 2368 FT STRAND 2371 2373 FT STRAND 2378 2384 FT STRAND 2395 2403 FT STRAND 2409 2412 FT STRAND 2419 2422 FT TURN 2433 2436 FT STRAND 2440 2445 FT HELIX 2448 2450 FT STRAND 2452 2461 FT STRAND 2471 2480 FT HELIX 2484 2488 FT STRAND 2489 2493 FT STRAND 2496 2499 FT STRAND 2503 2505 FT STRAND 2510 2513 FT STRAND 2519 2521 FT TURN 2529 2531 FT STRAND 2532 2542 FT STRAND 2547 2550 FT STRAND 2552 2555 FT STRAND 2562 2565 FT STRAND 2575 2582 FT STRAND 2584 2586 FT HELIX 2591 2593 FT STRAND 2594 2602 FT STRAND 2608 2613 FT STRAND 2622 2627 FT HELIX 2630 2632 FT STRAND 2634 2642 SQ SEQUENCE 3461 AA; 387513 MW; 4131F3E84A9D4AE2 CRC64; MERGCWAPRA LVLAVLLLLA TLRARAATGY YPRFSPFFFL CTHHGELEGD GEQGEVLISL HIAGNPTYYV PGQEYHVTIS TSTFFDGLLV TGLYTSTSIQ SSQSIGGSSA FGFGIMSDHQ FGNQFMCSVV ASHVSHLPTT NLSFVWIAPP AGTGCVNFMA TATHRGQVIF KDALAQQLCE QGAPTEATAY SHLAEIHSDS VILRDDFDSY QQLELNPNIW VECSNCEMGE QCGTIMHGNA VTFCEPYGPR ELTTTCLNTT TASVLQFSIG SGSCRFSYSD PSITVSYAKN NTADWIQLEK IRAPSNVSTV IHILYLPEEA KGESVQFQWK QDSLRVGEVY EACWALDNIL VINSAHREVV LEDNLDPVDT GNWLFFPGAT VKHSCQSDGN SIYFHGNEGS EFNFATTRDV DLSTEDIQEQ WSEEFESQPT GWDILGAVVG ADCGTVESGL SLVFLKDGER KLCTPYMDTT GYGNLRFYFV MGGICDPGVS HENDIILYAK IEGRKEHIAL DTLTYSSYKV PSLVSVVINP ELQTPATKFC LRQKSHQGYN RNVWAVDFFH VLPVLPSTMS HMIQFSINLG CGTHQPGNSV SLEFSTNHGR SWSLLHTECL PEICAGPHLP HSTVYSSENY SGWNRITIPL PNAALTRDTR IRWRQTGPIL GNMWAIDNVY IGPSCLKFCS GRGQCTRHGC KCDPGFSGPA CEMASQTFPM FISESFGSAR LSSYHNFYSI RGAEVSFGCG VLASGKALVF NKDGRRQLIT SFLDSSQSRF LQFTLRLGSK SVLSTCRAPD QPGEGVLLHY SYDNGITWKL LEHYSYVNYH EPRIISVELP DDARQFGIQF RWWQPYHSSQ GEDVWAIDEI VMTSVLFNSI SLDFTNLVEV TQSLGFYLGN VQPYCGHDWT LCFTGDSKLA SSMRYVETQS MQIGASYMIQ FSLVMGCGQK YTPHMDNQVK LEYSANHGLT WHLVQEECLP SMPSCQEFTS ASIYHASEFT QWRRVTVVLP QKTWSGATRF RWSQSYYTAQ DEWALDNIYI GQQCPNMCSG HGSCDHGVCR CDQGYQGTEC HPEAALPSTI MSDFENPSSW ESDWQEVIGG EVVKPEQGCG VVSSGSSLYF SKAGKRQLVS WDLDTSWVDF VQFYIQIGGE SAACNKPDSR EEGILLQYSN NGGIQWHLLA EMYFSDFSKP RFVYLELPAA GKTPCTRFRW WKPVFSGEDY DQWAVDDIII LSEKQKQVIP VVNPTLPQNF YEKPAFDYPM NQMSVWLMLA NEGMAKNDSF CATTPSAMVF GKSDGDRFAV TRDLTLKPGY VLQFKLNIGC TSQFSSTAPV LLQYSHDAGM SWFLLKEGCF PASAAKGCEG NSRELSEPTV YYTGDFEEWT RITIAIPRSL ASSKTRFRWI QESSSQKNVP PFGLDGVYIS EPCPSYCSGH GDCISGVCFC DLGYTAAQGT CVSNTPNHSE MFDRFEGKLS PLWYKITGGQ VGTGCGTLND GRSLYFNGLG KREARTVPLD TRNISLVQFY IQIGSKTSGI TYITPRARYE GLVVQYSNDN GILWHLLREL DFMSFLEPQI ISIDLPREAK TPATAFRWWQ PQHGKHSAQW ALGDVLIGVN DSSQTGFQDK LDGSIDLQAN WYRIQGGQVD IDCLSMDTAL IFTENIGNPR YAETWDFHVS ESSFLQWEMN MGCSKPFSGA HGIQLQYSLN NGKDWQLVTE ECVPPTIGCV HYTESSTYTS ERFQNWRRVT VYLPLATNSP RTRFRWIQTN YTVGADSWAI DNVILASGCP WMCSGRGICD SGRCVCDRGF GGPFCVPVVP LPSILKDDFN GNLHPDLWPE VYGAERGNLN GETIKSGTCL IFKGEGLRML ISRDLDCTNT MYVQFSLRFI AKGTPERSHS ILLQFSVSGG VTWHLMDEFY FPQTTSILFI NVPLPYGAQT NATRFRLWQP YNNGKKEEIW IIDDFIIDGN NLNNPVLLLD TFDFGPREDN WFFYPGGNIG LYCPYSSKGA PEEDSAMVFV SNEVGEHSIT TRDLSVNENT IIQFEINVGC STDSSSADPV RLEFSRDFGA TWHLLLPLCY HSSSLVSSLC STEHHPSSTY YAGTTQGWRR EVVHFGKLHL CGSVRFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCYGH GSCINGTKCI CDPGYSGPTC KISTKNPDFL KDDFEGQLES DRFLLMSGGK PSRKCGILSS GNNLFFNEDG LRMLVTRDLD LSHARFVQFF MRLGCGKGVP DPRSQPVLLQ YSLNGGLSWS LLQEFLFSNS SNVGRYIALE MPLKARSGST RLRWWQPSEN GHFYSPWVID QILIGGNISG NTVLEDDFST LDSRKWLLHP GGTKMPVCGS TGDALVFIEK ASTRYVVTTD IAVNEDSFLQ IDFAASCSVT DSCYAIELEY SVDLGLSWHP LVRDCLPTNV ECSRYHLQRI LVSDTFNKWT RITLPLPSYT RSQATRFRWH QPAPFDKQQT WAIDNVYIGD GCLDMCSGHG RCVQGSCVCD EQWGGLYCDE PETSLPTQLK DNFNRAPSNQ NWLTVSGGKL STVCGAVASG LALHFSGGCS RLLVTVDLNL TNAEFIQFYF MYGCLITPSN RNQGVLLEYS VNGGITWNLL MEIFYDQYSK PGFVNILLPP DAKEIATRFR WWQPRHDGLD QNDWAIDNVL ISGSADQRTV MLDTFSSAPV PQHERSPADA GPVGRIAFEM FLEDKTSVNE NWLFHDDCTV ERFCDSPDGV MLCGSHDGRE VYAVTHDLTP TENWIMQFKI SVGCKVPEKI AQNQIHVQFS TDFGVSWSYL VPQCLPADPK CSGSVSQPSV FFPTEGWKRI TYPLPESLTG NPVRFRFYQK YSDVQWAIDN FYLGPGCLDN CGGHGDCLKE QCICDPGYSG PNCYLTHSLK TFLKERFDSE EIKPDLWMSL EGGSTCTECG VLAENTALYF GGSTVRQAIT QDLDLRGAKF LQYWGRIGSE NNMTSCHRPV CRKEGVLLDF STDGGITWTL LHEMDFQKYI SVRHDYILLP EGALTNTTRL RWWQPFVISN GLVVSGVERA QWALDNILIG GAEINPSQLV DTFDDEGSSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK KDKTHNALSS RELIIQPGYM MQFKIVVGCE ATSCGDLHSV MLEYTKDARS DSWQLVQTQC LPSSSNSIGC SPFQFHEATI YNAVNSSSWK RITIQLPDHV SSSATQFRWI QKGEETEKQS WAIDHVYIGE ACPKLCSGHG YCTTGAVCIC DESFQGDDCS VFSHELPSYI KDNFESARVT EANWETIQGG VIGSGCGQLA PYAHGDSLYF NGCQIRQAAT KPLDLTRASK IMFVLQIGSP AQTDSCNSDL SGPHTVDKAV LLQYSVNNGI TWHVIAQHQP KDFTQAQRVS YNVPLEARMK GVLLRWWQPR HNGTGHDQWA LDHVEVVLVS TRKQNYMMNF SRQHGLRHFY NRRRRSLRRY P //