SNED1_MOUSE
ID SNED1_MOUSE Reviewed; 1403 AA.
AC Q70E20; A6H6I3; Q810H2; Q8BMD9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sushi, nidogen and EGF-like domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Secreted protein SST-3 {ECO:0000303|PubMed:12665856};
DE AltName: Full=Stromal nidogen extracellular matrix protein {ECO:0000303|PubMed:15162516};
DE Flags: Precursor;
GN Name=Sned1 {ECO:0000303|PubMed:33012048, ECO:0000312|MGI:MGI:3045960};
GN Synonyms=Snep {ECO:0000303|PubMed:15162516};
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 2).
RX PubMed=12665856; DOI=10.1038/ni916;
RA Ueno H., Sakita-Ishikawa M., Morikawa Y., Nakano T., Kitamura T., Saito M.;
RT "A stromal cell-derived membrane protein that supports hematopoietic stem
RT cells.";
RL Nat. Immunol. 4:457-463(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=15162516; DOI=10.1002/dvdy.20056;
RA Leimeister C., Schumacher N., Diez H., Gessler M.;
RT "Cloning and expression analysis of the mouse stroma marker Snep encoding a
RT novel nidogen domain protein.";
RL Dev. Dyn. 230:371-377(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1075-1403 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Wolffian duct;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=33724335; DOI=10.1042/bcj20200675;
RA Vallet S.D., Davis M.N., Barque A., Thahab A.H., Ricard-Blum S., Naba A.;
RT "Computational and experimental characterization of the novel ECM
RT glycoprotein SNED1 and prediction of its interactome.";
RL Biochem. J. 478:1413-1434(2021).
RN [6]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=33012048; DOI=10.1002/dvdy.258;
RA Barque A., Jan K., De La Fuente E., Nicholas C.L., Hynes R.O., Naba A.;
RT "Knockout of the gene encoding the extracellular matrix protein SNED1
RT results in early neonatal lethality and craniofacial malformations.";
RL Dev. Dyn. 250:274-294(2021).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:33724335}. Note=Forms microfibrils within
CC the extracellular matrix and colocalizes with fibronectin (FN1).
CC {ECO:0000269|PubMed:33724335}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q70E20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70E20-2; Sequence=VSP_027755;
CC -!- TISSUE SPECIFICITY: Expressed in lung. {ECO:0000269|PubMed:15162516}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in embryos, notably in skeletal
CC and craniofacial precursors (PubMed:33012048). Expressed in mesenchymal
CC cells or stromal cell from 10.5 dpc to 17.5 dpc (PubMed:15162516).
CC {ECO:0000269|PubMed:15162516, ECO:0000269|PubMed:33012048}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:Q8TER0}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8TER0}.
CC -!- DISRUPTION PHENOTYPE: Early neonatal lethality, possibly due to
CC impaired nasal respiration caused by asymmetric and occluded nasal
CC cavities (PubMed:33012048). In addition to nasal cavity occlusion, mice
CC display growth defects and craniofacial malformations
CC (PubMed:33012048). Mice with a specific deletion in neural crest-cells
CC survive, but display growth defects and craniofacial malformations
CC partly phenocopying the effect of the global knockout mice
CC (PubMed:33012048). {ECO:0000269|PubMed:33012048}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY169783; AAO41836.1; -; mRNA.
DR EMBL; AJ584850; CAE48492.1; -; mRNA.
DR EMBL; BC145886; AAI45887.1; -; mRNA.
DR EMBL; AK032805; BAC28030.1; ALT_INIT; mRNA.
DR CCDS; CCDS35670.1; -. [Q70E20-1]
DR RefSeq; NP_766051.4; NM_172463.4.
DR AlphaFoldDB; Q70E20; -.
DR SMR; Q70E20; -.
DR BioGRID; 229013; 2.
DR STRING; 10090.ENSMUSP00000050832; -.
DR GlyGen; Q70E20; 3 sites.
DR iPTMnet; Q70E20; -.
DR PhosphoSitePlus; Q70E20; -.
DR MaxQB; Q70E20; -.
DR PaxDb; Q70E20; -.
DR PRIDE; Q70E20; -.
DR ProteomicsDB; 261287; -. [Q70E20-1]
DR ProteomicsDB; 261288; -. [Q70E20-2]
DR DNASU; 208777; -.
DR GeneID; 208777; -.
DR KEGG; mmu:208777; -.
DR UCSC; uc007cdm.1; mouse. [Q70E20-1]
DR CTD; 25992; -.
DR MGI; MGI:3045960; Sned1.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4291; Eukaryota.
DR InParanoid; Q70E20; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; Q70E20; -.
DR TreeFam; TF335195; -.
DR BioGRID-ORCS; 208777; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q70E20; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q70E20; protein.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00008; EGF; 13.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF06119; NIDO; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 14.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00539; NIDO; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1403
FT /note="Sushi, nidogen and EGF-like domain-containing
FT protein 1"
FT /id="PRO_5000072108"
FT DOMAIN 103..258
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 268..309
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 311..347
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 349..385
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 387..423
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 429..465
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 468..500
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 541..577
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 580..616
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 619..655
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 657..693
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 696..753
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 753..789
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 791..827
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 829..865
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 867..903
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 908..1006
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1007..1105
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1106..1200
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1306..1342
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 278..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 320..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 337..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 375..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 433..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 438..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 472..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 474..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 490..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 545..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 550..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 567..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 584..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 589..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 606..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 623..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 628..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 666..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..692
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 698..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 724..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 757..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 762..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 779..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 795..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 817..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 833..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 838..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 855..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 871..882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 876..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 893..902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1310..1321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1315..1330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1332..1341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1066..1403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12665856"
FT /id="VSP_027755"
FT CONFLICT 288
FT /note="C -> W (in Ref. 2; CAE48492)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="V -> M (in Ref. 1; AAO41836)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="Missing (in Ref. 4; BAC28030)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="I -> V (in Ref. 3; AAI45887 and 4; BAC28030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 151581 MW; 869F84724E44D8CE CRC64;
MRLGAAWALL LAAALGLGTR GVRAAVALAD FYPFGTKRGD TVTPKQDDGG SGLQPLSVPF
PFFGAEHSGL YVNNNGIISF LKEVSQFTPV AFPIAKDRCV VAAFWADVDN RRAGDVYYRE
ATDPAMLNRA TEDIRRYFPE LPDFSATWVF VATWYRVTFF GGSSSSPVNT FQTVLITDGR
FSFTIFNYES ILWTTGTHAS SGGDTDGLGG IAAQAGFNAG DGHRYFNIPG SRTADMAEVE
TTTNVGVPGR WAFRIDDAQV RVGGCGHTTS VCLVLRPCLN GGKCIDDCVT GNPSYTCSCL
AGFTGRRCHL DVNECASHPC QNGGTCTHGV NSFSCQCPAG FKGPTCESAQ SPCDNKVCQN
GGQCQAESSS AVCVCQAGYT GATCETDVDE CSSDPCQNGG SCVDLVGNYS CICVEPFEGP
QCETGSYLVP SPCLSNPCQN GGTCVDADEG YVCECPEGFM GLDCRERILN DCDCRNGGRC
LGANTTLCQC PPGFFGLLCE FEVTATPCNM NTQCPDGGYC MEYGGSYLCV CHTDHNISHS
LPSPCDSDPC FNGGSCDAHE DSYTCECPRG FHGRHCEKAR PHLCSSGPCR NGGTCKEMGD
EYRCTCPYRF TGRHCEIGKP DSCASGPCHN GGTCFHYIGK YKCDCPPGFS GRHCEIAPSP
CFRSPCMNGG TCEDLGTDFS CYCQPGYTGH RCQAEVDCGH PEEVEHATMR FNGTHVGSVA
LYTCEPGFSL SALSHIRVCQ PQGVWSQPPQ CIEVDECRSQ PCLHGGSCQD LIADYQCLCS
PGYEGVHCEL ETDECQAQPC RNGGSCRDLP RAFICQCPEG FVGIHCETEV DACASSPCQH
GGRCEDGGGA YLCVCPEGFF GYNCETVSDP CFSSPCGSRG YCLASNGSHS CTCKVGYTGK
DCTKELLPPT ALRVERVEES GVSISWSPPE GTTARQVLDG YAVTYASSDG SSRRTDFVDR
SRSSHQLRAL AAGRAYNISV FSVKRNTNNK NDISRPAALL TRTRPRPIED FEVTNISANA
ISVQWALHRI QHATVSRVRV SILYPEASAV QSTEVDRSVD RLTFGDLLPG RRYTVRLTTL
SGPGGAEYPT ESLASAPLNV WTRPLPPANL TASRVTATSA HMIWDTPAPG ISLEAYVINV
TTSQSTKSRY IPNGKLVSYT VRDLMPGRRY QLSVTAVQST EQGQLHSEPA HLYIITSPRD
GTDRRWHHGG HHSRMLRNRP APVRLPELRL LNDHSAPETP TQSSRFSELV DGRGRVSARF
GGLPSRAVTV RSQPTTPVPL KNTEAPEQVH LALQLPKNSS KDTESTPGSC SEDACQNGGT
CVPGADAHSC DCRPGFKGRH CELACEKVPR PCTRLFSETK SFPVWEGDIC HHVYKKVYKV
HQDVCFKERC QSTSLRKPKQ ETK
