ID   NUDEL_DROME             Reviewed;        2616 AA.
AC   P98159; Q9VRX5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Serine protease nudel;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=ndl; ORFNames=CG10129;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Oregon-R; TISSUE=Ovary;
RX   PubMed=7671306; DOI=10.1016/0092-8674(95)90475-1;
RA   Hong C.C., Hashimoto C.;
RT   "An unusual mosaic protein with a protease domain, encoded by the nudel
RT   gene, is involved in defining embryonic dorsoventral polarity in
RT   Drosophila.";
RL   Cell 82:785-794(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   CLEAVAGE OF EASTER.
RX   PubMed=9477324; DOI=10.1242/dev.125.7.1261;
RA   Misra S., Hecht P., Maeda R., Anderson K.V.;
RT   "Positive and negative regulation of Easter, a member of the serine
RT   protease family that controls dorsal-ventral patterning in the Drosophila
RT   embryo.";
RL   Development 125:1261-1267(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-220; SER-574;
RP   SER-581; SER-1134 AND SER-1136, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Component of the extracellular signaling pathway that
CC       establishes the dorsal-ventral pathway of the embryo. Three proteases;
CC       ndl, gd and snk process easter to create active easter. Active easter
CC       defines cell identities along the dorsal-ventral continuum by
CC       activating the spz ligand for the Tl receptor in the ventral region of
CC       the embryo. Nudel, pipe and windbeutel together trigger the protease
CC       cascade within the extraembryonic perivitelline compartment which
CC       induces dorsoventral polarity of the Drosophila embryo.
CC       {ECO:0000269|PubMed:7671306}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:7671306}.
CC   -!- TISSUE SPECIFICITY: Follicle. {ECO:0000269|PubMed:7671306}.
CC   -!- PTM: Requires cleavage for activation (presumably).
CC       {ECO:0000269|PubMed:9477324}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; U29153; AAA83086.1; -; mRNA.
DR   EMBL; AE014296; AAF50656.1; -; Genomic_DNA.
DR   PIR; A57096; A57096.
DR   RefSeq; NP_523947.2; NM_079223.2.
DR   AlphaFoldDB; P98159; -.
DR   SMR; P98159; -.
DR   BioGRID; 64189; 1.
DR   IntAct; P98159; 3.
DR   STRING; 7227.FBpp0076693; -.
DR   MEROPS; S01.013; -.
DR   GlyCosmos; P98159; 25 sites, No reported glycans.
DR   GlyGen; P98159; 25 sites.
DR   iPTMnet; P98159; -.
DR   PaxDb; 7227-FBpp0076693; -.
DR   EnsemblMetazoa; FBtr0076984; FBpp0076693; FBgn0002926.
DR   GeneID; 38738; -.
DR   KEGG; dme:Dmel_CG10129; -.
DR   UCSC; CG10129-RA; d. melanogaster.
DR   AGR; FB:FBgn0002926; -.
DR   CTD; 38738; -.
DR   FlyBase; FBgn0002926; ndl.
DR   VEuPathDB; VectorBase:FBgn0002926; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_228608_0_0_1; -.
DR   InParanoid; P98159; -.
DR   OMA; DCMSAFL; -.
DR   OrthoDB; 3035825at2759; -.
DR   PhylomeDB; P98159; -.
DR   BioGRID-ORCS; 38738; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 38738; -.
DR   PRO; PR:P98159; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0002926; Expressed in egg chamber and 5 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0098595; C:perivitelline space; IDA:FlyBase.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IMP:FlyBase.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR   GO; GO:0007343; P:egg activation; IMP:FlyBase.
DR   GO; GO:0007306; P:egg chorion assembly; IMP:FlyBase.
DR   GO; GO:0016540; P:protein autoprocessing; IMP:FlyBase.
DR   GO; GO:0016485; P:protein processing; IMP:FlyBase.
DR   GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR   GO; GO:0160032; P:Toll receptor ligand protein activation cascade; IDA:FlyBase.
DR   GO; GO:0031638; P:zymogen activation; IMP:FlyBase.
DR   CDD; cd00112; LDLa; 7.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR015420; Peptidase_S1A_nudel.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24258:SF151; SERINE PROTEASE NUDEL; 1.
DR   PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR   Pfam; PF09342; DUF1986; 1.
DR   Pfam; PF00057; Ldl_recept_a; 4.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 9.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 7.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS01209; LDLRA_1; 6.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS50240; TRYPSIN_DOM; 2.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P98159; DM.
PE   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Hydrolase; Phosphoprotein; Protease; Proteoglycan; Reference proteome;
KW   Repeat; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..2616
FT                   /note="Serine protease nudel"
FT                   /id="PRO_0000028136"
FT   REPEAT          261..269
FT                   /note="WIID 1"
FT   REPEAT          320..328
FT                   /note="WIID 2"
FT   REPEAT          399..407
FT                   /note="WIID 3"
FT   REPEAT          446..454
FT                   /note="WIID 4"
FT   REPEAT          477..485
FT                   /note="WIID 5"
FT   REPEAT          528..536
FT                   /note="WIID 6"
FT   DOMAIN          889..929
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          929..956
FT                   /note="LDL-receptor class A 2; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          955..1006
FT                   /note="LDL-receptor class A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          1145..1383
FT                   /note="Peptidase S1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DOMAIN          1394..1432
FT                   /note="LDL-receptor class A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          1713..1743
FT                   /note="LDL-receptor class A 5; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          1745..1775
FT                   /note="LDL-receptor class A 6; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          1774..1813
FT                   /note="LDL-receptor class A 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          2027..2301
FT                   /note="Peptidase S1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DOMAIN          2308..2346
FT                   /note="LDL-receptor class A 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          2349..2389
FT                   /note="LDL-receptor class A 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          2387..2419
FT                   /note="LDL-receptor class A 10; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          2419..2459
FT                   /note="LDL-receptor class A 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   REGION          352..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1530..1557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1683..1704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1031..1033
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        1185
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1233
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1332
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         574
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        794
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        827
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        829
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        861
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        975
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1064
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1878
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1956
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2023
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2601
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        891..905
FT                   /evidence="ECO:0000250"
FT   DISULFID        899..918
FT                   /evidence="ECO:0000250"
FT   DISULFID        912..927
FT                   /evidence="ECO:0000250"
FT   DISULFID        957..982
FT                   /evidence="ECO:0000250"
FT   DISULFID        964..995
FT                   /evidence="ECO:0000250"
FT   DISULFID        989..1004
FT                   /evidence="ECO:0000250"
FT   DISULFID        1170..1186
FT                   /evidence="ECO:0000250"
FT   DISULFID        1276..1338
FT                   /evidence="ECO:0000255"
FT   DISULFID        1305..1317
FT                   /evidence="ECO:0000250"
FT   DISULFID        1328..1359
FT                   /evidence="ECO:0000250"
FT   DISULFID        1396..1408
FT                   /evidence="ECO:0000250"
FT   DISULFID        1401..1421
FT                   /evidence="ECO:0000250"
FT   DISULFID        1415..1430
FT                   /evidence="ECO:0000250"
FT   DISULFID        1728..1745
FT                   /evidence="ECO:0000250"
FT   DISULFID        1734..1764
FT                   /evidence="ECO:0000250"
FT   DISULFID        1758..1773
FT                   /evidence="ECO:0000250"
FT   DISULFID        1776..1789
FT                   /evidence="ECO:0000250"
FT   DISULFID        1783..1802
FT                   /evidence="ECO:0000250"
FT   DISULFID        1796..1811
FT                   /evidence="ECO:0000250"
FT   DISULFID        2055..2071
FT                   /evidence="ECO:0000250"
FT   DISULFID        2177..2230
FT                   /evidence="ECO:0000250"
FT   DISULFID        2310..2320
FT                   /evidence="ECO:0000250"
FT   DISULFID        2315..2333
FT                   /evidence="ECO:0000250"
FT   DISULFID        2327..2344
FT                   /evidence="ECO:0000250"
FT   DISULFID        2351..2364
FT                   /evidence="ECO:0000250"
FT   DISULFID        2358..2377
FT                   /evidence="ECO:0000250"
FT   DISULFID        2371..2387
FT                   /evidence="ECO:0000250"
FT   DISULFID        2421..2435
FT                   /evidence="ECO:0000250"
FT   DISULFID        2428..2448
FT                   /evidence="ECO:0000250"
FT   DISULFID        2442..2457
FT                   /evidence="ECO:0000250"
FT   CONFLICT        83
FT                   /note="I -> T (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="F -> L (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="N -> T (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        831
FT                   /note="Q -> R (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        864
FT                   /note="N -> S (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1150
FT                   /note="Y -> H (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1344
FT                   /note="P -> A (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1410
FT                   /note="A -> S (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1607
FT                   /note="I -> M (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1632
FT                   /note="K -> I (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1670
FT                   /note="L -> P (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1794
FT                   /note="S -> K (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1863
FT                   /note="D -> N (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1886..1888
FT                   /note="HEM -> QEK (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1903
FT                   /note="S -> A (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2147
FT                   /note="H -> N (in Ref. 1; AAA83086)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2616 AA;  292492 MW;  052F92CBAE9EB163 CRC64;
     MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV VEKIDQVQQI
     AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK DMEDSKNRRR KHMRQMLVKF
     RLNKKHRMRR DLHGLDLLDP VRMEANMQHL YTKLRSKRAR EALSQLEHEF VRCKKHTPQD
     CMSAFLRMYK MAKEVTEKME KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA
     TTVAVHATEK PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT
     TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT TSASSEPIVD
     TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD WILDGEENVE PEVKSTNTTT
     TTAATTTTGA TSETIIVTTE LPKITFDWII DGREVVEPQE TTTEVTGTTE RLRKMPFDWI
     IDGEEVVEPQ ENVTTTTIAT TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE
     VSTSSTSQPK LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES
     SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN PLNGHTWNAA
     DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV QFTSRAPGGF PVSGETMKAS
     AQFMFNPNFG MPSIPVCFYM TPANFRMPMW SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ
     FGPSGNFFGG SGGSGAGGQG ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS
     QQQQGGQSAF SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF
     GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED ELGCFGCESL
     AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD EEQCSMLVTD VADHMSHGAS
     ASEGYLYHNY RGDWHPVCNN GEKWAALACQ MDENSRMDHS ASLNVSFQTL TLPGPFIEPS
     LHAGVHFAQA CHGRNSHDSL VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV
     GDGRIVGGSY TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG
     LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK PICLPDKGRT
     TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP IRKKCTDPED QASEDICAGD
     PDGGRDACQG DSGGPLFCRS VSNPDEFYLA GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM
     ATTPRLLPKL QPLQLCPGFI CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG
     GVRQNISTTT ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ
     GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS TWLPSTNIET
     STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT DLVTEFIEST TFETTMEVET
     TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT ISSIVTLTTT PLATISTTIL TTEKHVAVTT
     LAPTTTTESA KTTTTHSSST HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE
     LDCTCKDYLK GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV
     DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH ETGYHEHQAK
     TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN RMSAQIHSMV GDNVQFTENE
     VIIPELGHPS ASRPEKDRLL PRKCVGIYVE CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV
     LSPTIETHNT PNVHFKPQIP AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH
     WPWLADVYMN GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH
     EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ CISVLHDDAT
     GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA EDMASISEEV ELINGVAPTE
     LPAITKFTTC NQFGLKNVSD AHHNPSDQGV LVCRDSHTGW FPTALFNYNN SDCQSFKQPF
     GIRTLELVYK SLQDIIDKPS CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE
     ETKCRQQKQQ CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK
     ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN GEDERYCFGI
     EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK CFPKSKPPQV DEVREICKKL
     GYNPYRQPSY RLIDDEENKP VHTYELADRQ GRSFSNESLM GKYRDSTKAL IISKFSPLQL
     NERLTLFLKS SRPIAELVRW NATDSSMCYR LEIRCA
//