NUDEL_DROME
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 03-AUG-2022, entry version 173.
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 GlyGen; P98159; 25 sites.
DR iPTMnet; P98159; -.
DR PaxDb; P98159; -.
DR PRIDE; P98159; -.
DR EnsemblMetazoa; FBtr0076984; FBpp0076693; FBgn0002926.
DR GeneID; 38738; -.
DR KEGG; dme:Dmel_CG10129; -.
DR UCSC; CG10129-RA; d. melanogaster.
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; 1314811at2759; -.
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 tissues.
DR Genevisible; P98159; DM.
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:eggshell chorion assembly; IMP:FlyBase.
DR GO; GO:0007313; P:maternal specification of dorsal/ventral axis, oocyte, soma encoded; IEA:InterPro.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IDA: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:0031638; P:zymogen activation; IMP:FlyBase.
DR CDD; cd00112; LDLa; 7.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.400.10; -; 7.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR034381; Nudel.
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:SF133; PTHR24258:SF133; 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; SSF50494; SSF50494; 2.
DR SUPFAM; SSF57424; SSF57424; 7.
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.
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
