NDG_DROME
ID NDG_DROME Reviewed; 1350 AA.
AC A1Z877; A1Z876; B7FNR1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nidogen {ECO:0000303|PubMed:30260959, ECO:0000312|FlyBase:FBgn0026403};
DE AltName: Full=Entactin {ECO:0000303|PubMed:30260959, ECO:0000312|FlyBase:FBgn0026403};
DE Flags: Precursor;
GN Name=Ndg {ECO:0000303|PubMed:30260959, ECO:0000312|FlyBase:FBgn0026403};
GN ORFNames=CG12908 {ECO:0000312|FlyBase:FBgn0026403};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:ABX00771.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABX00771.1};
RC TISSUE=Larva {ECO:0000312|EMBL:ABX00771.1}, and
RC Pupae {ECO:0000312|EMBL:ABX00771.1};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:ACK77669.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACK77669.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ACK77669.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=30260959; DOI=10.1371/journal.pgen.1007483;
RA Dai J., Estrada B., Jacobs S., Sanchez-Sanchez B.J., Tang J., Ma M.,
RA Magadan-Corpas P., Pastor-Pareja J.C., Martin-Bermudo M.D.;
RT "Dissection of Nidogen function in Drosophila reveals tissue-specific
RT mechanisms of basement membrane assembly.";
RL PLoS Genet. 14:E1007483-E1007483(2018).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30567930; DOI=10.1242/dev.168948;
RA Wolfstetter G., Dahlitz I., Pfeifer K., Toepfer U., Alt J.A., Pfeifer D.C.,
RA Lakes-Harlan R., Baumgartner S., Palmer R.H., Holz A.;
RT "Characterization of Drosophila Nidogen/entactin reveals roles in basement
RT membrane stability, barrier function and nervous system patterning.";
RL Development 146:0-0(2019).
CC -!- FUNCTION: Cell adhesion glycoprotein which is widely distributed in
CC basement membranes (PubMed:30260959, PubMed:30567930). Involved in
CC cell-extracellular matrix (ECM) interactions probably by connecting the
CC laminin and collagen IV networks (PubMed:30260959, PubMed:30567930).
CC Required for permeability and mechanical stability of basement
CC membranes, and ECM dependent neural plasticity (PubMed:30567930). Not
CC involved in assembly of the embryonic basement membrane
CC (PubMed:30567930). {ECO:0000269|PubMed:30260959,
CC ECO:0000269|PubMed:30567930}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30260959}. Secreted,
CC extracellular space, extracellular matrix, basement membrane
CC {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}.
CC Note=Secreted in the hemolymph (PubMed:30260959). Localization to the
CC basal membranes depends on laminin (PubMed:30260959, PubMed:30567930).
CC {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}.
CC -!- TISSUE SPECIFICITY: Expressed in the basement membrane around the
CC follicular epithelium of the adult ovary (at protein level).
CC {ECO:0000269|PubMed:30260959}.
CC -!- DEVELOPMENTAL STAGE: Expressed in different patterns throughout
CC embryogenesis (at protein levels) (PubMed:30260959, PubMed:30567930).
CC At stage 11/12, embeds dorsal median cells and somatic myoblasts
CC forming a thin layer between the ectoderm and the mesoderm and around
CC the prospective anal plate (PubMed:30567930). At stage 12, after germ
CC band retraction, accumulates in the forming basal membranes around the
CC developing brain and ventral nerve cord, in the differentiating
CC tracheal system, in the future digestive tract as well as in the
CC forming somatic muscles (PubMed:30567930). At stage 13, accumulates
CC around caudal visceral mesodermal cells (PubMed:30260959). At stage 16,
CC expressed in the basal membrane surrounding most tissues, including
CC muscles, gut and larval ventral nerve cord, brain, and in chordotonal
CC organs (at protein level) (PubMed:30260959, PubMed:30567930). Expressed
CC in embryonic macrophages (at protein level) (PubMed:30260959). In the
CC larva, expressed mainly by fat body adipocytes and blood cells in the
CC basal membranes that surround the fat body, imaginal disks, tracheae,
CC salivary glands, midgut, mature muscles and heart (at protein level)
CC (PubMed:30260959). Expressed during embryogenesis: at stage 11/12
CC detected in single cells of the head, especially in the gnathal
CC segments as well as in segmentally located patches of cells in the
CC dorsal mesoderm, detected in the midline-associated, mesodermal dorsal
CC median cells and somatic myoblasts (PubMed:30567930). Only low
CC expression in the amnioserosa (PubMed:30567930). After germ band
CC retraction (stage 12), expressed in the forming dorsal and ventral
CC muscles, the amnioserosa and the segmentally located chordotonal organs
CC (PubMed:30567930). Expressed in the esophageal visceral muscle
CC primordium and in the joint region between hind- and midgut
CC (PubMed:30567930). At stage 16, expressed in somatic and visceral
CC muscles, and in the cap cells of the chordotonal organs
CC (PubMed:30567930). {ECO:0000269|PubMed:30260959,
CC ECO:0000269|PubMed:30567930}.
CC -!- DOMAIN: The NIDO domain (also known as globular region 1 or G1)
CC contributes to the localization to the basal membrane probably by
CC binding to vkg. {ECO:0000269|PubMed:30260959}.
CC -!- DOMAIN: The EGF-like 1 and nidogen G2 beta-barrel domain (also known as
CC globular region 2 or G2) contribute to the localization to the basal
CC membrane probably by binding to vkg. {ECO:0000269|PubMed:30260959}.
CC -!- DOMAIN: The EGF-like 2-8 domains (also known as the ROD domain) is
CC necessary but not sufficient for localization to the basal membrane.
CC {ECO:0000269|PubMed:30260959}.
CC -!- DOMAIN: The LDL-receptor class B 1-4 domains (also known as globular
CC region 3 or G3) is necessary for cell-extracellular matrix (ECM)
CC interactions. Also, contributes to the localization to the basal
CC membrane probably by binding to laminins.
CC {ECO:0000269|PubMed:30260959}.
CC -!- DISRUPTION PHENOTYPE: Reduces fertility (PubMed:30260959,
CC PubMed:30567930). In larvae results in impaired climbing abilities and
CC in multiple holes in the basal membrane surrounding the fat body
CC adipose, the somatic muscles and the longitudinal and circular visceral
CC muscles, affecting permeability and mechanical stability of the
CC basement membrane (PubMed:30260959, PubMed:30567930). Impairs larvae
CC movement including reduced crawling speed, smaller stride frequency and
CC exploration area together with sudden motion defects in their crawling
CC pattern, such as head shaking, and spontaneous rolling and bending
CC (PubMed:30567930). Increases neuromuscular junction (NMJ) size
CC including abnormal branching numbers, overall branch length and
CC enhanced bouton density suggesting defective NMJ maturation
CC (PubMed:30567930). Reduces reaction to vibrational stimuli with partial
CC loss of alignment of sensory cilia and morphological defects of the
CC larval peripheral nervous system (PubMed:30567930). Results in smaller
CC pupae presenting an orientation shift of the pupal cases towards the
CC horizontal axis (PubMed:30567930). Results in incompletely inflated
CC wing blades in a small group of adults (PubMed:30567930).
CC {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}.
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DR EMBL; AE013599; AAF58809.3; -; Genomic_DNA.
DR EMBL; AE013599; AAS64880.2; -; Genomic_DNA.
DR EMBL; BT031149; ABX00771.1; -; mRNA.
DR EMBL; BT053751; ACK77669.1; -; mRNA.
DR RefSeq; NP_610575.1; NM_136731.2.
DR RefSeq; NP_995796.2; NM_206074.2.
DR AlphaFoldDB; A1Z877; -.
DR SMR; A1Z877; -.
DR IntAct; A1Z877; 1.
DR STRING; 7227.FBpp0087439; -.
DR GlyGen; A1Z877; 6 sites.
DR PaxDb; A1Z877; -.
DR PRIDE; A1Z877; -.
DR DNASU; 36089; -.
DR EnsemblMetazoa; FBtr0088349; FBpp0087438; FBgn0026403.
DR EnsemblMetazoa; FBtr0339459; FBpp0308545; FBgn0026403.
DR GeneID; 36089; -.
DR KEGG; dme:Dmel_CG12908; -.
DR UCSC; CG12908-RA; d. melanogaster.
DR UCSC; CG12908-RB; d. melanogaster.
DR CTD; 36089; -.
DR FlyBase; FBgn0026403; Ndg.
DR VEuPathDB; VectorBase:FBgn0026403; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000170029; -.
DR HOGENOM; CLU_003163_0_0_1; -.
DR OMA; HVSRLQF; -.
DR OrthoDB; 95286at2759; -.
DR PhylomeDB; A1Z877; -.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR Reactome; R-DME-977068; Termination of O-glycan biosynthesis.
DR SignaLink; A1Z877; -.
DR BioGRID-ORCS; 36089; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36089; -.
DR PRO; PR:A1Z877; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026403; Expressed in trunk mesoderm derivative and 35 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:FlyBase.
DR GO; GO:2001197; P:basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0071711; P:basement membrane organization; IMP:FlyBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0110011; P:regulation of basement membrane organization; IMP:UniProtKB.
DR CDD; cd00255; nidG2; 1.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.40.155.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR003886; NIDO_dom.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF06119; NIDO; 1.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 5.
DR SMART; SM00539; NIDO; 1.
DR SUPFAM; SSF54511; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51120; LDLRB; 4.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1350
FT /note="Nidogen"
FT /evidence="ECO:0000255"
FT /id="PRO_5015085945"
FT DOMAIN 107..260
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 281..321
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 325..550
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 545..583
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 591..631
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 788..829
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 832..874
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 912..953
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 955..996
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 997..1037
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1084..1126
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1127..1170
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1171..1216
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1257..1282
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REGION 645..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1032
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 285..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 292..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 309..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 549..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 556..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 595..608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 602..617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 619..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 792..804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 798..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 817..828
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 836..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 843..860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 862..873
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 916..927
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 921..938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 940..952
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 959..971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 965..982
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 984..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1001..1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1008..1023
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1025..1036
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 979
FT /note="N -> S (in Ref. 4; ACK77669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1350 AA; 149081 MW; 482243B79347A341 CRC64;
MPTFGSKLLA CLLLSSVILV SGQFEHYLDS LRASELYEFE DGSLGSIHLL PKGDSETIVL
QLEQPIHFYG EQYEQLYINT NGILTFNSEF PEYLNQPFPL EYASIAAFYS NVDTSFSDEG
TSISLFESKE QSILDRASSL VRYAFSSQSE FEARQVIVAT WRNVGYFDSK TDRLNTFQVA
LIANEQSTFV QFIYPDGGLN WLQGETAGLG LPDIRAQAGF VAEDGRFYTL NGSGSENARF
LSESTNLGVP GVWLFEVAPI ENEQNVRSPD NAESLTESPA LALSCQAHAH QCHEKAECHD
KAEGYCCVCG SGFYGNGKSC LANDQPIRVT GTLTGELNKQ PVSEEAKLQS YVVTSEGRTY
TTINPLTPEL GAQLRLVLPL LTTVPWLFAK SVGGVANGYQ LTGGVYTHVS RLQFDSGENL
HVNQTFEGLN YWDQLSVKIE IYGEVPAVAA DAVLILPDYV EEYTFERPGE LKSVQVLNIN
ITEEQRVLGL QVEQRILYRS CLRDDEADPS ATKVLQKISK VALDYVERDQ ALRIGAMSKV
GVTPESNACN DGTADCVENS VCVPYEDTYR CDCYHGFAAQ LDERGVEVCL DIDECATGSH
VCDENAVCDN TEGGFNCYCT EGFEGNGYRC LSNSTADNIE YPPAVEGQAE PTSEPSPNPS
PYPDQGQDQE REREDDQYPQ PNPYPYPEEQ IPQHPDECYR CSKDADCYQG RCTCHEGFDG
DGYTCTNICG HGEVWENGRC EPLLLERHDV DPLCDALGEC RCPYGYELSE DSQRCTYVQE
FDGERNADLI PCDVDENCHI NATCNWYGQE LRHICTCQPG FRGDGYNCDP ISDDSCAIRP
DICDVHADCV YEEHLGKSEC QCQAGYTGNG FNCQLAAECQ SAEHCGENAF CDDGVCRCQA
DFERDVSDRC VPAGRCGSVF CGSNAICKWD SAEGVQYCDC LDGYQGDALT GCTSKPLSCH
VLNNCGIHAT CEPTEDPANY ECQCIAGFKG DGYVCIEEQN CLNNPTLCDM NAQCRSTNSG
LVCVCNQGFF GNGSLCQERQ HQDSDFLIVS QGVMIARVPL NGRNVRPISV AQMAIGLDKD
CVEGRVYWGD ISTKKIVSTK YDGTDLRPFI TTDIESPEGI AIDVISRRLY WADSAKDTIE
VASLDDPSLR AVIINKQLVN PRGIAVDPYR EKLFWSDWDR ESPKIEMSNL DGTGRELLLG
KDDVTLPNSL VVLENSGEVC YADAGTKKVE CIEPQNRQIR TISNELSYPF GITFTHDQFY
WTDWTTKKVE IVDSLGARQT PIQPPFFGSH KMYGMTVVEQ HCPQYQSPCQ ISNGGCTDSR
LCLVNRQAPS GKSCKCTSAS TGCTVLAPGY
