CAD99_DROME
ID CAD99_DROME Reviewed; 1706 AA.
AC Q9VAF5; Q5D716; Q5U133; Q961C6; Q9VAF6;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cadherin-99C {ECO:0000303|PubMed:15708564};
DE Flags: Precursor;
GN Name=Cad99C {ECO:0000303|PubMed:15708564, ECO:0000312|FlyBase:FBgn0039709};
GN ORFNames=CG31009 {ECO:0000312|FlyBase:FBgn0039709};
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|EMBL:AAX12107.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=15708564; DOI=10.1016/j.ydbio.2004.12.008;
RA Schlichting K., Demontis F., Dahmann C.;
RT "Cadherin Cad99C is regulated by Hedgehog signaling in Drosophila.";
RL Dev. Biol. 279:142-154(2005).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:AAV36944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-1706.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAV36944.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16260500; DOI=10.1083/jcb.200507072;
RA D'Alterio C., Tran D.D., Yeung M.W., Hwang M.S., Li M.A., Arana C.J.,
RA Mulligan V.K., Kubesh M., Sharma P., Chase M., Tepass U., Godt D.;
RT "Drosophila melanogaster Cad99C, the orthologue of human Usher cadherin
RT PCDH15, regulates the length of microvilli.";
RL J. Cell Biol. 171:549-558(2005).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16507588; DOI=10.1242/jcs.02831;
RA Schlichting K., Wilsch-Braeuninger M., Demontis F., Dahmann C.;
RT "Cadherin Cad99C is required for normal microvilli morphology in Drosophila
RT follicle cells.";
RL J. Cell Sci. 119:1184-1195(2006).
RN [7] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=24718992; DOI=10.1242/dev.104166;
RA Chung S., Andrew D.J.;
RT "Cadherin 99C regulates apical expansion and cell rearrangement during
RT epithelial tube elongation.";
RL Development 141:1950-1960(2014).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CK.
RX PubMed=25236597; DOI=10.1242/jcs.099242;
RA Glowinski C., Liu R.H., Chen X., Darabie A., Godt D.;
RT "Myosin VIIA regulates microvillus morphogenesis and interacts with
RT cadherin Cad99C in Drosophila oogenesis.";
RL J. Cell Sci. 127:4821-4832(2014).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY BACTERIAL URACIL, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
RN [10]
RP INTERACTION WITH CK AND CUL1; UBR3.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
CC -!- FUNCTION: Cadherin that functions in epithelial morphogenesis and the
CC intestine epithelial immune response (PubMed:16260500, PubMed:16507588,
CC PubMed:24718992, PubMed:25639794). Essential for female fertility
CC (PubMed:16260500, PubMed:16507588). Regulates the length and
CC organization of apical microvilli in developing follicle cells and
CC salivary glands (PubMed:16260500, PubMed:16507588, PubMed:24718992,
CC PubMed:25236597). Function in the follicle cell is essential for egg
CC development as the microvilli secrete eggshell material such as the
CC vitelline membrane (PubMed:16260500, PubMed:16507588, PubMed:25236597).
CC Acts at least in part by regulating the recruitment of the myosin ck to
CC the follicle cell microvilli (PubMed:25236597). Also required to
CC regulate cell rearrangements during salivary tube elongation, possibly
CC by modulating cellular adhesion between the apical surface and apical
CC extracellular matrix during epithelial tube elongation
CC (PubMed:24718992). May also function in cellular adhesion during the
CC development of other tubular epithelia such as the trachea
CC (PubMed:24718992). Possibly functions as an apical membrane determinant
CC which acts in apical membrane expansion during salivary and tracheal
CC epithelial tube elongation (PubMed:24718992). In salivary gland
CC development, this function is independent of the other apical membrane
CC determinants crb and sas (PubMed:24718992). Essential downstream
CC component of a hh-signaling pathway which regulates the Duox-dependent
CC gut epithelial immune response to bacterial uracil; required for
CC endosome formation in the enterocyte and activating norpA-dependent
CC Ca2+ mobilization, which are essential steps in the Duox-dependent
CC production of reactive oxygen species (ROS) in response to intestinal
CC bacterial infection (PubMed:25639794). {ECO:0000269|PubMed:16260500,
CC ECO:0000269|PubMed:16507588, ECO:0000269|PubMed:24718992,
CC ECO:0000269|PubMed:25236597, ECO:0000269|PubMed:25639794}.
CC -!- SUBUNIT: Interacts (via the cytoplasmic domain) with ck
CC (PubMed:25236597, PubMed:27331610). Interacts (via the cytoplasmic
CC domain) with Cul1 and Ubr3 (PubMed:27331610).
CC {ECO:0000269|PubMed:25236597, ECO:0000269|PubMed:27331610}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:16260500, ECO:0000269|PubMed:16507588}; Single-pass
CC type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:25639794}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:16260500, ECO:0000269|PubMed:16507588,
CC ECO:0000269|PubMed:25639794}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Dispersed throughout the enterocyte membrane, but
CC becomes clustered in the brush border membrane in response to uracil.
CC {ECO:0000269|PubMed:25639794}.
CC -!- DEVELOPMENTAL STAGE: Low expression throughout the imaginal disks of
CC third instar larvae with higher levels of expression at the anterior-
CC posterior boundary (at protein level) (PubMed:15708564). Detected in
CC the germarium and stage 2 and stage 3 egg chambers (at protein level)
CC (PubMed:16507588). From stages 2 to 8, expressed in the follicle cells
CC at the anterior and posterior poles of the egg chambers (at protein
CC level) (PubMed:16260500, PubMed:16507588). From stage 4 to the end of
CC oogenesis, only detected in follicle cells that are in contact with the
CC oocyte (at protein level) (PubMed:16260500, PubMed:16507588). From
CC stage 11 expressed at the apical surface of several embryonic tubular
CC organs including the salivary glands, trachea, foregut and hindgut
CC (PubMed:24718992). {ECO:0000269|PubMed:15708564,
CC ECO:0000269|PubMed:16260500, ECO:0000269|PubMed:16507588,
CC ECO:0000269|PubMed:24718992}.
CC -!- INDUCTION: Up-regulated in the adult anterior midgut after the
CC ingestion of bacterial uracil. Strong up-regulation detected 1 hour, 2
CC hours and 16 hours after ingestion, whereas no up-regulation was
CC detected at 4 hours. {ECO:0000269|PubMed:25639794}.
CC -!- DOMAIN: The extracellular domain is necessary for conferring apical
CC characteristics on the salivary gland membrane (PubMed:24718992).
CC Necessary for regulating salivary gland membrane expansion and tube
CC length, but is not required for cell rearrangement during tube
CC elongation (PubMed:24718992). Sufficient to promote the outgrowth of
CC follicle cell microvilli and the formation of microvilli bundles
CC (PubMed:16260500, PubMed:24718992) Sufficient to promote formation of
CC microvilli-like structures in the salivary glands and the follicle cell
CC microvilli bundles (PubMed:16507588, PubMed:24718992). Dispensable for
CC apical localization (PubMed:24718992). {ECO:0000269|PubMed:16260500,
CC ECO:0000269|PubMed:16507588, ECO:0000269|PubMed:24718992}.
CC -!- DOMAIN: The cytoplasmic domain is necessary for the formation of
CC uracil-induced endosomes. {ECO:0000269|PubMed:25639794}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain (By similarity).
CC {ECO:0000250|UniProtKB:P12830}.
CC -!- DISRUPTION PHENOTYPE: Females display reduced fertility as well as
CC defective eggshell development (PubMed:16260500). Ovarian follicle cell
CC microvilli are abnormally shaped and display a range of defects
CC including decreased length, reduced number and an irregular
CC distribution pattern, leading to impaired vitelline membrane formation
CC (PubMed:16260500, PubMed:16507588). In the intestines of 3-day old
CC adults there is no formation of endosomes and consequently no DUOX-
CC dependent up-regulation of reactive oxygen species (ROS) in response to
CC the ingestion of bacteria-derived uracil (PubMed:25639794). Embryos
CC display irregular cell rearrangements during salivary gland development
CC with fewer cells surrounding the salivary gland lumens and lumens
CC appear to be elongated (PubMed:24718992). {ECO:0000269|PubMed:16260500,
CC ECO:0000269|PubMed:16507588, ECO:0000269|PubMed:24718992,
CC ECO:0000269|PubMed:25639794}.
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DR EMBL; AY853687; AAX12107.1; -; mRNA.
DR EMBL; AY853686; AAX12106.1; -; mRNA.
DR EMBL; AE014297; AAF56955.2; -; Genomic_DNA.
DR EMBL; AE014297; ADV37401.1; -; Genomic_DNA.
DR EMBL; BT016059; AAV36944.1; -; mRNA.
DR RefSeq; NP_001189311.1; NM_001202382.1.
DR RefSeq; NP_733314.1; NM_170435.2.
DR AlphaFoldDB; Q9VAF5; -.
DR SMR; Q9VAF5; -.
DR IntAct; Q9VAF5; 2.
DR STRING; 7227.FBpp0292214; -.
DR GlyGen; Q9VAF5; 11 sites.
DR PaxDb; Q9VAF5; -.
DR EnsemblMetazoa; FBtr0085488; FBpp0084854; FBgn0039709.
DR EnsemblMetazoa; FBtr0303095; FBpp0292214; FBgn0039709.
DR GeneID; 43528; -.
DR KEGG; dme:Dmel_CG31009; -.
DR UCSC; CG31009-RA; d. melanogaster.
DR CTD; 43528; -.
DR FlyBase; FBgn0039709; Cad99C.
DR VEuPathDB; VectorBase:FBgn0039709; -.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_003665_0_0_1; -.
DR InParanoid; Q9VAF5; -.
DR OMA; DPTGPNN; -.
DR OrthoDB; 21247at2759; -.
DR PhylomeDB; Q9VAF5; -.
DR SignaLink; Q9VAF5; -.
DR BioGRID-ORCS; 43528; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43528; -.
DR PRO; PR:Q9VAF5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039709; Expressed in epithelial cell and 18 other tissues.
DR ExpressionAtlas; Q9VAF5; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR GO; GO:0005902; C:microvillus; IDA:FlyBase.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IGI:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
DR GO; GO:0007304; P:chorion-containing eggshell formation; IMP:FlyBase.
DR GO; GO:0032529; P:follicle cell microvillus organization; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:FlyBase.
DR GO; GO:0032533; P:regulation of follicle cell microvillus length; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
DR GO; GO:0007305; P:vitelline membrane formation involved in chorion-containing eggshell formation; IMP:FlyBase.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR Pfam; PF00028; Cadherin; 8.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 11.
DR SUPFAM; SSF49313; SSF49313; 10.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 11.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Endosome; Glycoprotein; Immunity;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1706
FT /note="Cadherin-99C"
FT /evidence="ECO:0000255"
FT /id="PRO_5008180598"
FT TOPO_DOM 29..1395
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1396..1416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1417..1706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 68..142
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 143..264
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 277..387
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 388..500
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 519..604
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 605..704
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 707..807
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 808..908
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 909..1005
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1038..1148
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1156..1270
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 61
FT /note="P -> A (in Ref. 1; AAX12106/AAX12107)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="V -> I (in Ref. 1; AAX12106/AAX12107)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="G -> E (in Ref. 1; AAX12106/AAX12107)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="K -> R (in Ref. 1; AAX12106/AAX12107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1706 AA; 186874 MW; 2A2CB6F3D5561D8B CRC64;
MAARNSLTPQ QGLGFFGLLI LLCSAVLGKS QMCEVETGQT NIILDIEESR ESFIGQPTTP
PELPIFGDPD TEIALNLVFP KGQPIFQLNG KKLQLLQPLD RDEENLSHIV FQVSCTTRST
GKKRTIPIIV RVSDINDNAP RFMNTPYEVT VPESTPVGTT IFRNIQALDK DAGVNGLVEY
FIAEGSPNST NVEKYSADGY GTFAISFPHQ GQVTVAKTLD FEKIQTYYLT IVASDRARNT
ADRLSSTTTL TVNIADSNDL DPSFIYSGCV SLDGACINPE YSASVPAGSL LGVLTVLPER
IQAVDLDTIN SPIRYSFASG MPGNYADYFQ IDESTGVLKQ TKAVDTSTAK KYDIIVKAEE
VSPGPQRFTT AKLEIFVKPV DANPPVISSS QAEGYVDENS PIGTRVLDAH GNPISFMTTD
ADLSDSDPKP DYIYELTTPS FNVTGDGILV VNEENLDRDP PAPGRFKFQV VAREPRTNAA
SAPLSLTVHL RDVNDNAPKL AMVAPISITA GDQSESRLVT QVTATDNDEG PNAVVTYSIY
HVSNNGIQKF TINATTGEIR TQGRLLAGEQ YSITVQATDI GGLSSQAIVE VSVTPGPNTK
PPRFQKPIYE VQVSEGAEIN STVTVVHAED PENDAVVYSI ISGNDLRQFA VGQESGVIIV
IRKLDRESLT RYQLILKAED TGGLSSSATV NIKVTDINDK NPEFEASTLP YVFQVEEGKA
QASVGVVHAT DADEGINAEI TYSIPTDIPF TINATSGEIL TAKELDYEQL NEYKFVVTAK
DGAPDARLGT ASVTVMVLDL PDEVPKFSDA RIDVHIPENE ENFLVATVQA FDPDSMPEIT
YVLRKGNAEL FKVSEKSGEV RTIKGLDYES QKQHQLTIGT IENDGNGPGD TILLVVDVED
RNDLPPRFIT VPDPVTVNDD QGIGTIIATL PAIDGDGTSP GNVVRYEIVG RGKAPKYFQV
DPDTGAVRIR DELRKEEDTE YQVDIRAYDL GEPQLSSVAP LRVDVHHLLS SGNNEIKLDN
KLESGTGMSS ESIGLAFSDD SYTTSVPESM EANSTLKLIQ IVNSKTSGDG PPAFRCEFVS
GNGGGIFNLS SADHGCNLLL IQPLDFENKS SYSLQLRLTS HRYFVNPLKD TTSVEIIVQD
ENDNAPEFEF NRLRGQQDTF YTVVTEEMDV DTTILQVRAT DRDSGKFGTV RYTLYDDDEN
RVNMPTSFFM MSEDTGVLRT AKHFKNENDF PLTFLVEARD SDGQEQGSHR TRARIVVNKL
ADINRMALSF PNAAPSDLRN YYTELEELLD KKTGLVSGIE RMSSQKYLAK NGSVIENPAA
TDIWFYLIDP KTEQLVSRKD SIVETTLLEP AARSELNIAL PRATAENISF PLERKEHVHK
VKAAVAIDNE VFPFTLIAIS LVILILGTIG IIYICISWSK YKNFKQRMRQ YSSTNPPRYD
PVIVNQQASS ASETIANMKE YETQMLAMAV PPDVDDDLQL DFSAKNHAFS LDNVSYITHK
ENTNGGGQSS PSHSDATTAT IATLRRHKNL NNASMNNNLA INNRQNTFNR TLEMNTRNNA
NPLASPPNGA LSGTLTLGRI KHQNSNHYQN GAYNIDPTGP NNMAHAKNNA YSTMGRRGNT
FGDVGLLNGN GELMNATLGR NGQLNNRLYG GEVPITNPLF QRSNSDHNHL SSTNENVSFG
KRDYGQIGFS YLNDLDRSEV ETTTEL
