SEELE_DROME
ID SEELE_DROME Reviewed; 189 AA.
AC Q7JXF7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein seele {ECO:0000312|EMBL:AAF58856.1};
DE Flags: Precursor;
GN Name=sel {ECO:0000312|FlyBase:FBgn0263260};
GN ORFNames=CG12918 {ECO:0000312|FlyBase:FBgn0263260};
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|EMBL:AAM11051.1};
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:AAM11051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11051.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM11051.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20970335; DOI=10.1016/j.cub.2010.09.069;
RA Stein D., Charatsi I., Cho Y.S., Zhang Z., Nguyen J., DeLotto R.,
RA Luschnig S., Moussian B.;
RT "Localization and activation of the Drosophila protease easter require the
RT ER-resident saposin-like protein seele.";
RL Curr. Biol. 20:1953-1958(2010).
CC -!- FUNCTION: Involved in embryonic dorsal-ventral patterning which is
CC generated by a series of serine protease processing events where gd
CC processes snk which cleaves ea which then processes spz into the
CC activating ligand for the Toll receptor. Required during this process
CC for the secretion of ea from the developing embryo into the
CC perivitelline space and for ea processing.
CC {ECO:0000269|PubMed:20970335}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:20970335}.
CC -!- DEVELOPMENTAL STAGE: Expressed in blastoderm embryos (at protein
CC level). Abundantly expressed in late-stage embryos including in the
CC developing salivary glands (at protein level).
CC {ECO:0000269|PubMed:20970335}.
CC -!- DISRUPTION PHENOTYPE: Formation of embryos with altered dorsal-ventral
CC patterning, dramatically decreased levels of ea in the perivitelline
CC space and reduced processing of ea. {ECO:0000269|PubMed:20970335}.
CC -!- SIMILARITY: Belongs to the canopy family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58856.1; -; Genomic_DNA.
DR EMBL; AY094698; AAM11051.1; -; mRNA.
DR RefSeq; NP_610547.1; NM_136703.5.
DR AlphaFoldDB; Q7JXF7; -.
DR IntAct; Q7JXF7; 3.
DR STRING; 7227.FBpp0087519; -.
DR PaxDb; Q7JXF7; -.
DR PRIDE; Q7JXF7; -.
DR DNASU; 36046; -.
DR EnsemblMetazoa; FBtr0088433; FBpp0087519; FBgn0263260.
DR GeneID; 36046; -.
DR KEGG; dme:Dmel_CG12918; -.
DR UCSC; CG12918-RA; d. melanogaster.
DR CTD; 36046; -.
DR FlyBase; FBgn0263260; sel.
DR VEuPathDB; VectorBase:FBgn0263260; -.
DR eggNOG; KOG3782; Eukaryota.
DR GeneTree; ENSGT00940000168977; -.
DR HOGENOM; CLU_095726_0_0_1; -.
DR InParanoid; Q7JXF7; -.
DR OMA; VWARRSQ; -.
DR OrthoDB; 1417418at2759; -.
DR PhylomeDB; Q7JXF7; -.
DR BioGRID-ORCS; 36046; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36046; -.
DR PRO; PR:Q7JXF7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0263260; Expressed in spermathecum and 44 other tissues.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0051087; F:chaperone binding; ISS:FlyBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:FlyBase.
DR GO; GO:0007311; P:maternal specification of dorsal/ventral axis, oocyte, germ-line encoded; HMP:FlyBase.
DR GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IMP:FlyBase.
DR GO; GO:0070613; P:regulation of protein processing; IMP:FlyBase.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:FlyBase.
DR InterPro; IPR042415; CNPY.
DR InterPro; IPR021852; DUF3456.
DR PANTHER; PTHR13341; PTHR13341; 1.
DR Pfam; PF11938; DUF3456; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..189
FT /note="Protein seele"
FT /id="PRO_5007711062"
FT DOMAIN 23..176
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT MOTIF 186..189
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 27..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 30..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 85..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 189 AA; 21301 MW; 7543184AE979DEB0 CRC64;
MLTKALILFG LLALAQGYSF TSREVKCHVC KAVVTELEEA IAKEDPHKMA DVSGFRLDAQ
GNSISKKVRL VKSEMFLTEL MEKICEKMDD YLKATYKSNG KFTLLKMIIN GQMNPDSSLV
DFVQDGDLNK SLGHFCNEVL EDNDEIFVKA FQAEELGNDL DIKICSEQAS YCDESPVQEE
YDFDGKEEL
