SP77B_DROME
ID SP77B_DROME Reviewed; 450 AA.
AC Q0E8C8; Q8IGD7; Q95SG7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Serine protease inhibitor 77Ba {ECO:0000303|PubMed:18854145};
DE Short=Serpin 77Ba {ECO:0000303|PubMed:18854145};
DE Flags: Precursor;
GN Name=Spn77Ba {ECO:0000312|FlyBase:FBgn0262057};
GN ORFNames=CG6680 {ECO:0000312|FlyBase:FBgn0262057};
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:AAL28354.1, ECO:0000312|EMBL:AAN71584.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28354.1, ECO:0000312|EMBL:AAN71584.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAL28354.1, ECO:0000312|EMBL:AAN71584.1};
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:0000312|EMBL:AGV77185.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18854145; DOI=10.1016/j.devcel.2008.08.017;
RA Tang H., Kambris Z., Lemaitre B., Hashimoto C.;
RT "A serpin that regulates immune melanization in the respiratory system of
RT Drosophila.";
RL Dev. Cell 15:617-626(2008).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22227521; DOI=10.1038/emboj.2011.476;
RA Nam H.J., Jang I.H., You H., Lee K.A., Lee W.J.;
RT "Genetic evidence of a redox-dependent systemic wound response via Hayan
RT protease-phenoloxidase system in Drosophila.";
RL EMBO J. 31:1253-1265(2012).
CC -!- FUNCTION: Serine protease inhibitor which plays an essential role in
CC regulating the tracheal melanization immune response to bacterial and
CC fungal infection (PubMed:18854145, PubMed:22227521). Acts by negatively
CC regulating a protease cascade involving Mp1 and Sp7, that functions in
CC the activation of the Hayan-phenoloxidase (PPO1) cascade
CC (PubMed:18854145). {ECO:0000269|PubMed:18854145,
CC ECO:0000269|PubMed:22227521}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:18854145}. Note=Detected in the extracellular space
CC at the apical surface of tracheal cells. {ECO:0000269|PubMed:18854145}.
CC -!- DEVELOPMENTAL STAGE: In larvae, highly expressed in the tracheal
CC system. Weak expression is also detected in other larval tissues
CC including the gut and epidermis. {ECO:0000269|PubMed:18854145}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in spontaneous
CC melanization of the tracheal system in larvae and pupae
CC (PubMed:18854145, PubMed:22227521). Displays melanization at the 2nd or
CC 3rd larval stage and affected larvae die a few days after it first
CC occurs (PubMed:18854145). Melanization is first detected between
CC tracheal cells and the overlying cuticle, then increases in intensity
CC and spreads to the epithelial layer of the affected tracheal cells
CC (PubMed:18854145). Increased expression of the antimicrobial gene Drs
CC in the trachea and fat body (PubMed:18854145).
CC {ECO:0000269|PubMed:18854145, ECO:0000269|PubMed:22227521}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49033.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF49034.2; -; Genomic_DNA.
DR EMBL; AE014296; AHN58153.1; -; Genomic_DNA.
DR EMBL; AY060806; AAL28354.1; -; mRNA.
DR EMBL; BT001829; AAN71584.1; -; mRNA.
DR EMBL; BT150283; AGV77185.1; -; mRNA.
DR RefSeq; NP_001287128.1; NM_001300199.1.
DR RefSeq; NP_649205.3; NM_140948.4.
DR RefSeq; NP_730512.2; NM_168844.3.
DR AlphaFoldDB; Q0E8C8; -.
DR SMR; Q0E8C8; -.
DR IntAct; Q0E8C8; 1.
DR STRING; 7227.FBpp0074610; -.
DR MEROPS; I04.092; -.
DR GlyGen; Q0E8C8; 3 sites.
DR PaxDb; Q0E8C8; -.
DR PRIDE; Q0E8C8; -.
DR EnsemblMetazoa; FBtr0074841; FBpp0074610; FBgn0262057.
DR EnsemblMetazoa; FBtr0074842; FBpp0074611; FBgn0262057.
DR EnsemblMetazoa; FBtr0345816; FBpp0311802; FBgn0262057.
DR GeneID; 40234; -.
DR KEGG; dme:Dmel_CG6680; -.
DR UCSC; CG6680-RA; d. melanogaster.
DR CTD; 40234; -.
DR FlyBase; FBgn0262057; Spn77Ba.
DR VEuPathDB; VectorBase:FBgn0262057; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000171113; -.
DR HOGENOM; CLU_023330_0_1_1; -.
DR InParanoid; Q0E8C8; -.
DR OMA; KPFQYMI; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q0E8C8; -.
DR Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-DME-375276; Peptide ligand-binding receptors.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 40234; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40234; -.
DR PRO; PR:Q0E8C8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262057; Expressed in crop (Drosophila) and 20 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035009; P:negative regulation of melanization defense response; IMP:FlyBase.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISM:FlyBase.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Melanin biosynthesis; Protease inhibitor; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..450
FT /note="Serine protease inhibitor 77Ba"
FT /id="PRO_5007922613"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 52
FT /note="S -> N (in Ref. 3; AAN71584)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="V -> A (in Ref. 3; AAL28354)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="I -> F (in Ref. 3; AAN71584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 50163 MW; C633F8960EE6F367 CRC64;
MGKIADCLML WIPLLLGAIF LCSADPQNNQ APLQLSVGNP LTAFTAPTAF QSGVSHIQSM
RSNFDTDVLV SISQGVQDFA LDLLQRISVE VEKANKDFMI SPFSVWSLLV LLYEGSEGET
RNQLKKSLRI NVEDEKLRGA YKVWSSFLNI TTSTIEVATL QAIYTGKGYP IKNNYRDAIQ
NYNVQPMEVD FYSPDSVIQI NEDTNRTTRG LIPYTILPQD VYGAKMFLLS SLYFKGQWKF
PFNKTLTREE PFFSESGEVI GKIPMMVQEA NFAYVSNVEG LDGYVLELPY GTQDRLAMIV
VLPKRGFKLN DVANNLKALG LRPILQRLAA FRNRASEDNE VEVMMPKFVT ATDFTLKGVL
IQMGIRDLFD ENTANLDRMS SGLFAKLVVH STKIIVDEQG TTAGAVTEAA LANKATPPKF
LLNRPFQYMI VEKATGLLLF AGQVRNPKAA
