STUB_DROME
ID STUB_DROME Reviewed; 787 AA.
AC Q05319; Q8MRH5; Q9VEY6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine proteinase stubble;
DE EC=3.4.21.-;
DE AltName: Full=Protein stubble-stubbloid;
DE Contains:
DE RecName: Full=Serine proteinase stubble non-catalytic chain;
DE Contains:
DE RecName: Full=Serine proteinase stubble catalytic chain;
GN Name=Sb; Synonyms=Sb-sbd; ORFNames=CG4316;
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, AND INDUCTION.
RC STRAIN=Oregon-R;
RX PubMed=7685111; DOI=10.1073/pnas.90.11.4937;
RA Appel L.F., Prout M., Abu-Shumays R., Hammonds A., Garbe J.C., Fristrom D.,
RA Fristrom J.;
RT "The Drosophila Stubble-stubbloid gene encodes an apparent transmembrane
RT serine protease required for epithelial morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4937-4941(1993).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-787.
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
CC -!- FUNCTION: Hormone dependent protease required for epithelial
CC morphogenesis, including the formation of bristles, legs, and wings.
CC Has a dual function, detaches imaginal disk cells from extracellular
CC matrices through its extracellular proteolytic domain and transmits an
CC outside-to-inside signal to its intracellular domain to modify the
CC cytoskeleton during morphogenesis. {ECO:0000269|PubMed:7685111}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- INDUCTION: By 20-hydroxyecdysone (20HE). {ECO:0000269|PubMed:7685111}.
CC -!- PTM: May activate itself by proteolytic cleavage.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-24 is the initiator.
CC {ECO:0000305}.
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DR EMBL; L11451; AAA28918.1; -; mRNA.
DR EMBL; AE014297; AAF55277.1; -; Genomic_DNA.
DR EMBL; AY119618; AAM50272.1; -; mRNA.
DR PIR; A47547; A47547.
DR RefSeq; NP_001287355.1; NM_001300426.1.
DR RefSeq; NP_476709.1; NM_057361.4.
DR AlphaFoldDB; Q05319; -.
DR SMR; Q05319; -.
DR BioGRID; 67009; 6.
DR STRING; 7227.FBpp0082704; -.
DR MEROPS; S01.225; -.
DR GlyGen; Q05319; 2 sites.
DR PaxDb; Q05319; -.
DR EnsemblMetazoa; FBtr0083250; FBpp0082704; FBgn0003319.
DR EnsemblMetazoa; FBtr0344008; FBpp0310459; FBgn0003319.
DR GeneID; 41958; -.
DR KEGG; dme:Dmel_CG4316; -.
DR UCSC; CG4316-RA; d. melanogaster.
DR CTD; 20233; -.
DR FlyBase; FBgn0003319; Sb.
DR VEuPathDB; VectorBase:FBgn0003319; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000176272; -.
DR HOGENOM; CLU_006842_17_0_1; -.
DR InParanoid; Q05319; -.
DR OMA; IVNLPMP; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q05319; -.
DR BioGRID-ORCS; 41958; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41958; -.
DR PRO; PR:Q05319; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003319; Expressed in wing disc and 8 other tissues.
DR ExpressionAtlas; Q05319; baseline and differential.
DR Genevisible; Q05319; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..543
FT /note="Serine proteinase stubble non-catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028141"
FT CHAIN 544..787
FT /note="Serine proteinase stubble catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028142"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..80
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 81..787
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 544..787
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 590
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 640
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 738
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 532..660
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 575..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 704..723
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 734..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 287
FT /note="Missing (in Ref. 1; AAA28918)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="T -> S (in Ref. 1; AAA28918)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="P -> S (in Ref. 1; AAA28918)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="H -> R (in Ref. 1; AAA28918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 85144 MW; 02B2B8758BD6025A CRC64;
MKQPTLIRPR LRHRRSTPAA ATKMCPKRHW LVNNRAAGSR GSGGAAARSR RSLDQIVEVL
VALIVVNCLA TAAAALITPP DSLESLGSLG IPSSSASSSE DDDDMSSGFY RIPHRLEGYP
QLQQLQRGQN FKISPKPCSF GRVEGTCMFV WECIKSEGKH VGMCVDSFMF GSCCTHNYTD
NIVLPQTAFS YTRPTKPLTL RPRPPAAPYK PMISGMTTIE RPHGAGTLVI RPSGPHHQGT
LARPHPPPYQ SKPTTASDLH GSASHPSSSS SSSSSSNPNS IWHTSTQQQQ QQQHQQNQQN
HWQMTTEPSF ITKPRPTGWT KPGIVNLPMP ARPSKPSKPT KKPIVYDRTP PPPPSVPPST
STSTTSTSLI WPAQTHPPQP HRPTRPQLSP GTSLAASSSS HWPSSTTSTT SSTTSTTTTT
TTTRRTTTPT TTTRRTTTNK PTRPYQRPTT ATSSSSTSTT SSKTPTTTRP ISSSSSSSSG
IVTSSQRPTQ PTHRTPVLAT SGIETNEISD SSIPDAGALG HVKTISAARS ECGVPTLARP
ETRIVGGKSA AFGRWPWQVS VRRTSFFGFS STHRCGGALI NENWIATAGH CVDDLLISQI
RIRVGEYDFS HVQEQLPYIE RGVAKKVVHP KYSFLTYEYD LALVKLEQPL EFAPHVSPIC
LPETDSLLIG MNATVTGWGR LSEGGTLPSV LQEVSVPIVS NDNCKSMFMR AGRQEFIPDI
FLCAGYETGG QDSCQGDSGG PLQAKSQDGR FFLAGIISWG IGCAEANLPG VCTRISKFTP
WILEHVR
