SCARF_DROME
ID SCARF_DROME Reviewed; 655 AA.
AC Q7K5M0;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Inactive serine protease scarface {ECO:0000303|PubMed:15342518, ECO:0000303|PubMed:20379222};
DE Flags: Precursor;
GN Name=scaf {ECO:0000303|PubMed:20530545, ECO:0000312|FlyBase:FBgn0033033};
GN Synonyms=scarf {ECO:0000303|PubMed:20379222};
GN ORFNames=CG11066 {ECO:0000312|FlyBase:FBgn0033033};
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:AAK77280.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK77280.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAK77280.1};
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 SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15342518; DOI=10.1534/genetics.104.027557;
RA Bonin C.P., Mann R.S.;
RT "A piggyBac transposon gene trap for the analysis of gene expression and
RT function in Drosophila.";
RL Genetics 167:1801-1811(2004).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20379222; DOI=10.1038/embor.2010.43;
RA Sorrosal G., Perez L., Herranz H., Milan M.;
RT "Scarface, a secreted serine protease-like protein, regulates polarized
RT localization of laminin A at the basement membrane of the Drosophila
RT embryo.";
RL EMBO Rep. 11:373-379(2010).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20530545; DOI=10.1242/dev.050781;
RA Rousset R., Bono-Lauriol S., Gettings M., Suzanne M., Speder P.,
RA Noselli S.;
RT "The Drosophila serine protease homologue Scarface regulates JNK signalling
RT in a negative-feedback loop during epithelial morphogenesis.";
RL Development 137:2177-2186(2010).
RN [7] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25737837; DOI=10.1016/j.fob.2015.01.008;
RA Srivastava A., Dong Q.;
RT "Regulation of a serine protease homolog by the JNK pathway during thoracic
RT development of Drosophila melanogaster.";
RL FEBS Open Bio 5:117-123(2015).
RN [8] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=28628612; DOI=10.1371/journal.pgen.1006860;
RA Kushnir T., Mezuman S., Bar-Cohen S., Lange R., Paroush Z., Helman A.;
RT "Novel interplay between JNK and Egfr signaling in Drosophila dorsal
RT closure.";
RL PLoS Genet. 13:E1006860-E1006860(2017).
CC -!- FUNCTION: Inactive serine protease that plays a role in germ-band
CC retraction and dorsal closure morphogenesis in embryogenesis;
CC contributes to amnioserosa attachment and epithelial apico-basal
CC polarity by regulating the localization of laminin LanA on the apical
CC side of the amnioserosa epithelium (PubMed:28628612, PubMed:20379222).
CC Contributes to epithelial morphogenesis probably by regulating the
CC bsk/JNK pathway, as part of a negative-feedback loop, and by modulating
CC the cross-talk between the Egfr, bsk/JNK and dpp signal transduction
CC pathways (PubMed:28628612, PubMed:20379222). In larval development,
CC antagonizes the morphogenetic movements controlled by the bsk/JNK
CC signaling including male genitalia formation and thorax development
CC (PubMed:20379222, PubMed:20530545, PubMed:25737837).
CC {ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545,
CC ECO:0000269|PubMed:25737837, ECO:0000269|PubMed:28628612}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15342518,
CC ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545}.
CC -!- DEVELOPMENTAL STAGE: In embryos, expressed in leading edge (LE) cells
CC (at protein level) (PubMed:20530545). In larvae, expressed in the wing
CC imaginal disk cells in the future hinge region, specifically in the
CC peripodial stalk and in the peripodial membrane cells (at protein
CC level) (PubMed:15342518, PubMed:25737837). In larvae, expressed in the
CC A8 abdomen-derived cells in the male genital disk (at protein level)
CC (PubMed:20530545). In third instar larvae, expressed in the anterior
CC and posterios termini (at protein level) (PubMed:15342518). In adult
CC fly, expressed in the wing hinge, in the socket cells of the micro- and
CC macrochaete and proboscis (at protein level) (PubMed:15342518). In
CC embryos, expressed in leading edge (LE) cells during germ-band
CC retraction and dorsal closure from stage 13; expressed in some cells of
CC the amnioserosa in particular in the posterior canthus as well as in
CC the ventral ectoderm; expressed both in head and tail region
CC (PubMed:20379222, PubMed:20530545, PubMed:28628612).
CC {ECO:0000269|PubMed:15342518, ECO:0000269|PubMed:20379222,
CC ECO:0000269|PubMed:20530545, ECO:0000269|PubMed:25737837,
CC ECO:0000269|PubMed:28628612}.
CC -!- DOMAIN: The CLIP domain consists of 37-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal due to defects in the dorsal
CC closure and germ-band retraction; these defects include
CC undifferentiated or defective larval cuticles presenting dorsal holes
CC and wrinkles, defective attachment of the amnioserosa to the tail end
CC of the germ band, defective elongation of the lateral ectoderm with
CC compromised interface between the LE cells and the amnioserosa
CC (PubMed:20379222, PubMed:20530545, PubMed:15342518). RNAi-mediated
CC knockdown results in pupal lethality and scarring (PubMed:25737837).
CC RNAi-mediated knockdown in the epidermis results in loss of wing veins
CC and thorax mechanosensory bristles as well as male terminalia
CC malformations including genitalia rotation defects and partial
CC dissociation of the genital plate from the abdomen (PubMed:20530545).
CC RNAi-mediated knockdown in the dorsal compartment of the wing disk
CC results in loss of bristles from the medio-lateral region of the thorax
CC and in the appearance of a mild thoracic cleft (PubMed:25737837). RNAi-
CC mediated knockdown in the notum area of the wing disk, destined to form
CC the dorsal medio-lateral region of the adult thorax as well as thoracic
CC bristles, results in a thoracic cleft and loss of bristles from the
CC medio-lateral region of the thorax (PubMed:25737837).
CC {ECO:0000269|PubMed:15342518, ECO:0000269|PubMed:20379222,
CC ECO:0000269|PubMed:20530545, ECO:0000269|PubMed:25737837}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Lacks the conserved residues within the catalytic triad,
CC probably resulting in a loss of proteolytic activity.
CC {ECO:0000303|PubMed:20379222}.
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DR EMBL; AE013599; AAF57320.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68354.1; -; Genomic_DNA.
DR EMBL; AY047548; AAK77280.1; -; mRNA.
DR RefSeq; NP_610180.1; NM_136336.3.
DR RefSeq; NP_724424.1; NM_165441.2.
DR AlphaFoldDB; Q7K5M0; -.
DR SMR; Q7K5M0; -.
DR STRING; 7227.FBpp0085396; -.
DR PaxDb; Q7K5M0; -.
DR PRIDE; Q7K5M0; -.
DR DNASU; 35505; -.
DR EnsemblMetazoa; FBtr0086060; FBpp0085396; FBgn0033033.
DR EnsemblMetazoa; FBtr0086061; FBpp0085397; FBgn0033033.
DR GeneID; 35505; -.
DR KEGG; dme:Dmel_CG11066; -.
DR UCSC; CG11066-RA; d. melanogaster.
DR CTD; 35505; -.
DR FlyBase; FBgn0033033; scaf.
DR VEuPathDB; VectorBase:FBgn0033033; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000170789; -.
DR HOGENOM; CLU_387467_0_0_1; -.
DR InParanoid; Q7K5M0; -.
DR OMA; IPHREPR; -.
DR OrthoDB; 871933at2759; -.
DR PhylomeDB; Q7K5M0; -.
DR BioGRID-ORCS; 35505; 0 hits in 1 CRISPR screen.
DR ChiTaRS; scaf; fly.
DR GenomeRNAi; 35505; -.
DR PRO; PR:Q7K5M0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033033; Expressed in mouthpart and 22 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0007394; P:dorsal closure, elongation of leading edge cells; IMP:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0007390; P:germ-band shortening; IMP:UniProtKB.
DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP:UniProtKB.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0048802; P:notum morphogenesis; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0050793; P:regulation of developmental process; IMP:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR040973; CLIP_SPH_Scar.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF18399; CLIP_SPH_Scar; 1.
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.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Reference proteome; Secreted;
KW Serine protease homolog; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..655
FT /note="Inactive serine protease scarface"
FT /evidence="ECO:0000255"
FT /id="PRO_5010683600"
FT DOMAIN 421..644
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 213..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..407
FT /note="CLIP"
FT /evidence="ECO:0000255"
FT COMPBIAS 215..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 344..394
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 350..383
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 356..395
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 450..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 547..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 579..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 595..623
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 655 AA; 71417 MW; 4726435D771ABF14 CRC64;
MSASHFREQL ALCITLAVLA AASGDYRANM FLNGQYQNGI KDQKENNLLV NPSTNVFLNH
AIISRQASPF QGPTYLPPKE FLKCAPGQQC VRSGQCLNGY FAQQLPKIQN CDPETTVCCT
YRPPPTTTTT TTTSVPVANC AYDSDCVTPD NCRNGEISAI NYVKKQGPNR CPAPNICCRI
PSTTLTEDGY IFNLPEKTFP LPTKPAVLAM PSTQAPFRPQ PTTAVPASRP TIEYLPPSTT
QHPSYEKVQT SRRPVYLPPS PATESASSLI PKIRPRPEPR PQPTRRPTNE YLPPAAANEI
PRFEPDRAPQ PSNQKPIYRG EDQLSPQIFP TPQPANVPKH FAKCASALVC TSENFCNAIG
VLSETPVELS PMEAAFRVPL TDCLQTENGS PGKCCRDPNY VDPWPVNLAG VCATRNKRTK
PTGVKDLDAN FAEIPWQAMI LRESSKTLIC GGAIIGDQFV LSSASCVNGL PVTDIRVKAG
EWELGSTNEP LPFQLTGVKT VDVHPDYDPS TNSHDLAIIR LERRLEFASH IQPICISDED
PKDSEQCFTS GWGKQALSIH EEGALMHVTD TLPQARSECS ADSSSVCSAT KFDSCQFDVG
SALACGSGSS VRLKGIFAGE NSCGEGQTVR FAKPDIKWIN TAFAENNKPL LLKRF
