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Serine protease grass (EC 3.4.21.-) (Gram-positive specific serine protease)

 GRASS_DROME             Reviewed;         377 AA.
Q9VB68; Q86PB3; Q8MR95; Q9VB67;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 148.
RecName: Full=Serine protease grass {ECO:0000305};
EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
AltName: Full=Gram-positive specific serine protease {ECO:0000303|PubMed:16631589};
Flags: Precursor;
Name=grass {ECO:0000303|PubMed:16631589,
ECO:0000312|FlyBase:FBgn0039494};
Synonyms=c-SP1 {ECO:0000312|FlyBase:FBgn0039494};
ORFNames=CG5896 {ECO:0000312|FlyBase:FBgn0039494};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000312|EMBL:AAM52037.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley {ECO:0000312|EMBL:AAM52037.1};
TISSUE=Head {ECO:0000312|EMBL:AAM52037.1};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000312|EMBL:AAO24994.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAO24994.1};
TISSUE=Larva {ECO:0000312|EMBL:AAO24994.1}, and
Pupae {ECO:0000312|EMBL:AAO24994.1};
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000244|PDB:2XXL}
PROTEIN SEQUENCE OF 27-30, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN
COMPLEX WITH CALCIUM, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN,
PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-230 AND ASN-270, AND
DISULFIDE BONDS.
PubMed=21310954; DOI=10.1074/jbc.M110.182741;
Kellenberger C., Leone P., Coquet L., Jouenne T., Reichhart J.M.,
Roussel A.;
"Structure-function analysis of grass clip serine protease involved in
Drosophila Toll pathway activation.";
J. Biol. Chem. 286:12300-12307(2011).
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16631589; DOI=10.1016/j.cub.2006.03.020;
Kambris Z., Brun S., Jang I.H., Nam H.J., Romeo Y., Takahashi K.,
Lee W.J., Ueda R., Lemaitre B.;
"Drosophila immunity: a large-scale in vivo RNAi screen identifies
five serine proteases required for Toll activation.";
Curr. Biol. 16:808-813(2006).
[7] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18724373; DOI=10.1038/ni.1643;
El Chamy L., Leclerc V., Caldelari I., Reichhart J.M.;
"Sensing of 'danger signals' and pathogen-associated molecular
patterns defines binary signaling pathways 'upstream' of Toll.";
Nat. Immunol. 9:1165-1170(2008).
-!- FUNCTION: Endopeptidase (By similarity). Plays a key role in
innate immunity by activating the Toll pathway in response to
fungal and Gram-positive bacterial infections, presumably
downstream of pattern-recognition receptors (PRR), such as PGRP-
SA, GNBP1 and GNBP3, and upstream of spz processing enzyme SPE
(PubMed:16631589, PubMed:18724373). {ECO:0000250|UniProtKB:Q9XXV0,
ECO:0000269|PubMed:16631589, ECO:0000269|PubMed:18724373}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21310954}.
Note=Probably secreted in the hemolymph. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B {ECO:0000312|FlyBase:FBgn0039494};
IsoId=Q9VB68-1; Sequence=Displayed;
Name=A {ECO:0000312|FlyBase:FBgn0039494};
IsoId=Q9VB68-2; Sequence=VSP_059329;
-!- DOMAIN: The CLIP domain consists of 37-55 residues which are
"knitted" together usually by 3 conserved disulfide bonds forming
a clip-like compact structure. {ECO:0000305}.
-!- PTM: Proteolytically cleaved by a tryspin-like protease which is
likely to activate grass. {ECO:0000269|PubMed:21310954}.
-!- DISRUPTION PHENOTYPE: Results in increased susceptibility to
fungal or Gram-positive bacterial infection and failure to induce
the expression of the Toll pathway-activated antifungal peptide
Drs (PubMed:18724373). siRNA-mediated knockdown results in
increased susceptibility to Gram-positive bacterial infection and
severe reduction in the expression of the antifungal peptide Drs
(PubMed:16631589). In a protease psh mutant background, complete
loss of Drs induction and increased susceptibility to Gram-
positive bacterial infection (PubMed:18724373).
{ECO:0000269|PubMed:16631589, ECO:0000269|PubMed:18724373}.
-!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM52037.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AE014297; AAF56675.1; -; Genomic_DNA.
EMBL; AE014297; AAF56676.1; -; Genomic_DNA.
EMBL; AY121710; AAM52037.1; ALT_INIT; mRNA.
EMBL; BT003238; AAO24994.1; -; mRNA.
RefSeq; NP_651543.1; NM_143286.3. [Q9VB68-1]
RefSeq; NP_733197.1; NM_170318.3. [Q9VB68-2]
UniGene; Dm.13751; -.
PDB; 2XXL; X-ray; 1.80 A; A/B=1-377.
PDBsum; 2XXL; -.
ProteinModelPortal; Q9VB68; -.
SMR; Q9VB68; -.
STRING; 7227.FBpp0084482; -.
MEROPS; S01.502; -.
PaxDb; Q9VB68; -.
PRIDE; Q9VB68; -.
EnsemblMetazoa; FBtr0085111; FBpp0084481; FBgn0039494. [Q9VB68-2]
EnsemblMetazoa; FBtr0085112; FBpp0084482; FBgn0039494. [Q9VB68-1]
GeneID; 43273; -.
KEGG; dme:Dmel_CG5896; -.
UCSC; CG5896-RA; d. melanogaster.
UCSC; CG5896-RB; d. melanogaster. [Q9VB68-1]
CTD; 43273; -.
FlyBase; FBgn0039494; grass.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00540000072294; -.
InParanoid; Q9VB68; -.
KO; K20673; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q9VB68; -.
GenomeRNAi; 43273; -.
PRO; PR:Q9VB68; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0039494; -.
ExpressionAtlas; Q9VB68; baseline and differential.
Genevisible; Q9VB68; DM.
GO; GO:0005576; C:extracellular region; HDA:FlyBase.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
GO; GO:0006952; P:defense response; IMP:FlyBase.
GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:UniProtKB.
GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; ISM:FlyBase.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.20.20.90; -; 1.
InterPro; IPR022700; CLIP.
InterPro; IPR038565; CLIP_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF12032; CLIP; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00680; CLIP; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Immunity; Innate immunity; Metal-binding; Protease;
Reference proteome; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 26 {ECO:0000269|PubMed:21310954}.
CHAIN 27 377 Serine protease grass.
{ECO:0000305|PubMed:21310954}.
/FTId=PRO_5004335652.
DOMAIN 32 89 CLIP. {ECO:0000255}.
DOMAIN 119 373 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 91 118 Linker. {ECO:0000269|PubMed:21310954}.
ACT_SITE 163 163 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 223 223 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 318 318 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
METAL 179 179 Calcium. {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
METAL 181 181 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
METAL 184 184 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
METAL 187 187 Calcium. {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 32 88 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 42 78 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 48 89 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 111 243 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 148 164 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 188 197 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 290 304 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
DISULFID 314 349 {ECO:0000244|PDB:2XXL,
ECO:0000269|PubMed:21310954}.
VAR_SEQ 1 42 Missing (in isoform A). {ECO:0000305}.
/FTId=VSP_059329.
STRAND 31 33 {ECO:0000244|PDB:2XXL}.
STRAND 39 44 {ECO:0000244|PDB:2XXL}.
HELIX 45 47 {ECO:0000244|PDB:2XXL}.
HELIX 49 60 {ECO:0000244|PDB:2XXL}.
HELIX 67 76 {ECO:0000244|PDB:2XXL}.
STRAND 77 81 {ECO:0000244|PDB:2XXL}.
STRAND 84 90 {ECO:0000244|PDB:2XXL}.
HELIX 91 93 {ECO:0000244|PDB:2XXL}.
HELIX 98 104 {ECO:0000244|PDB:2XXL}.
STRAND 133 139 {ECO:0000244|PDB:2XXL}.
STRAND 141 154 {ECO:0000244|PDB:2XXL}.
STRAND 157 160 {ECO:0000244|PDB:2XXL}.
HELIX 162 164 {ECO:0000244|PDB:2XXL}.
TURN 165 167 {ECO:0000244|PDB:2XXL}.
TURN 169 171 {ECO:0000244|PDB:2XXL}.
STRAND 172 178 {ECO:0000244|PDB:2XXL}.
STRAND 188 191 {ECO:0000244|PDB:2XXL}.
STRAND 194 197 {ECO:0000244|PDB:2XXL}.
STRAND 202 211 {ECO:0000244|PDB:2XXL}.
TURN 217 220 {ECO:0000244|PDB:2XXL}.
STRAND 225 231 {ECO:0000244|PDB:2XXL}.
HELIX 248 253 {ECO:0000244|PDB:2XXL}.
TURN 254 256 {ECO:0000244|PDB:2XXL}.
STRAND 258 264 {ECO:0000244|PDB:2XXL}.
STRAND 278 285 {ECO:0000244|PDB:2XXL}.
HELIX 287 294 {ECO:0000244|PDB:2XXL}.
STRAND 302 305 {ECO:0000244|PDB:2XXL}.
STRAND 310 312 {ECO:0000244|PDB:2XXL}.
HELIX 313 315 {ECO:0000244|PDB:2XXL}.
STRAND 321 326 {ECO:0000244|PDB:2XXL}.
STRAND 335 344 {ECO:0000244|PDB:2XXL}.
STRAND 356 360 {ECO:0000244|PDB:2XXL}.
HELIX 361 364 {ECO:0000244|PDB:2XXL}.
HELIX 365 375 {ECO:0000244|PDB:2XXL}.
SEQUENCE 377 AA; 41511 MW; 5B953F3D505CBDC4 CRC64;
MMIASSLAVL YGIAIVSSMG VQSARADYAD DCTTPDGDQG QCMPFSSCRT IEERLTEAQK
AGQKVPADYA SYLQKALCGE FNGVRHFCCP SANIQHNSKV MSLFKDENFD CGNFLSQRVS
NGYEVKLSSR PWMALLRYQQ FGESRFLCGG AMISERYILT AAHCVHGLQN DLYEIRLGEH
RISTEEDCRQ QGRKKKCAPP VVNVGIEKHL IHEKYDARHI MHDIALLKLN RSVPFQKHIK
PICLPITDEL KEKAEQISTY FVTGWGTTEN GSSSDVLLQA NVPLQPRSAC SQAYRRAVPL
SQLCVGGGDL QDSCKGDSGG PLQAPAQYLG EYAPKMVEFG IVSQGVVTCG QISLPGLYTN
VGEYVQWITD TMASNGL


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