ID Q8SXG6_DROME Unreviewed; 546 AA.
AC Q8SXG6;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN ORFNames=CG1299 {ECO:0000313|EMBL:AAL90385.1,
GN ECO:0000313|FlyBase:FBgn0035501};
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:0000313|EMBL:AAL90385.1};
RN [1] {ECO:0000313|EMBL:AAL90385.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Berkeley {ECO:0000313|EMBL:AAL90385.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036320};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366078}.
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000256|RuleBase:RU366078}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195, ECO:0000256|RuleBase:RU366078}.
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DR EMBL; AY089647; AAL90385.1; -; mRNA.
DR AlphaFoldDB; Q8SXG6; -.
DR MEROPS; S01.B33; -.
DR AGR; FB:FBgn0035501; -.
DR FlyBase; FBgn0035501; CG1299.
DR VEuPathDB; VectorBase:FBgn0035501; -.
DR OrthoDB; 3026955at2759; -.
DR PhylomeDB; Q8SXG6; -.
DR ExpressionAtlas; Q8SXG6; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.30.1640.30; -; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR038565; CLIP_sf.
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; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF12032; CLIP; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51888; CLIP; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Secreted {ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|RuleBase:RU366078};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 26..546
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5023968310"
FT DOMAIN 163..216
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 261..508
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 60186 MW; 9C73F8A5151FE967 CRC64;
MKSMCCVSAV ITLLPLVLLP PPTVAQFNQR RQVRQNCITP ENYYGSCVAL TYCPQVVNIF
QTTSRDRAQR YVIALQRSCG TRSINGDPVI CCTEPRYNPV TERPRNPFFP SGSTFIGPQP
PPEVPDNPFL IPTPRTTTTT TTTTPAPIPD TSAAPLIEPR GTVCRGPDTK PGNCVEIKEC
ASLLNELRSR SQDATFANFL RASNAVCQNK GTQVCCPTGQ GITNTTPAPS QIVPKNTDEI
PRRLLNVEEG CGSTVGYFKK IVGGEVSRKG AWPWIALLGY DDPSGSPFKC GGTLITARHV
LTAAHCIRQD LQFVRLGEHD LSTDTETGHV DINIARYVSH PDYNRRNGRS DMAILYLERN
VEFTSKIAPI CLPHTANLRQ KSYVGYMPFV AGWGKTMEGG ESAQVLNELQ IPIYDNKVCV
QSYAKEKRYF SADQFDKAVL CAGVLSGGKD TCQGDSGGPL MLPEPYQGQL RFYLIGVVSY
GIGCARPNVP GVYSSTQYFM DWIIQQVQDT PRFAIAIVLH LAHKIPNLKQ THNQQKTCAM
RTKRLI
//
