ID T1KCS2_TETUR Unreviewed; 440 AA.
AC T1KCS2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN Name=107362950 {ECO:0000313|EnsemblMetazoa:tetur09g00280.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur09g00280.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur09g00280.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; CAEY01001996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015785581.1; XM_015930095.1.
DR RefSeq; XP_015785582.1; XM_015930096.1.
DR AlphaFoldDB; T1KCS2; -.
DR STRING; 32264.T1KCS2; -.
DR EnsemblMetazoa; tetur09g00280.1; tetur09g00280.1; tetur09g00280.
DR GeneID; 107362950; -.
DR KEGG; tut:107362950; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_3_1; -.
DR OMA; PDSVCQE; -.
DR OrthoDB; 3026955at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.30.1640.30; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Secreted {ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 21..440
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5023965878"
FT DOMAIN 43..88
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 193..440
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 97..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48310 MW; 75B3C4F5B8368EBC CRC64;
MKVSCLIVIF NLFLIKLVTG SLVKRQIVFP SDEDIKSDDL QILCKTFQGG RGTCLPILKC
PSMQKERNLL ILRNSICGFD GVVPKLCCPS SIPNGIDNGN GDPLEPQPSK PEQETSVNPD
SSAELIGPND KNGANIHENI TPRPQPVKTT ALPKPTGRPK QGNDRGLKEL NLRVPPTLPS
KECGVNKQAE TRIVGGVPAK PGTWPWMAAL LFDEDGAKNS QCGATLVSEE IIITAAHCVY
EAGAVRDPSK VTVRLGEHNI EQDSQDDAVQ DFLVESIKIH QSFDPKTYKN DIAMLKLKNK
VSFNDRMAPV CLPFDSQLLR FGNLTGRSAT ITGWGRTSFN GPSSEVLLQA SFEIVPQEYC
REAFKKWVPI SQVYLCASNA GATRDSCQGD SGGPLVMFDN TMRKWYLMGV VSFGRRCATP
GFPGVYTRIP EFLDWIEKNL
//
