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Database: UniProt
Entry: U4TZ65_DENPD
LinkDB: U4TZ65_DENPD
Original site: U4TZ65_DENPD 
ID   U4TZ65_DENPD            Unreviewed;       365 AA.
AC   U4TZ65;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN   ORFNames=D910_03546 {ECO:0000313|EMBL:ERL86132.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL86132.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL86132.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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; KB631792; ERL86132.1; -; Genomic_DNA.
DR   RefSeq; XP_019764958.1; XM_019909399.1.
DR   AlphaFoldDB; U4TZ65; -.
DR   STRING; 77166.U4TZ65; -.
DR   GeneID; 109540884; -.
DR   KEGG; dpa:109540884; -.
DR   OrthoDB; 3026955at2759; -.
DR   Proteomes; UP000030742; 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; 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; 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:UP000030742};
KW   Secreted {ECO:0000256|RuleBase:RU366078};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|RuleBase:RU366078}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU366078"
FT   CHAIN           20..365
FT                   /note="CLIP domain-containing serine protease"
FT                   /evidence="ECO:0000256|RuleBase:RU366078"
FT                   /id="PRO_5023974129"
FT   DOMAIN          26..79
FT                   /note="Clip"
FT                   /evidence="ECO:0000259|PROSITE:PS51888"
FT   DOMAIN          118..365
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   365 AA;  40103 MW;  2F643AFAB59F3352 CRC64;
     MCNYYILFLF AAVIYRVNGQ VEDGTSCTTP TNQNGQCINI LNCKVVTNLL RTEANNVEVR
     SYVRSLYCGS KYNTPYVCCP ADNTRNILIK PDETSFGESD KFLSPPACGL SNATLPKVVG
     GIPAKLGEFP WMVSLGYRNL KNPSQTRWLC GGTLISHRHV LTAAHCVVTD LYLARVGELD
     LYDDNDGANP TDIEIEKTKV HENYDATKHI NDIAVLALSR STEGLVGVWP ICLPWEADKK
     NRSFLGNQPF VAGWGNLQFN GPSSTNLQLA TIPVVENSKC KKAYESAAII DESILCAGWD
     NGNKDACKGD SGGPLMYGTV QRDTKGIRFF QIGVVSYGFQ CAVAGYPGVY TRVTYFLNWI
     GNNLN
//
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