ID A0A0N1IPY4_PAPMA Unreviewed; 291 AA.
AC A0A0N1IPY4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU366078};
GN ORFNames=RR48_00949 {ECO:0000313|EMBL:KPJ18878.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ18878.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ18878.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ18878.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ18878.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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; KQ459985; KPJ18878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1IPY4; -.
DR STRING; 76193.A0A0N1IPY4; -.
DR InParanoid; A0A0N1IPY4; -.
DR Proteomes; UP000053240; 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 PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF131; CLIP DOMAIN-CONTAINING SERINE PROTEASE-RELATED; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU366078};
KW Protease {ECO:0000256|RuleBase:RU366078, ECO:0000313|EMBL:KPJ18878.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Secreted {ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU366078};
KW Signal {ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 20..291
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5031604187"
FT DOMAIN 113..291
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 291 AA; 32498 MW; 6552BF161DCCDDF8 CRC64;
MRSHPTVLFC VLFAALTNAL KQCDDCVKIT NCASAIQLIR TDRSAAAIQQ LQNALCGFEG
VQKVCCSDLF TSPSLNVENE SKNNTQIYGD EIENHRNIRL LPSECGDVDG NRIVGGTSAG
LYEFPWLALI SYRENERKLM FECGGTVINA RYVLTAAHCI YNKDIAGVRI GDYDISKPKD
CLGEDEIMEC ESRYQDIAVS HKIHHRGYVT QPYILNDIGL LRLARPVDFS YRNSGSICLP
ITKDLREKDL VGERGVVAGW GMADNQTKSN ILLKVELPIF SESSCNMLYK R
//
