ID Q2FAY4_MANSE Unreviewed; 443 AA.
AC Q2FAY4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN Name=HP23 {ECO:0000313|EMBL:AAZ91697.1};
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130 {ECO:0000313|EMBL:AAZ91697.1};
RN [1] {ECO:0000313|EMBL:AAZ91697.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16324822; DOI=10.1016/j.ygeno.2005.10.003;
RA Wang Y., Zou Z., Jiang H.;
RT "An expansion of the dual clip-domain serine proteinase family in Manduca
RT sexta: gene organization, expression, and evolution of prophenoloxidase-
RT activating proteinase-2, hemolymph proteinase 12, and other related
RT proteinases.";
RL Genomics 87:399-409(2006).
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; DQ115324; AAZ91697.1; -; mRNA.
DR AlphaFoldDB; Q2FAY4; -.
DR MEROPS; S01.305; -.
DR EnsemblMetazoa; XM_037444219.1; XP_037300116.1; LOC115454329.
DR OrthoDB; 3680196at2759; -.
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; -; 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; PTHR24256:SF537; RE37738P-RELATED; 1.
DR PANTHER; PTHR24256; TRYPTASE-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; 2.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Secreted {ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 18..443
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5023967045"
FT DOMAIN 19..72
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 79..130
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 173..442
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 443 AA; 49194 MW; 1C7856ED095EE7AA CRC64;
MHFALVLCVF GIAFTSGEPC TSPTDDKGTC KSIYECDLLR GIVVKAKRTS LDEQFLRKSK
CGYDGNMPKV CCPDTDKLSC TTPDGKKGQC VNIITCSNLS DLLKEMNDTV KLNYLKSSKC
AGPQDYSVCC GPRPNLGMTL QKSCAERVSA LPPHEEEDGC CGVDNFEENK LLATGGNQTF
IDQYPWLVVI EYEHPIEKNK LMCGGALISG KYVLTAAHCV TGAILKEGTP KYVRLGEYNT
TNKGPDCFRL SDHELDCTED MILAPIEEII VHPKYDRFDP HKRHDIALIR LKIYAPYTDF
IRPICLPKVD YALSPPLNFT FFVAGWGLYF ENKTKQFRKS EVKLHVEVPY VVRDQCQTAV
RSLKGAENIV FRSGQICAGG VSGKDACRGD SGGPLMYLSR EGWKFEVVGL VGAGASICGQ
AGIPGVYTYV YEYLPWIRQN MRH
//
