ID Q2FAY7_MANSE Unreviewed; 455 AA.
AC Q2FAY7;
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=HP12 {ECO:0000313|EMBL:AAZ91694.1};
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:AAZ91694.1};
RN [1] {ECO:0000313|EMBL:AAZ91694.1}
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; DQ115323; AAZ91694.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2FAY7; -.
DR MEROPS; S01.305; -.
DR EnsemblMetazoa; XM_030177799.2; XP_030033659.2; LOC115449907.
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:SF527; CLIP DOMAIN-CONTAINING SERINE PROTEASE-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 3: Inferred from homology;
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..19
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 20..455
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5023963925"
FT DOMAIN 21..74
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 81..132
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 176..454
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 455 AA; 49680 MW; BA114979C4D02354 CRC64;
MHFVLALCVF AISAGFASGQ SCTLPNNDKG TCKILTECDA ATKIFTKKNR TSEDENFLRK
TYCGHAGQTP MVCCPESEKF SCTTPDNKTG ECVNIQKCTY LAEIQDDPLN EGETVFLKNS
VCAGPEENSV CCGSEGSSVD VDSLGKNVPV TCEQSAFPPD PDSDCCGLDS SVSDKIIGGT
ATGINQYPWL VIIEYAKLET SRLLCGGFLI SNKYVLTAGH CVKGPILEAG TPKYVHLGEY
NTTNEGPDCV SSGAGQPDCN EGIIRATIDE IIPHPDYLKP NNFYEQHDIA LIRLKVWAPR
TEFIRPICLP KIDHTLSLPP NYKFQVAGWG RYYQDFVNKI FKASEVKLHV DVPYVNHGDC
QRKLRTIPNL YKLSNGIKVS VNVTLWNGQL CAGGVAGKDS CKGDSGGPLM YENERKYTAV
GMVSYGLGEC GIGGYPGVYT NIYPYLPWIK ATIRE
//
