ID C0L2M8_ANOQN Unreviewed; 360 AA.
AC C0L2M8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 22-FEB-2023, entry version 46.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN Name=SP14D1 {ECO:0000313|EMBL:ACN38225.1};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EMBL:ACN38225.1};
RN [1] {ECO:0000313|EMBL:ACN38225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AQ116 {ECO:0000313|EMBL:ACN38225.1};
RX PubMed=19234606; DOI=10.1371/journal.pone.0004549;
RA Lehmann T., Hume J.C., Licht M., Burns C.S., Wollenberg K., Simard F.,
RA Ribeiro J.M.;
RT "Molecular evolution of immune genes in the malaria mosquito Anopheles
RT gambiae.";
RL PLoS ONE 4:E4549-E4549(2009).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC 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; FJ653872; ACN38225.1; -; Genomic_DNA.
DR AlphaFoldDB; C0L2M8; -.
DR MEROPS; S01.201; -.
DR VEuPathDB; VectorBase:AQUA015865; -.
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; PTHR24256:SF527; SERINE PROTEASE EASTER; 1.
DR PANTHER; PTHR24256; TRYPTASE-RELATED; 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, ECO:0000313|EMBL:ACN38225.1};
KW Secreted {ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 25..360
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5023968372"
FT DOMAIN 30..83
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 108..360
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 360 AA; 39441 MW; C3B8C9A3C26A4C48 CRC64;
MIGNRVFNLL IAATLALAGQ TVLALELGQD CVNPVGEAGK CVLFRECQPL VDIYNKPVNT
PDDTQFLTES RCGLFERKTL VCCAGVRSKG KTSLPESPNC GVQLTDRVIG GQPTKIDEFP
WTALIEYEKP NGRFGFHCGG SVINERYILT AAHCITSIPR GWKVHRVRLG EWDLSSTTDQ
EDDFYADAPI DLDIEKIIVH PGYNLQDKSH HNDIALIRFN REINYSSTIR AICLPLSNSL
RNRKHAGLSS YAAGWGKTET ASASQKKLKV ELTVVDVKDC SPAYQRNGIS LDSTQMCAGG
VRGKDTCSGD SGGPLMRQMT GSWYLIGVVS FGPQKCGAPG VPGVYTNVAE YVDWIKDNIY
//