ID C0L2Q0_ANOGA Unreviewed; 360 AA.
AC C0L2Q0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:ACN38247.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:ACN38247.1};
RN [1] {ECO:0000313|EMBL:ACN38247.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GA5023 {ECO:0000313|EMBL:ACN38257.1}, GA5028
RC {ECO:0000313|EMBL:ACN38258.1}, GS16025 {ECO:0000313|EMBL:ACN38247.1},
RC and GS16035 {ECO:0000313|EMBL:ACN38249.1};
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; FJ653894; ACN38247.1; -; Genomic_DNA.
DR EMBL; FJ653896; ACN38249.1; -; Genomic_DNA.
DR EMBL; FJ653904; ACN38257.1; -; Genomic_DNA.
DR EMBL; FJ653905; ACN38258.1; -; Genomic_DNA.
DR AlphaFoldDB; C0L2Q0; -.
DR MEROPS; S01.201; -.
DR VEuPathDB; VectorBase:AGAP003250; -.
DR HOGENOM; CLU_006842_0_3_1; -.
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; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:ACN38247.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, 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_5010109385"
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; 39465 MW; 9EDD3A4C25033F09 CRC64;
MIGNRVINLL IVATLALAGQ TVLALELGQD CVNPVGEAGK CVLFRECQPL VDIYNKPVNT
PDDTQFLTES RCGLYERKTL VCCAGVRSKG KTSLPESPNC GVQLTDRVIG GQPTKIDEFP
WTALIEYEKP NGRFGFHCGG SVINERYILT AAHCITSIPR GWKVHRVRLG EWDLSSTTDQ
EDDFYADAPI DLDIEKIIVH PGYNLQDKSH HNDIALIRFN REINYSSTIR AICLPLSNSL
RNRKHAGLSS YAAGWGKTET ASASQKKLKV ELTVVDVKDC SPAYQRNGIS LDSTQMCAGG
IRGKDTCSGD SGGPLMRQMT GSWYLIGVVS FGPQKCGAPG VPGVYTNVAE YVDWIKDNIY
//