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Database: UniProt
Entry: C0L2M8_ANOQN
LinkDB: C0L2M8_ANOQN
Original site: C0L2M8_ANOQN 
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
//
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