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Database: UniProt
Entry: A0A182WMS8_9DIPT
LinkDB: A0A182WMS8_9DIPT
Original site: A0A182WMS8_9DIPT 
ID   A0A182WMS8_9DIPT        Unreviewed;       360 AA.
AC   A0A182WMS8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
OS   Anopheles minimus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN014039-PA, ECO:0000313|Proteomes:UP000075920};
RN   [1] {ECO:0000313|Proteomes:UP000075920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMIN014039-PA}
RP   IDENTIFICATION.
RC   STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN014039-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   AlphaFoldDB; A0A182WMS8; -.
DR   STRING; 112268.A0A182WMS8; -.
DR   EnsemblMetazoa; AMIN014039-RA; AMIN014039-PA; AMIN014039.
DR   VEuPathDB; VectorBase:AMIN014039; -.
DR   OrthoDB; 3680196at2759; -.
DR   Proteomes; UP000075920; Unassembled WGS sequence.
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};
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_5023971130"
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;  39592 MW;  DACE09E75477311E CRC64;
     MTGKRVMGVL IVGLLALAGQ MVTALELGQD CVNPYGEAGK CVLFRECQPL IEIYQKDVNT
     PDDTQFLTAS RCGVFERKTL VCCPGVKNSE KTSLPEPLNC GVQLSDRIVG GQPTKIDEFP
     WTALIEYQKP DGRFGFHCGG SIINERYIVT AAHCINSIPR NWKVHRVRLG EWDLGSSSDC
     EDDFCSVAPI DLDIEKIIVH TGYDTRDKSH HNDIALIRFN REIHYSATVR PICLPLADTI
     RNRAHAGLTS YAAGWGKTET ATASQKKLKV ELKVTDLKDC APVYQRNSII IDSTQMCAGG
     VRLKDTCSGD SGGPLMRQIA GAWYLIGVVS FGPQKCGTAG VPGVYTNVAE YVDWIRDNIY
//
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