ID A8WZH3_CAEBR Unreviewed; 446 AA.
AC A8WZH3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 3.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Protein CBR-ASP-4 {ECO:0000313|EMBL:CAP25783.3};
GN Name=asp-4 {ECO:0000313|WormBase:CBG05258};
GN Synonyms=Cbr-asp-4 {ECO:0000313|EMBL:CAP25783.3};
GN ORFNames=CBG05258 {ECO:0000313|WormBase:CBG05258}, CBG_05258
GN {ECO:0000313|EMBL:CAP25783.3};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP25783.3, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP25783.3, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP25783.3,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; HE601042; CAP25783.3; -; Genomic_DNA.
DR RefSeq; XP_002645565.1; XM_002645519.1.
DR AlphaFoldDB; A8WZH3; -.
DR STRING; 6238.A8WZH3; -.
DR MEROPS; A01.068; -.
DR EnsemblMetazoa; CBG05258.1; CBG05258.1; WBGene00027753.
DR GeneID; 8587564; -.
DR KEGG; cbr:CBG_05258; -.
DR CTD; 8587564; -.
DR WormBase; CBG05258; CBP01338; WBGene00027753; Cbr-asp-4.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; A8WZH3; -.
DR OMA; IGELWIL; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.60.40.1960; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002729737"
FT DOMAIN 95..411
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 414..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 126..133
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 290..294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 333..370
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 446 AA; 49498 MW; 66686FE57E4730A5 CRC64;
MNRCIILLLG ALLLVQGLHI HKKQPKLRTI SLKKQPTLRE TLLQAGTFET FARHRHGYQK
KFLKHHGNHH FDKYNGVKPL GEIDELLRNY MDAQYFGTIS IGTPGQNFTV IFDTGSSNLW
VPSKKCPFYD IACMLHHRYD SKSSSTYKED GRKMAIQYGT GSMKGFISKD SVCVAGICAE
DQPFAEATSE PGITFVAAKF DGILGMAYPE IAVLGVQPVF NTLFEQKKVP SNVFSFWLNR
NPDSELGGEI TFGGIDARRY VEPITYTPVT RKGYWQFKMD KVVGSGVLGC SNGCQAIADT
GTSLIAGPKA QIEAIQNFIG AEPLIKGEYM ISCDKVPTLP PVSFVIGGQE FSLKGEDYVL
KVSQGGKTIC LSGFMGIDLP ERVGELWILG DVFIGRYYTV FDFDQNRVGF AQAKTADGHP
VDPAPRKYRS VFDDEESEES SEQDDQ
//
