ID W5J5H8_ANODA Unreviewed; 493 AA.
AC W5J5H8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Peroxisomal leader peptide-processing protease {ECO:0000256|PIRNR:PIRNR037989};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR037989};
GN ORFNames=AND_010305 {ECO:0000313|EMBL:ETN58120.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN58120.1};
RN [1] {ECO:0000313|EMBL:ETN58120.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN58120.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN58120.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC010305-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Peroxisomal protease that mediates both the removal of the
CC leader peptide from proteins containing a PTS2 target sequence and
CC processes several PTS1-containing proteins. Catalyzes the processing of
CC PTS1-proteins involved in the peroxisomal beta-oxidation of fatty
CC acids. {ECO:0000256|PIRNR:PIRNR037989}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|PIRNR:PIRNR037989}.
CC -!- PTM: The full-lengh TYSND1 is the active the proteolytic processing of
CC PTS1- and PTS2-proteins and in self-cleavage, and intermolecular self-
CC cleavage of TYSND1 down-regulates its protease activity.
CC {ECO:0000256|PIRNR:PIRNR037989}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|PIRNR:PIRNR037989}.
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DR EMBL; ADMH02002165; ETN58120.1; -; Genomic_DNA.
DR AlphaFoldDB; W5J5H8; -.
DR STRING; 43151.W5J5H8; -.
DR EnsemblMetazoa; ADAC010305-RA; ADAC010305-PA; ADAC010305.
DR VEuPathDB; VectorBase:ADAC010305; -.
DR VEuPathDB; VectorBase:ADAR2_010104; -.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_535608_0_0_1; -.
DR OMA; GGPMFDQ; -.
DR OrthoDB; 3487426at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR039245; TYSND1/DEG15.
DR PANTHER; PTHR21004:SF0; PEROXISOMAL LEADER PEPTIDE-PROCESSING PROTEASE; 1.
DR PANTHER; PTHR21004; SERINE PROTEASE-RELATED; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037989};
KW Peroxisome {ECO:0000256|PIRNR:PIRNR037989};
KW Protease {ECO:0000256|PIRNR:PIRNR037989};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Serine protease {ECO:0000256|PIRNR:PIRNR037989}.
SQ SEQUENCE 493 AA; 54527 MW; 8F9F1E974D50D302 CRC64;
MRIPGFPNHG TVFYTSGGHK TSAVFLGEEF VITSALIFSD NVEYAKTIAD AVLQTPLVEI
SKTQRLQNLY QLDFRIVRKN GNDLQERRAR ACHIVHSRRA KACLENLLNG LQVCLDGEAK
PMQDYSALYS SFLILTTSSS RVPPWRSVSA LLKQVTGRND VSLKLLDKVV AISTPFGNES
FFNTVNVGHV CNILDDEGCV LLLDVPLNPG SEGGALYDQS MKLRGFFIGS SYKYRGDIVI
LPLAISVDEI LSIGCSERNL CQRVPHSFPL EAFRSVCMID SQGCWGTGCA FELKGKRYII
SCAHVLSTDN VTCFFGDQKV MHPRVLYKNP VFDSAYDVAL MEASYDEAQP SGWFCRLANY
IPAVGQRIYS VGFPVFKSLA SKLTFKPSII PGRVTKYTEG ILFTDCSIQY GQSGGPIFDE
NGLLVAIAVS NFKSSLDNRI YPFHNMCIPV QGIHATLAQY ADTGDKSSLA ALQADWDVRS
SWKLKPPKIL NKL
//
