ID A0A158NKX4_ATTCE Unreviewed; 504 AA.
AC A0A158NKX4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Peroxisomal leader peptide-processing protease {ECO:0000256|PIRNR:PIRNR037989};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR037989};
GN Name=105621327 {ECO:0000313|EnsemblMetazoa:XP_012058182.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012058182.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012058182.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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; ADTU01018997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012058182.1; XM_012202792.1.
DR AlphaFoldDB; A0A158NKX4; -.
DR STRING; 12957.A0A158NKX4; -.
DR EnsemblMetazoa; XM_012202792.1; XP_012058182.1; LOC105621327.
DR GeneID; 105621327; -.
DR KEGG; acep:105621327; -.
DR eggNOG; KOG1320; Eukaryota.
DR InParanoid; A0A158NKX4; -.
DR OrthoDB; 7519at2759; -.
DR Proteomes; UP000005205; 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; 2.40.10.10; Trypsin-like serine proteases; 2.
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; 1.
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:UP000005205};
KW Serine protease {ECO:0000256|PIRNR:PIRNR037989}.
SQ SEQUENCE 504 AA; 55352 MW; 55E461D10728BB61 CRC64;
MDVPSSALLL HSSIDKDPLP QGCSGISIST DWILTHGIVL DPIIDKSYAV SNFVTNMVSG
ELITVPRELM SELKFRVYRD LGNDNDSRSS PLKEHHGMIV AAWQCPLLKK TFDEFFKTWS
FSKSSEFTRS LRSIFLFVRI YNSESIVETS LEQALSCLLN QIPRNLIRGS SVIIESTPFG
NPVFAGSIAH GVISNVVGDE GCVIMTDAYA FPGGEGGPVY IILPDSKHRI ISGMVIAPLS
WCRGEWVDYT FAANLMPCVL NILRKKNLPC RPITYQENID VALDRGVVLV RCGINWGTGV
LVHKDTGTFL TCSHVVAEAS EREISIIMRP DKTNSCIRAK LLYRTPENQP YDIAVLRMDP
QDVDPSLKSV RLSHTAILNK GEPVVSIGFP FSSSIRPTIS SGVVSKSMDC ALLTTCCVQS
GTSGGPIINR TTGDMLGMVV CNVLSSDGTT LYPRMSLAVP ATILSGPLRE YLRTDNPNVL
RAFTCDDAIV CKIWDFYPFL PAKL
//
