ID A0A2U4BES6_TURTR Unreviewed; 568 AA.
AC A0A2U4BES6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peroxisomal leader peptide-processing protease {ECO:0000256|PIRNR:PIRNR037989};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR037989};
GN Name=TYSND1 {ECO:0000313|RefSeq:XP_019791712.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019791712.1};
RN [1] {ECO:0000313|RefSeq:XP_019791712.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019791712.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_019791712.1; XM_019936153.2.
DR AlphaFoldDB; A0A2U4BES6; -.
DR STRING; 9739.ENSTTRP00000006280; -.
DR GeneID; 101316514; -.
DR InParanoid; A0A2U4BES6; -.
DR OrthoDB; 7519at2759; -.
DR Proteomes; UP000245320; Chromosome 16.
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; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037989};
KW Peroxisome {ECO:0000256|PIRNR:PIRNR037989};
KW Protease {ECO:0000256|PIRNR:PIRNR037989,
KW ECO:0000313|RefSeq:XP_019791712.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Serine protease {ECO:0000256|PIRNR:PIRNR037989}.
SQ SEQUENCE 568 AA; 59038 MW; C891E98B033F8E94 CRC64;
MGRQWGPAMR AAEQAGCVVS ATRAGQPEAG SWSCSGVILS RRLGLVLCHG GIFTPFLRAG
SGALTAAGAV FLPGDSCGDD LRLHVQWGPT AASPAGRAER GRPGLCTPQC AGLEPGPPAR
FRGRPLQPPR PAELLLLLSC PAFRGHFARL FGGEAAKQWS FASAAPDDEV SEEEEEDQLR
ALGWFALLRV RPDPEKEAEA EERGPVLAVA PLGAVPKGEP LVACGSPFGA FCPDIFLNTL
SCGVLSNSAG PLLLTDARCL PGTEGGGVFE ARPAGALVAL VAAPLCWKAR EWVGLTLLCA
AAPLLCAARA ALCRLHPGAA ALAAFLPHEM GSPWGLPLRD PGPPWAAAAV LVECGSVWGS
GVAVAPRLVV TCRHVAPREA AKVLVRSTTP KSAVIWGHVV FATQETSPYD IAVVSLEEDL
DGVPVPVPAE HFHEGEAVSV VGFGVFGQAC GPSVTSGILS AVVQVDDTPV MLQTTCAVHG
GSSGGPLFST CSGDLLGIIA SNTRDNNTGA TYPHLNFSIP ITVLQPALQR YSQAGDLGGL
RQLDRAPEPV RVVWRLQRPL AEAPRSKL
//
