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Database: UniProt
Entry: F6TJX5_HORSE
LinkDB: F6TJX5_HORSE
Original site: F6TJX5_HORSE 
ID   F6TJX5_HORSE            Unreviewed;       588 AA.
AC   F6TJX5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 4.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Tripeptidyl peptidase 1 {ECO:0000313|Ensembl:ENSECAP00000006230.4};
GN   Name=TPP1 {ECO:0000313|Ensembl:ENSECAP00000006230.4,
GN   ECO:0000313|VGNC:VGNC:24438};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000006230.4, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000006230.4, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000006230.4,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000006230.4}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000006230.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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DR   AlphaFoldDB; F6TJX5; -.
DR   STRING; 9796.ENSECAP00000006230; -.
DR   PaxDb; 9796-ENSECAP00000006230; -.
DR   Ensembl; ENSECAT00000008332.4; ENSECAP00000006230.4; ENSECAG00000007829.4.
DR   VGNC; VGNC:24438; TPP1.
DR   GeneTree; ENSGT00390000008684; -.
DR   HOGENOM; CLU_013783_5_1_1; -.
DR   InParanoid; F6TJX5; -.
DR   OMA; YARSVCN; -.
DR   TreeFam; TF333497; -.
DR   Proteomes; UP000002281; Chromosome 7.
DR   Bgee; ENSECAG00000007829; Expressed in adult mammalian kidney and 23 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0035727; F:lysophosphatidic acid binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0120146; F:sulfatide binding; IEA:Ensembl.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:1905146; P:lysosomal protein catabolic process; IEA:Ensembl.
DR   GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:Ensembl.
DR   GO; GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F6TJX5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN          220..588
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        293
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        297
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        500
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         542
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         543
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         566
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         568
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   588 AA;  63849 MW;  4363A52DE74D9D08 CRC64;
     MVLECRAHVI RHMTADLQKG GMGLRACLLG LLALFVTGKC SYSPEPDQLR TLPPGWVSLG
     RVDPEEELSL TFALRQQNLE RLSKLVQAVS DPSSPRYGKY LTLEDVAELV RPSPLTLSTV
     QKWLLAAGAR NCHSVTTQDF LTCWLSVRQA ELLLSGAEFH LYVGGPTETH VVRSPRPYQL
     PKALASHVDF VGGLHRFPPT SSLRQRPEPQ VAGTVGLHLG VTPSVIRERY NLTAQDVGSG
     TTNNSQACAQ FLEQYFRDSD LAEFMRLFGG NFAHQASVAR VVGQQGRGLA GIEASLDVQY
     LMSAGANIST WVYSNPGRHE SQEPFLQWLL LLSNESALPH VHTVSYGDDE DSLSSAYIQR
     VNTEFMKAAA RGLTLLFASV SLPGDSGAGC WSVSGRHQFR PSFPASSPYV TTVGGTSFQN
     PFRVTNEVVD YISGGGFSNV FPQPSYQEDA VAHFLSSSPN LPPSSYFNAS GRAYPDVAAL
     SDGYWVVSNN VPIPWVSGTS ASTPVFGGLL SLINEHRILS GHPPLGFLNP RLYQQRGAGL
     FDVTRGCHES CLNEEVQGQG FCSGPGWDPV TGWGTPNFPA LLKTLINP
//
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