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Database: UniProt
Entry: H2TG06_TAKRU
LinkDB: H2TG06_TAKRU
Original site: H2TG06_TAKRU 
ID   H2TG06_TAKRU            Unreviewed;       334 AA.
AC   H2TG06;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE            EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
GN   Name=LOC101076659 {ECO:0000313|Ensembl:ENSTRUP00000023604.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000023604.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000023604.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000023604.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule
CC         substrates (thus differing from cathepsin L). In addition to being an
CC         endopeptidase, shows peptidyl-dipeptidase activity, liberating C-
CC         terminal dipeptides.; EC=3.4.22.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001754};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   AlphaFoldDB; H2TG06; -.
DR   STRING; 31033.ENSTRUP00000066275; -.
DR   MEROPS; C01.060; -.
DR   Ensembl; ENSTRUT00000023702.3; ENSTRUP00000023604.3; ENSTRUG00000009391.3.
DR   eggNOG; KOG1543; Eukaryota.
DR   GeneTree; ENSGT00940000158680; -.
DR   HOGENOM; CLU_012184_3_3_1; -.
DR   TreeFam; TF314576; -.
DR   Proteomes; UP000005226; Chromosome 13.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02620; Peptidase_C1A_CathepsinB; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR012599; Propeptide_C1A.
DR   PANTHER; PTHR12411:SF895; CATHEPSIN B; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   Pfam; PF08127; Propeptide_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..334
FT                   /note="Cathepsin B"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025479444"
FT   DOMAIN          83..332
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   334 AA;  36757 MW;  5EBE80291659E921 CRC64;
     TTSLILLAAF LIVVTSFSSS LARPNLKPLS IEMVNYINKL NTTWMAGRNF HNIEYSYIQK
     LCGTLLKGPK LPIMIQYAGG FKLPRQFDSR EQWPNCPTLK EIRDQGSCGS CWAFGASEAM
     SDRICIHSNA KISVELSAED LLSCCESCGM GCNGGYPSAA WDFWTKDGLV SGGLYDSHIG
     CRPYTIPPCE HHVNGSRPSC SGEGGETPQC VYRCEAGYTP SYKQDKHYGK TSYSVSSDED
     DIKHEIYKNG PVEGAFTVYE DFVLYKTGVY QHVTGSALGG HAIKILGWGE ENGIPYWLCA
     NSWNTDWGNN GFFKILRGSN HCGIESEIVA GIPN
//
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