GenomeNet

Database: UniProt
Entry: A0A5N5N650_PANHP
LinkDB: A0A5N5N650_PANHP
Original site: A0A5N5N650_PANHP 
ID   A0A5N5N650_PANHP        Unreviewed;       330 AA.
AC   A0A5N5N650;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE            EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
GN   ORFNames=PHYPO_G00019090 {ECO:0000313|EMBL:KAB5562548.1};
OS   Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Pangasiidae; Pangasianodon.
OX   NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5562548.1, ECO:0000313|Proteomes:UP000327468};
RN   [1] {ECO:0000313|EMBL:KAB5562548.1, ECO:0000313|Proteomes:UP000327468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indonesia {ECO:0000313|EMBL:KAB5562548.1,
RC   ECO:0000313|Proteomes:UP000327468};
RC   TISSUE=Blood {ECO:0000313|EMBL:KAB5562548.1};
RA   Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA   Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA   Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA   Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA   Schartl M., Guiguen Y.;
RT   "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT   hypophthalmus.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB5562548.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; VFJC01000011; KAB5562548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5N650; -.
DR   OrthoDB; 808912at2759; -.
DR   Proteomes; UP000327468; Chromosome 10.
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:UP000327468};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..330
FT                   /note="Cathepsin B"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5024306483"
FT   DOMAIN          79..328
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   330 AA;  36362 MW;  D488DC58294B8C1D CRC64;
     MRCLSLLYLA SALAVCWARP HLHPLSHEMV NYINKFNSTW TAGLNFGNVD YSYVKQLCGT
     RLKGPKLPVM VQYAGDVKLP ANFDPREQWP NCPTLKEIRD QGSCGSCWAF GAAEAISDRI
     CIHSNGKVSV EISSEDLLTC CSDCGEGCNG GYPSAAWEFW TNQGLVTGGL YNSHIGCRPY
     TIEPCEHHIN GSRPPCTGEG GDTPNCEEKC EPGYSLSYMQ DKHFGKQAYR VASDEKQIMQ
     ELYSNGPVEG AFTVYEDFLL YKSGVYKHIT GGVLGGHAIK ILGWGEENGT PYWLAANSWN
     TDWGDNGYFK ILRGVDHCGI ESEIVAGIPK
//
DBGET integrated database retrieval system