| General information | | DisProt: | DP00484 | | Name: | Tricorn protease | | Synonym(s): | TRI_THEAC
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | P96086 | | UniGene: | | | SwissProt: | TRI_THEAC | | TrEMBL: | | | NCBI (GI): | 11387137 | | Source organism: | Thermoplasma acidophilum | | Sequence length: | 1071 | | Percent disordered: | 4% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MPSLMSFGSC QWIDQGRFSR SLYRNFKTFK LHEMHGLCMP NLLLNPDIHG DRIIFVCCDD - 60
LWEHDLKSGS TRKIVSNLGV INNARFFPDG RKIAIRVMRG SSLNTADLYF YNGENGEIKR - 120
ITYFSGKSTG RRMFTDVAGF DPDGNLIIST DAMQPFSSMT CLYRVENDGI NFVPLNLGPA - 180
THILFADGRR VIGRNTFELP HWKGYRGGTR GKIWIEVNSG AFKKIVDMST HVSSPVIVGH - 240
RIYFITDIDG FGQIYSTDLD GKDLRKHTSF TDYYPRHLNT DGRRILFSKG GSIYIFNPDT - 300
EKIEKIEIGD LESPEDRIIS IPSKFAEDFS PLDGDLIAFV SRGQAFIQDV SGTYVLKVPE - 360
PLRIRYVRRG GDTKVAFIHG TREGDFLGIY DYRTGKAEKF EENLGNVFAM GVDRNGKFAV - 420
VANDRFEIMT VDLETGKPTV IERSREAMIT DFTISDNSRF IAYGFPLKHG ETDGYVMQAI - 480
HVYDMEGRKI FAATTENSHD YAPAFDADSK NLYYLSYRSL DPSPDRVVLN FSFEVVSKPF - 540
VIPLIPGSPN PTKLVPRSMT SEAGEYDLND MYKRSSPINV DPGDYRMIIP LESSILIYSV - 600
PVHGEFAAYY QGAPEKGVLL KYDVKTRKVT EVKNNLTDLR LSADRKTVMV RKDDGKIYTF - 660
PLEKPEDERT VETDKRPLVS SIHEEFLQMY DEAWKLARDN YWNEAVAKEI SERIYEKYRN - 720
LVPLCKTRYD LSNVIVEMQG EYRTSHSYEM GGTFTDKDPF RSGRIACDFK LDGDHYVVAK - 780
AYAGDYSNEG EKSPIFEYGI DPTGYLIEDI DGETVGAGSN IYRVLSEKAG TSARIRLSGK - 840
GGDKRDLMID ILDDDRFIRY RSWVEANRRY VHERSKGTIG YIHIPDMGMM GLNEFYRLFI - 900
NESSYQGLIV DVRFNGGGFV SQLIIEKLMN KRIGYDNPRR GTLSPYPTNS VRGKIIAITN - 960
EYAGSDGDIF SFSFKKLGLG KLIGTRTWGG VVGITPKRRL IDGTVLTQPE FAFWFRDAGF - 1020
GVENYGVDPD VEIEYAPHDY LSGKDPQIDY AIDALIEELR NWNEELPQRP S
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| Functional narrative |
Tricorn degrades oligopeptides (probably derived from the proteasome) and channels the products to F1, F2 and F3 proteases, which then catalyze the terminal degradation step, yielding free amino acids.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | N-terminal | | Location: | 1 - 38 | | Length: | 38 | | Region sequence: |
MPSLMSFGSCQWIDQGRFSRSLYRNFKTFKLHEMHGLC | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (293 K; pH: 6; isopropranol 2-morpholinoethanesulphonic acid (MES) (25-30%))
| References:
- Brandstetter H, Kim JS, Groll M, Huber R. "Crystal structure of the tricorn protease reveals a protein disassembly line." Nature. 2001; 414(6862): 466-70. PubMed: 11719810
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | C-terminal | | Location: | 1062 - 1071 | | Length: | 10 | | Region sequence: |
WNEELPQRPS | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (293 K; pH: 6; isopropranol 2-morpholinoethanesulphonic acid (MES) (25-30%))
| References:
- Brandstetter H, Kim JS, Groll M, Huber R. "Crystal structure of the tricorn protease reveals a protein disassembly line." Nature. 2001; 414(6862): 466-70. PubMed: 11719810
| Comments:
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| References |
- Tamura T, Tamura N, Cejka Z, Hegerl R, Lottspeich F, Baumeister W. "Tricorn protease--the core of a modular proteolytic system." Science. 1996; 274(5291): 1385-9. PubMed: 8910281
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