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P00761

- TRYP_PIG

UniProt

P00761 - TRYP_PIG

Protein

Trypsin

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei48 – 481Charge relay system
    Metal bindingi60 – 601Calcium
    Metal bindingi62 – 621Calcium; via carbonyl oxygen
    Metal bindingi65 – 651Calcium; via carbonyl oxygen
    Metal bindingi70 – 701Calcium
    Active sitei92 – 921Charge relay system
    Sitei179 – 1791Required for specificityBy similarity
    Active sitei185 – 1851Charge relay system

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Digestion

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin (EC:3.4.21.4)
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 88Activation peptide1 PublicationPRO_0000028205
    Chaini9 – 231223TrypsinPRO_0000028206Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi15 ↔ 145
    Disulfide bondi33 ↔ 49
    Disulfide bondi117 ↔ 218
    Disulfide bondi124 ↔ 191
    Disulfide bondi156 ↔ 170
    Disulfide bondi181 ↔ 205

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP00761.
    PRIDEiP00761.

    Expressioni

    Gene expression databases

    ArrayExpressiP00761.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-6083N.
    IntActiP00761. 1 interaction.
    MINTiMINT-1512991.
    STRINGi9823.ENSSSCP00000017465.

    Structurei

    Secondary structure

    1
    231
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 3917
    Beta strandi42 – 454
    Helixi47 – 493
    Beta strandi55 – 595
    Beta strandi61 – 655
    Beta strandi71 – 8010
    Turni86 – 883
    Beta strandi94 – 1007
    Beta strandi105 – 1084
    Beta strandi123 – 1308
    Beta strandi134 – 1363
    Beta strandi144 – 1507
    Helixi153 – 1597
    Turni161 – 1633
    Beta strandi168 – 1725
    Beta strandi174 – 1774
    Turni182 – 1865
    Beta strandi188 – 1914
    Beta strandi194 – 2018
    Beta strandi203 – 2064
    Beta strandi212 – 2165
    Helixi217 – 2193
    Helixi221 – 23010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AKSX-ray1.80A9-133[»]
    B134-231[»]
    1AN1X-ray2.03E9-231[»]
    1AVWX-ray1.75A9-231[»]
    1AVXX-ray1.90A9-231[»]
    1C9PX-ray2.80A9-231[»]
    1D3Omodel-A9-231[»]
    1DF2model-A9-231[»]
    1EJAX-ray2.70A9-231[»]
    1EPTX-ray1.80A9-51[»]
    B52-133[»]
    C134-231[»]
    1EWUmodel-A9-231[»]
    1FMGX-ray1.90A9-231[»]
    1FN6X-ray1.80A9-231[»]
    1FNIX-ray1.60A9-231[»]
    1H9HX-ray1.50E9-231[»]
    1H9IX-ray1.90E9-231[»]
    1LDTX-ray1.90T9-231[»]
    1LT2model-A9-231[»]
    1MCTX-ray1.60A9-231[»]
    1QQUX-ray1.63A9-231[»]
    1S5SX-ray1.40A9-231[»]
    1S6FX-ray1.80A9-231[»]
    1S6HX-ray1.45A9-231[»]
    1S81X-ray1.70A9-231[»]
    1S82X-ray1.85A9-231[»]
    1S83X-ray1.25A9-231[»]
    1S84X-ray1.85A9-231[»]
    1S85X-ray2.20A9-231[»]
    1TFXX-ray2.60A/B9-231[»]
    1TX6X-ray2.20A/B/C/D9-231[»]
    1UHBX-ray2.15A9-133[»]
    B134-231[»]
    P177-185[»]
    1V6DX-ray1.90A9-231[»]
    1YF4X-ray1.98A9-231[»]
    1Z7KX-ray1.90A9-231[»]
    2A31X-ray1.25A9-231[»]
    2A32X-ray1.50A9-231[»]
    3MYWX-ray2.50A/B9-231[»]
    4AN7X-ray2.23A1-231[»]
    4DOQX-ray2.00A/C/E9-231[»]
    ProteinModelPortaliP00761.
    SMRiP00761. Positions 9-231.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00761.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 229221Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00761-1 [UniParc]FASTAAdd to Basket

    « Hide

    FPTDDDDKIV GGYTCAANSI PYQVSLNSGS HFCGGSLINS QWVVSAAHCY    50
    KSRIQVRLGE HNIDVLEGNE QFINAAKIIT HPNFNGNTLD NDIMLIKLSS 100
    PATLNSRVAT VSLPRSCAAA GTECLISGWG NTKSSGSSYP SLLQCLKAPV 150
    LSDSSCKSSY PGQITGNMIC VGFLEGGKDS CQGDSGGPVV CNGQLQGIVS 200
    WGYGCAQKNK PGVYTKVCNY VNWIQQTIAA N 231
    Length:231
    Mass (Da):24,409
    Last modified:July 21, 1986 - v1
    Checksum:iA0A125CF7FC138C2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201I → V.

    Sequence databases

    PIRiA90641. TRPGTR.

    Cross-referencesi

    Sequence databases

    PIRi A90641. TRPGTR.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AKS X-ray 1.80 A 9-133 [» ]
    B 134-231 [» ]
    1AN1 X-ray 2.03 E 9-231 [» ]
    1AVW X-ray 1.75 A 9-231 [» ]
    1AVX X-ray 1.90 A 9-231 [» ]
    1C9P X-ray 2.80 A 9-231 [» ]
    1D3O model - A 9-231 [» ]
    1DF2 model - A 9-231 [» ]
    1EJA X-ray 2.70 A 9-231 [» ]
    1EPT X-ray 1.80 A 9-51 [» ]
    B 52-133 [» ]
    C 134-231 [» ]
    1EWU model - A 9-231 [» ]
    1FMG X-ray 1.90 A 9-231 [» ]
    1FN6 X-ray 1.80 A 9-231 [» ]
    1FNI X-ray 1.60 A 9-231 [» ]
    1H9H X-ray 1.50 E 9-231 [» ]
    1H9I X-ray 1.90 E 9-231 [» ]
    1LDT X-ray 1.90 T 9-231 [» ]
    1LT2 model - A 9-231 [» ]
    1MCT X-ray 1.60 A 9-231 [» ]
    1QQU X-ray 1.63 A 9-231 [» ]
    1S5S X-ray 1.40 A 9-231 [» ]
    1S6F X-ray 1.80 A 9-231 [» ]
    1S6H X-ray 1.45 A 9-231 [» ]
    1S81 X-ray 1.70 A 9-231 [» ]
    1S82 X-ray 1.85 A 9-231 [» ]
    1S83 X-ray 1.25 A 9-231 [» ]
    1S84 X-ray 1.85 A 9-231 [» ]
    1S85 X-ray 2.20 A 9-231 [» ]
    1TFX X-ray 2.60 A/B 9-231 [» ]
    1TX6 X-ray 2.20 A/B/C/D 9-231 [» ]
    1UHB X-ray 2.15 A 9-133 [» ]
    B 134-231 [» ]
    P 177-185 [» ]
    1V6D X-ray 1.90 A 9-231 [» ]
    1YF4 X-ray 1.98 A 9-231 [» ]
    1Z7K X-ray 1.90 A 9-231 [» ]
    2A31 X-ray 1.25 A 9-231 [» ]
    2A32 X-ray 1.50 A 9-231 [» ]
    3MYW X-ray 2.50 A/B 9-231 [» ]
    4AN7 X-ray 2.23 A 1-231 [» ]
    4DOQ X-ray 2.00 A/C/E 9-231 [» ]
    ProteinModelPortali P00761.
    SMRi P00761. Positions 9-231.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6083N.
    IntActi P00761. 1 interaction.
    MINTi MINT-1512991.
    STRINGi 9823.ENSSSCP00000017465.

    Chemistry

    BindingDBi P00761.
    ChEMBLi CHEMBL2366.

    Proteomic databases

    PaxDbi P00761.
    PRIDEi P00761.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.

    Miscellaneous databases

    EvolutionaryTracei P00761.

    Gene expression databases

    ArrayExpressi P00761.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: PROTEIN SEQUENCE OF 1-10.
    2. "Determination of the amino acid sequence of porcine trypsin by sequenator analysis."
      Hermodson M.A., Ericsson L.H., Neurath H., Walsh K.A.
      Biochemistry 12:3146-3153(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 9-231.
    3. "Refined 1.6-A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex."
      Huang Q., Liu S., Tang Y.
      J. Mol. Biol. 229:1022-1036(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    4. "Amino acid sequencing of a trypsin inhibitor by refined 1.6 A X-ray crystal structure of its complex with porcine beta-trypsin."
      Huang Q., Liu S., Tang Y., Zeng F., Qian R.
      FEBS Lett. 297:143-146(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    5. "Refined 1.8-A resolution crystal structure of the porcine epsilon-trypsin."
      Huang Q., Wang Z., Li Y., Liu S., Tang Y.
      Biochim. Biophys. Acta 1209:77-82(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    6. "The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition."
      Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R., Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.
      J. Biol. Chem. 272:19931-19937(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH LDTI.
    7. "Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system."
      di Marco S., Priestle J.P.
      Structure 5:1465-1474(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF COMPLEX WITH LDTI.
    8. "L-isoaspartate 115 of porcine beta-trypsin promotes crystallization of its complex with bdellastasin."
      Rester U., Moser M., Huber R., Bode W.
      Acta Crystallogr. D 56:581-588(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH BDELLASTASIN.

    Entry informationi

    Entry nameiTRYP_PIG
    AccessioniPrimary (citable) accession number: P00761
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3